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Conserved domains on  [gi|488216789|ref|WP_002287997|]
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MULTISPECIES: multiple monosaccharide ABC transporter substrate-binding protein [Enterococcus]

Protein Classification

sugar-binding protein( domain architecture ID 14448371)

sugar-binding protein is a type 1 periplasmic binding protein, similar to Agrobacterium fabrum multiple sugar-binding periplasmic receptor ChvE that binds diverse plant sugars as virulence signals

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ChvE super family cl46169
sugar ABC transporter substrate-binding protein;
37-355 0e+00

sugar ABC transporter substrate-binding protein;


The actual alignment was detected with superfamily member NF040907:

Pssm-ID: 468842  Cd Length: 319  Bit Score: 619.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:NF040907   1 VGIAMPTKSSERWIADGNNMVKQLEAAGYKTDLQYAEDDVPTQVSQIENMITKGAKVLVIAAIDGTALTDVLQQAADAGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSENVDYYATFDNFGVGVSQAAYIEEHLGLKEGKGPFTIELFGGSPDDNNALINYNGVMSVLQPYMDNGQ 196
Cdd:NF040907  81 PVIAYDRLIRGSENVDYYATFDNFKVGVLQGTYIVDGLGLKDGKGPFNIELFAGSPDDNNAYFFFDGAMSVLQPYIDSGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LVVPSGQTSFSQIATLRWDGSTAQARMDNLLSANYTDQTLDAVLSPYDPISLGIISSLKGVGYGSESKPLPVITGQDATV 276
Cdd:NF040907 161 LVVRSGQTDFDQVATLRWDGATAQARMDNLLSAFYTDKKVDAVLSPYDGISIGIISALKGVGYGSGDKPLPVVTGQDAEV 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488216789 277 AGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNDTETYDNGVKTVPTYLANTVSVDKDNYQAELIDTDYY 355
Cdd:NF040907 241 ASVKSIIAGEQTSTIFKDTRELAKVTVKMVDAVLKGEEPEVNDTKTYDNGVKVVPSYLLEPVSVDKDNYKEVLVDSGYY 319
 
Name Accession Description Interval E-value
ChvE NF040907
sugar ABC transporter substrate-binding protein;
37-355 0e+00

sugar ABC transporter substrate-binding protein;


Pssm-ID: 468842  Cd Length: 319  Bit Score: 619.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:NF040907   1 VGIAMPTKSSERWIADGNNMVKQLEAAGYKTDLQYAEDDVPTQVSQIENMITKGAKVLVIAAIDGTALTDVLQQAADAGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSENVDYYATFDNFGVGVSQAAYIEEHLGLKEGKGPFTIELFGGSPDDNNALINYNGVMSVLQPYMDNGQ 196
Cdd:NF040907  81 PVIAYDRLIRGSENVDYYATFDNFKVGVLQGTYIVDGLGLKDGKGPFNIELFAGSPDDNNAYFFFDGAMSVLQPYIDSGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LVVPSGQTSFSQIATLRWDGSTAQARMDNLLSANYTDQTLDAVLSPYDPISLGIISSLKGVGYGSESKPLPVITGQDATV 276
Cdd:NF040907 161 LVVRSGQTDFDQVATLRWDGATAQARMDNLLSAFYTDKKVDAVLSPYDGISIGIISALKGVGYGSGDKPLPVVTGQDAEV 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488216789 277 AGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNDTETYDNGVKTVPTYLANTVSVDKDNYQAELIDTDYY 355
Cdd:NF040907 241 ASVKSIIAGEQTSTIFKDTRELAKVTVKMVDAVLKGEEPEVNDTKTYDNGVKVVPSYLLEPVSVDKDNYKEVLVDSGYY 319
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
 37-340 5.89e-163

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: 457.86  E-value: 5.89e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd19994    2 IGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSENVDYYATFDNFGVGVSQAAYIEEHLGLKEGKGPFTIELFGGSPDDNNALINYNGVMSVLQPYMDNGQ 196
Cdd:cd19994   82 PVIAYDRLIMNTDAVDYYVTFDNEKVGELQGQYLVDKLGLKDGKGPFNIELFAGSPDDNNAQLFFKGAMEVLQPYIDDGT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LVVPSGQTSFSQIATLRWDGSTAQARMDNLLSANYT-DQTLDAVLSPYDPISLGIISSLKGVGYGseSKPLPVITGQDAT 275
Cdd:cd19994  162 LVVRSGQTTFEQVATPDWDTETAQARMETLLSAYYTgGKKLDAVLSPNDGIARGVIEALKAAGYD--TGPWPVVTGQDAE 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488216789 276 VAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNDTETYDNGVKTVPTYLANTVSV 340
Cdd:cd19994  240 DASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVEVNDTKTYDNGVKVVPSYLLDPVIV 304
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
 33-360 5.07e-160

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 450.36  E-value: 5.07e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  33 STGYVGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAK 112
Cdd:COG4213    1 GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 113 EADIKVIAYDRLLMNSeNVDYYATFDNFGVGVSQAAYIEEHLGLKeGKGPftIELFGGSPDDNNALINYNGVMSVLQPYM 192
Cdd:COG4213   81 AAGIPVIAYDRLILNS-DVDYYVSFDNVKVGELQGQYLVDGLPLK-GKGN--IELFGGSPTDNNATLFFEGAMSVLQPYI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 193 DNGQLVVPSGQTsfsqiaTLRWDGSTAQARMDNLLSANytDQTLDAVLSPYDPISLGIISSLKGVGYGseskPLPVITGQ 272
Cdd:COG4213  157 DSGKLVVVSGQW------TLGWDPETAQKRMENLLTAN--GNKVDAVLAPNDGLAGGIIQALKAQGLA----GKVVVTGQ 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 273 DATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNdtETYDNGVKTVPTYLANTVSVDKDNYQAELIDT 352
Cdd:COG4213  225 DAELAAVQRILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPEVN--GTYDNGKKDVPSYLLEPVAVTKDNVKETLIDS 302


                 ....*...
gi 488216789 353 DYYKESDL 360
Cdd:COG4213  303 GYYTAEQV 310
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
13-360 5.27e-62

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 201.51  E-value: 5.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  13 AILTASILLSACGNSGSADDSTgyVGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVD 92
Cdd:PRK10355   6 ILLTLCASLLLTSVAAHAKEVK--IGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQMSQIENMINRGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  93 TLVIASIDGSALTDVLAKAKEADIKVIAYDRLLmNSENVDYYATFDNFGVGVSQAAYIEEhlglKEGKGPFTieLFGGSP 172
Cdd:PRK10355  84 VLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMI-NNADIDFYISFDNEKVGELQAKALVD----KVPQGNYF--LMGGSP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 173 DDNNALINYNGVMSVLQPYMDNGQLVVPSGQTSFSqiatlrWDGSTAQARMDNLLSANytDQTLDAVLSPYDPISLGIIS 252
Cdd:PRK10355 157 VDNNAKLFRAGQMKVLKPYIDSGKIKVVGDQWVDG------WLPENALKIMENALTAN--NNKIDAVVASNDATAGGAIQ 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 253 SLKGVGYGSESkplpVITGQDATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNdtETYDNGVKTVPT 332
Cdd:PRK10355 229 ALSAQGLSGKV----AISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKAN--TTLNNGLKDVPS 302

                        330       340
                 ....*....|....*....|....*...
gi 488216789 333 YLANTVSVDKDNYQAELIDTDYYKESDL 360
Cdd:PRK10355 303 RLLTPIDVNKNNIDSTVIKDGFHKKSEL 330
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 37-314 4.59e-57

Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 186.36  E-value: 4.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789   37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQ-YGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEAD 115
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVgPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  116 IKVIAYDRlLMNSENVDYYATFDNFGVGVSQAAYIEEHLGlkeGKGpfTIELFGGSPDDNNALINYNGVMSVLQPYMDNG 195
Cdd:pfam13407  81 IPVVTFDS-DAPSSPRLAYVGFDNEAAGEAAGELLAEALG---GKG--KVAILSGSPGDPNANERIDGFKKVLKEKYPGI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  196 QLVvpsgqtsfSQIATLRWDGSTAQARMDNLLSANytDQTLDAVLSPYDPISLGIISSLKGVGYgsesKPLPVITGQDAT 275
Cdd:pfam13407 155 KVV--------AEVEGTNWDPEKAQQQMEALLTAY--PNPLDGIISPNDGMAGGAAQALEAAGL----AGKVVVTGFDAT 220

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 488216789  276 VAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEE 314
Cdd:pfam13407 221 PEALEAIKDGTIDATVLQDPYGQGYAAVELAAALLKGKK 259
 
Name Accession Description Interval E-value
ChvE NF040907
sugar ABC transporter substrate-binding protein;
37-355 0e+00

sugar ABC transporter substrate-binding protein;


Pssm-ID: 468842  Cd Length: 319  Bit Score: 619.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:NF040907   1 VGIAMPTKSSERWIADGNNMVKQLEAAGYKTDLQYAEDDVPTQVSQIENMITKGAKVLVIAAIDGTALTDVLQQAADAGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSENVDYYATFDNFGVGVSQAAYIEEHLGLKEGKGPFTIELFGGSPDDNNALINYNGVMSVLQPYMDNGQ 196
Cdd:NF040907  81 PVIAYDRLIRGSENVDYYATFDNFKVGVLQGTYIVDGLGLKDGKGPFNIELFAGSPDDNNAYFFFDGAMSVLQPYIDSGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LVVPSGQTSFSQIATLRWDGSTAQARMDNLLSANYTDQTLDAVLSPYDPISLGIISSLKGVGYGSESKPLPVITGQDATV 276
Cdd:NF040907 161 LVVRSGQTDFDQVATLRWDGATAQARMDNLLSAFYTDKKVDAVLSPYDGISIGIISALKGVGYGSGDKPLPVVTGQDAEV 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488216789 277 AGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNDTETYDNGVKTVPTYLANTVSVDKDNYQAELIDTDYY 355
Cdd:NF040907 241 ASVKSIIAGEQTSTIFKDTRELAKVTVKMVDAVLKGEEPEVNDTKTYDNGVKVVPSYLLEPVSVDKDNYKEVLVDSGYY 319
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
 37-340 5.89e-163

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: 457.86  E-value: 5.89e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd19994    2 IGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSENVDYYATFDNFGVGVSQAAYIEEHLGLKEGKGPFTIELFGGSPDDNNALINYNGVMSVLQPYMDNGQ 196
Cdd:cd19994   82 PVIAYDRLIMNTDAVDYYVTFDNEKVGELQGQYLVDKLGLKDGKGPFNIELFAGSPDDNNAQLFFKGAMEVLQPYIDDGT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LVVPSGQTSFSQIATLRWDGSTAQARMDNLLSANYT-DQTLDAVLSPYDPISLGIISSLKGVGYGseSKPLPVITGQDAT 275
Cdd:cd19994  162 LVVRSGQTTFEQVATPDWDTETAQARMETLLSAYYTgGKKLDAVLSPNDGIARGVIEALKAAGYD--TGPWPVVTGQDAE 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488216789 276 VAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNDTETYDNGVKTVPTYLANTVSV 340
Cdd:cd19994  240 DASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVEVNDTKTYDNGVKVVPSYLLDPVIV 304
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
 33-360 5.07e-160

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 450.36  E-value: 5.07e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  33 STGYVGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAK 112
Cdd:COG4213    1 GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 113 EADIKVIAYDRLLMNSeNVDYYATFDNFGVGVSQAAYIEEHLGLKeGKGPftIELFGGSPDDNNALINYNGVMSVLQPYM 192
Cdd:COG4213   81 AAGIPVIAYDRLILNS-DVDYYVSFDNVKVGELQGQYLVDGLPLK-GKGN--IELFGGSPTDNNATLFFEGAMSVLQPYI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 193 DNGQLVVPSGQTsfsqiaTLRWDGSTAQARMDNLLSANytDQTLDAVLSPYDPISLGIISSLKGVGYGseskPLPVITGQ 272
Cdd:COG4213  157 DSGKLVVVSGQW------TLGWDPETAQKRMENLLTAN--GNKVDAVLAPNDGLAGGIIQALKAQGLA----GKVVVTGQ 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 273 DATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNdtETYDNGVKTVPTYLANTVSVDKDNYQAELIDT 352
Cdd:COG4213  225 DAELAAVQRILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPEVN--GTYDNGKKDVPSYLLEPVAVTKDNVKETLIDS 302


                 ....*...
gi 488216789 353 DYYKESDL 360
Cdd:COG4213  303 GYYTAEQV 310
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
 37-334 6.95e-100

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: 297.03  E-value: 6.95e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd01538    2 IGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSEnVDYYATFDNFGVGVSQA-AYIEEhlglkegKGPFTIELFGGSPDDNNALINYNGVMSVLQPYMDNG 195
Cdd:cd01538   82 KVIAYDRLILNAD-VDYYISFDNEKVGELQAqALLDA-------KPEGNYVLIGGSPTDNNAKLFRDGQMKVLQPAIDSG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 196 QLVVPSGQtsfsqiATLRWDGSTAQARMDNLLSANYTDqtLDAVLSPYDPISLGIISSLKGVGYGseskPLPVITGQDAT 275
Cdd:cd01538  154 KIKVVGDQ------WVDDWLPANAQQIMENALTANGNN--VDAVVASNDGTAGGAIAALKAQGLS----GGVPVSGQDAD 221

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488216789 276 VAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNdtETYDNGVKTVPTYL 334
Cdd:cd01538  222 LAAIKRILAGTQTMTVYKDIRLLADAAAEVAVALMRGEKPPIN--GTTNNGLKDVPSYL 278
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
 37-340 1.76e-70

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: 221.73  E-value: 1.76e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd19991    2 IGFSMDSLRVERWQRDRDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSeNVDYYATFDNFGVGVSQAAYIEEHlglkEGKGPFTIelFGGSPDDNNALINYNGVMSVLQPYMDNGQ 196
Cdd:cd19991   82 PVLAYDRLILNA-DVDLYVSFDNEKVGELQAEALVKA----KPKGNYVL--LGGSPTDNNAKLFREGQMKVLQPLIDSGD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LvvpsgqTSFSQIATLRWDGSTAQARMDNLLSANytDQTLDAVLSPYDPISLGIISSLKgvGYGSESKplPVITGQDATV 276
Cdd:cd19991  155 I------KVVGDQWVDDWDPEEALKIMENALTAN--NNKIDAVIASNDGTAGGAIQALA--EQGLAGK--VAVSGQDADL 222

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488216789 277 AGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEevPVNDTETYDNGVKTVPTYLANTVSV 340
Cdd:cd19991  223 AACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGE--KNEANRTINNGKKEVPSILLDPIAV 284
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 37-334 3.19e-70

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: 221.30  E-value: 3.19e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd19992    2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSeNVDYYATFDNFGVGVSQAAYIEEHLglkeGKGPFTIelFGGSPDDNNALINYNGVMSVLQPYMDNGQ 196
Cdd:cd19992   82 PVISYDRLILNA-DVDLYVGRDNYKVGQLQAEYALEAV----PKGNYVI--LSGDPGDNNAQLITAGAMDVLQPAIDSGD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LVVPSGQtsfsqiATLRWDGSTAQARMDNLLSANYTDqtLDAVLSPYDPISLGIISSLKGVGygseskpLP---VITGQD 273
Cdd:cd19992  155 IKIVLDQ------YVKGWSPDEAMKLVENALTANNNN--IDAVLAPNDGMAGGAIQALKAQG-------LAgkvFVTGQD 219

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488216789 274 ATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNDtETYDNGVKTVPTYL 334
Cdd:cd19992  220 AELAALKRIVEGTQTMTVWKDLKELARAAADAAVKLAKGEKPQTTD-ETINNGGKDVPAIL 279
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
13-360 5.27e-62

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 201.51  E-value: 5.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  13 AILTASILLSACGNSGSADDSTgyVGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVD 92
Cdd:PRK10355   6 ILLTLCASLLLTSVAAHAKEVK--IGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQMSQIENMINRGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  93 TLVIASIDGSALTDVLAKAKEADIKVIAYDRLLmNSENVDYYATFDNFGVGVSQAAYIEEhlglKEGKGPFTieLFGGSP 172
Cdd:PRK10355  84 VLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMI-NNADIDFYISFDNEKVGELQAKALVD----KVPQGNYF--LMGGSP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 173 DDNNALINYNGVMSVLQPYMDNGQLVVPSGQTSFSqiatlrWDGSTAQARMDNLLSANytDQTLDAVLSPYDPISLGIIS 252
Cdd:PRK10355 157 VDNNAKLFRAGQMKVLKPYIDSGKIKVVGDQWVDG------WLPENALKIMENALTAN--NNKIDAVVASNDATAGGAIQ 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 253 SLKGVGYGSESkplpVITGQDATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNdtETYDNGVKTVPT 332
Cdd:PRK10355 229 ALSAQGLSGKV----AISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKAN--TTLNNGLKDVPS 302

                        330       340
                 ....*....|....*....|....*...
gi 488216789 333 YLANTVSVDKDNYQAELIDTDYYKESDL 360
Cdd:PRK10355 303 RLLTPIDVNKNNIDSTVIKDGFHKKSEL 330
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 37-339 2.07e-61

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: 198.67  E-value: 2.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIA-DGNNMVSELEKL--GYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKE 113
Cdd:cd19995    2 VAFLLPDTTSARWEQqDAPGFEKAMKKLcpDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 114 ADIKVIAYDRLLmNSENVDYYATFDNFGVGVSQAAYIEEHLGLKEGKGPfTIELFGGSPDDNNALINYNGVMSVLQPYMD 193
Cdd:cd19995   82 AGVPVIAYDRLI-LGGPADYYVSFDNVAVGEAQAQSLVDHLKAIGKKGV-NIVMINGSPTDNNAGLFKKGAHEVLDPLGD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 194 NGQLVVPSGQTsfsqiaTLRWDGSTAQARMDNLLSANYTDqtLDAVLSPYDPISLGIISSLKGVGYgsesKPLPVITGQD 273
Cdd:cd19995  160 SGELKLVCEYD------TPDWDPANAQTAMEQALTKLGNN--IDGVLSANDGLAGGAIAALKAQGL----AGKVPVTGQD 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488216789 274 ATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNDTE-TYDNGVKTVPTYLANTVS 339
Cdd:cd19995  228 ATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGETPPSDLVTgTVTNGGDKVPAVLLPPVV 294
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 37-314 4.59e-57

Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 186.36  E-value: 4.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789   37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQ-YGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEAD 115
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVgPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  116 IKVIAYDRlLMNSENVDYYATFDNFGVGVSQAAYIEEHLGlkeGKGpfTIELFGGSPDDNNALINYNGVMSVLQPYMDNG 195
Cdd:pfam13407  81 IPVVTFDS-DAPSSPRLAYVGFDNEAAGEAAGELLAEALG---GKG--KVAILSGSPGDPNANERIDGFKKVLKEKYPGI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  196 QLVvpsgqtsfSQIATLRWDGSTAQARMDNLLSANytDQTLDAVLSPYDPISLGIISSLKGVGYgsesKPLPVITGQDAT 275
Cdd:pfam13407 155 KVV--------AEVEGTNWDPEKAQQQMEALLTAY--PNPLDGIISPNDGMAGGAAQALEAAGL----AGKVVVTGFDAT 220

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 488216789  276 VAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEE 314
Cdd:pfam13407 221 PEALEAIKDGTIDATVLQDPYGQGYAAVELAAALLKGKK 259
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 37-334 7.31e-51

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: 171.12  E-value: 7.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd19993    2 VGVSWSNFQEERWKTDEAAMKKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSenVDYYATFDNFGVGVSQAAYIeehLGLKeGKGPFTieLFGGSPDDNNALINYNGVMSVLQPYMDNGQ 196
Cdd:cd19993   82 PVIAYDRLIENP--IAFYISFDNVEVGRMQARGV---LKAK-PEGNYV--FIKGSPTDPNADFLRAGQMEVLQPAIDSGK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LVVPSGQTsfsqiaTLRWDGSTAQARMDNLLSANytDQTLDAVLSPYDPISLGIISSLKGVGYGSEskpLPViTGQDATV 276
Cdd:cd19993  154 IKIVGEQY------TDGWKPANAQKNMEQILTAN--NNKVDAVVASNDGTAGGAVAALAAQGLAGK---VPV-SGQDADK 221

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488216789 277 AGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEV--PVNDTETYDNGVK-TVPTYL 334
Cdd:cd19993  222 AALNRIALGTQTVTVWKDARELGKEAAEIAVELAKGTKIeaIKGAALTNDGPKKvAVPSIF 282
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 37-316 2.92e-42

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: 148.10  E-value: 2.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd01536    2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSENVDYYATFDNFGVGVSQAAYIEEHLGlkeGKGpfTIELFGGSPDDNNALINYNGVMSVLQPYMDNgQ 196
Cdd:cd01536   82 PVVAVDTDIDGGGDVVAFVGTDNYEAGKLAGEYLAEALG---GKG--KVAILEGPPGSSTAIDRTKGFKEALKKYPDI-E 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LVvpsgqtsFSQIAtlRWDGSTAQARMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYGSEskplPVITGQDATV 276
Cdd:cd01536  156 IV-------AEQPA--NWDRAKALTVTENLLQAN---PDIDAVFAANDDMALGAAEALKAAGRTGD----IKIVGVDGTP 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 488216789 277 AGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVP 316
Cdd:cd01536  220 EALKAIKDGELDATVAQDPYLQGYLAVEAAVKLLNGEKVP 259
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 6-316 1.03e-41

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: 147.76  E-value: 1.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789   6 RKIVGTIAILTASILLSACGNSGS----ADDSTGYVGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVA 81
Cdd:COG1879    1 KRLALLAAVLALALALAACGSAAAeaaaAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  82 QIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLmNSENVDYYATFDNFGVGVSQAAYIEEHLGlkeGKG 161
Cdd:COG1879   81 QIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDV-DGSDRVAYVGSDNYAAGRLAAEYLAKALG---GKG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 162 pfTIELFGGSPDDNNALINYNGVMSVLQPYmdnGQLVVPSGQTSFsqiatlrWDGSTAQARMDNLLSANytdQTLDAVLS 241
Cdd:COG1879  157 --KVAILTGSPGAPAANERTDGFKEALKEY---PGIKVVAEQYAD-------WDREKALEVMEDLLQAH---PDIDGIFA 221

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488216789 242 PYDPISLGIISSLKGVGYgsesKPLPVITGQDATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVP 316
Cdd:COG1879  222 ANDGMALGAAQALKAAGR----KGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVP 292
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
 37-316 4.76e-30

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: 115.72  E-value: 4.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIAdgnnMVSELEKLGYKT---DLQY--GEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKA 111
Cdd:cd06308    2 IGFSQCSLNDPWRAA----MNEEIKAEAAKYpnvELIVtdAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 112 KEADIKVIAYDRLLmnseNVDYYATF---DNFGVGVSQAAYIEEHLGlkeGKGpfTIELFGGSPDDNNALINYNGVMSVL 188
Cdd:cd06308   78 YDAGIPVIVLDRKV----SGDDYTAFigaDNVEIGRQAGEYIAELLN---GKG--NVVEIQGLPGSSPAIDRHKGFLEAI 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 189 QPYMDNGQLVVPSGQtsfsqiatlrWDGSTAQARMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYGSEskplPV 268
Cdd:cd06308  149 AKYPGIKIVASQDGD----------WLRDKAIKVMEDLLQAH---PDIDAVYAHNDEMALGAYQALKKAGREKE----IK 211

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488216789 269 ITGQDA-TVAGVKSIIAGEQTQTIFKDTRilAKNTIEMIKAISDGEEVP 316
Cdd:cd06308  212 IIGVDGlPEAGEKAVKDGILAATFLYPTG--GKEAIEAALKILNGEKVP 258
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 37-324 3.18e-29

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: 113.85  E-value: 3.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd06309    2 VGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRlLMNSENVDYYATF---DNFGVGVSQAAYIEEHLGLKEGKgpfTIELFG--GSPDDNNaliNYNGVMSVLQPY 191
Cdd:cd06309   82 PVILVDR-TIDGEDGSLYVTFigsDFVEEGRRAAEWLVKNYKGGKGN---VVELQGtaGSSVAID---RSKGFREVIKKH 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 192 mdngqlvvPSGQTSFSQIATlrWDGSTAQARMDNLLSANYTDqtLDAVLSPYDPISLGIISSLKGVGYGSESKplPVITG 271
Cdd:cd06309  155 --------PNIKIVASQSGN--FTREKGQKVMENLLQAGPGD--IDVIYAHNDDMALGAIQALKEAGLKPGKD--VLVVG 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488216789 272 QDATVAGVKSIIAGEQTQTIFKDTRiLAKNTIEMIKAISDGEEVP---VNDTETYD 324
Cdd:cd06309  221 IDGQKDALEAIKAGELNATVECNPL-FGPTAFDTIAKLLAGEKVPkliIVEERLFD 275
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
 54-328 1.06e-23

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: 99.20  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  54 NNMVSELEKL-----GYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDR----- 123
Cdd:cd01539   16 SSVRKALEKAakaggKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVIFFNRepsre 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 124 LLMNSENVdYYATFDNFGVGVSQAA----YIEEHLGL-KEGKGPFTIELFGGSPDDNNALINYNGVMSVLQPYMDNGQLV 198
Cdd:cd01539   96 DLKSYDKA-YYVGTDAEESGIMQGEiiadYWKANPEIdKNGDGKIQYVMLKGEPGHQDAIARTKYSVKTLNDAGIKTEQL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 199 vpsgqtsfsQIATLRWDGSTAQARMDNLLSaNYTDQtLDAVLSPYDPISLGIISSLKGVGY--GSESKPLPVItGQDATV 276
Cdd:cd01539  175 ---------AEDTANWDRAQAKDKMDAWLS-KYGDK-IELVIANNDDMALGAIEALKAAGYntGDGDKYIPVF-GVDATP 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488216789 277 AGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNDTETYDNGVK 328
Cdd:cd01539  243 EALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLETGYKFLVEGKY 294
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 37-344 1.10e-20

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: 90.55  E-value: 1.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd06318    2 IGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSENVDYYATFDNFGVGVSQAAYIEEHLGLKEGKgpftIELFGGSPDDNNALINYNGVMSVLQPYMdngq 196
Cdd:cd06318   82 PVITVDSALDPSANVATQVGRDNKQNGVLVGKEAAKALGGDPGK----IIELSGDKGNEVSRDRRDGFLAGVNEYQ---- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 lVVPSGQTSFSQIATL--RWDGSTAQARMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYGSESKplpvITGQDA 274
Cdd:cd06318  154 -LRKYGKSNIKVVAQPygNWIRSGAVAAMEDLLQAH---PDINVVYAENDDMALGAMKALKAAGMLDKVK----VAGADG 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488216789 275 TVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEvpvndtetydngvkTVP-TYLANTVSVDKDN 344
Cdd:cd06318  226 QKEALKLIKDGKYVATGLNDPDLLGKTAVDTAAKVVKGEE--------------SFPeFTYTPTALITKDN 282
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 59-316 5.28e-20

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: 88.51  E-value: 5.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  59 ELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLMNSENVDYYATfD 138
Cdd:cd06323   24 EAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSVTGGKVVSHIAS-D 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 139 NFGVGVSQAAYIEEHLGlKEGKgpfTIELFG--GSPDDN-------NALINYNGVmsvlqpymdngqlvvpsgqtsfSQI 209
Cdd:cd06323  103 NVAGGEMAAEYIAKKLG-GKGK---VVELQGipGTSAARergkgfhNAIAKYPKI----------------------NVV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 210 ATLRWDGSTAQAR--MDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGygsesKPLPVITGQDATVAGVKSIIAGEQ 287
Cdd:cd06323  157 ASQTADFDRTKGLnvMENLLQAH---PDIDAVFAHNDEMALGAIQALKAAG-----RKDVIVVGFDGTPDAVKAVKDGKL 228

                        250       260
                 ....*....|....*....|....*....
gi 488216789 288 TQTIFKDTRILAKNTIEMIKAISDGEEVP 316
Cdd:cd06323  229 AATVAQQPEEMGAKAVETADKYLKGEKVP 257
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 72-316 1.93e-19

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: 86.94  E-value: 1.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  72 GEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLmNSENVDYYATFDNFGVGVSQAAYIE 151
Cdd:cd06313   37 GNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAGIPLVGVNALI-ENEDLTAYVGSDDVVAGELEGQAVA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 152 EHLGlkeGKGPFTIeLFGgsPDDNNALIN-YNGVMSVLQPYMDngqLVVPSGQTSfsqiatlRWDGSTAQARMDNLLSAn 230
Cdd:cd06313  116 DRLG---GKGNVVI-LEG--PIGQSAQIDrGKGIENVLKKYPD---IKVLAEQTA-------NWSRDEAMSLMENWLQA- 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 231 YTDQtLDAVLSPYDPISLGIISSLKGVGYGSeskplPVITGQDATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAIS 310
Cdd:cd06313  179 YGDE-IDGIIAQNDDMALGALQAVKAAGRDD-----IPVVGIDGIEDALQAVKSGELIATVLQDAEAQGKGAVEVAVDAV 252


                 ....*.
gi 488216789 311 DGEEVP 316
Cdd:cd06313  253 KGEGVE 258
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 54-273 3.40e-19

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


Pssm-ID: 380651 [Multi-domain]  Cd Length: 302  Bit Score: 86.53  E-value: 3.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  54 NNMVSELEKLGYK-TDLQY--GEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLmNSEN 130
Cdd:cd19996   19 AEFEAEAAKLKKLiKELIYtdAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSGV-GSDK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 131 VDYYATFDNFGVGVSQAAYIEEHLGlkeGKGpfTIELFGGSPDDNNALINYNGVMSVLQPYMDNGqlVVPSGQTSfsqia 210
Cdd:cd19996   98 YTAFVGVDDAAFGRVGAEWLVKQLG---GKG--NIIALRGIAGVSVSEDRWAGAKEVFKEYPGIK--IVGEVYAD----- 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488216789 211 tlrWDGSTAQARMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGygsesKPLPVITGQD 273
Cdd:cd19996  166 ---WDYAKAKQAVESLLAAY---PDIDGVWSDGGAMTLGAIEAFEEAG-----RPLVPMTGED 217
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 37-316 1.23e-18

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


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 84.64  E-value: 1.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd06322    2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLmNSENVDYYATFDNFGVGVSQAAYIEEHLGLKEGKgpftielfggspddnNALINYNGVMSVLQpyMDNGQ 196
Cdd:cd06322   82 PVFTVDVKA-DGAKVVTHVGTDNYAGGKLAGEYALKALLGGGGK---------------IAIIDYPEVESVVL--RVNGF 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LVVPSGQTSFSQIATLRWDG--STAQARMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYGSESKplpvITGQDA 274
Cdd:cd06322  144 KEAIKKYPNIEIVAEQPGDGrrEEALAATEDMLQAN---PDLDGIFAIGDPAALGALTAIESAGKEDKIK----VIGFDG 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 488216789 275 TVAGVKSIIAGEQTQT-IFKDTRILAKNTIEMIKAISDGEEVP 316
Cdd:cd06322  217 NPEAIKAIAKGGKIKAdIAQQPDKIGQETVEAIVKYLAGETVE 259
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
 61-316 4.86e-18

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: 83.05  E-value: 4.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLMNSENVDYYATFDNF 140
Cdd:cd06301   28 EYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPLVYVNREPDSKPKGVAFVGSDDI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 141 GVGVSQAAYIEEHLGlkeGKGpfTIELFGGSPDDNNALINYNGVMSVLQPYmdngqlvvPSGQTSFSQIAtlRWDGSTAQ 220
Cdd:cd06301  108 ESGELQMEYLAKLLG---GKG--NIAILDGVLGHEAQILRTEGNKDVLAKY--------PGMKIVAEQTA--NWSREKAM 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 221 ARMDNLLSAnYTDqtLDAVLSPYDPISLGIISSLKGVGygseSKPLPVITGQDATVAGVKSIIAGEQTQTIFKDTRILAK 300
Cdd:cd06301  173 DIVENWLQS-GDK--IDAIVANNDEMAIGAILALEAAG----KKDDILVAGIDATPDALKAMKAGRLDATVFQDAAGQGE 245

                        250
                 ....*....|....*.
gi 488216789 301 NTIEMIKAISDGEEVP 316
Cdd:cd06301  246 TAVDVAVKAAKGEEVE 261
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 49-316 5.03e-18

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: 82.63  E-value: 5.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  49 WIADGNNMVSELEKLGYK---TDLQYGEDKvenQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLL 125
Cdd:cd19971   14 FIAINDGIKKAVEANGDElitRDPQLDQNK---QNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 126 MNSENVDYYATFDNFGVGVSQAAYIEEHLGlkEGKGPFTIElfggSPDDNNALINYNGVMSVLQPYMDngqlvvpsgqts 205
Cdd:cd19971   91 KDTDLVDSTIASDNYNAGKLCGEDMVKKLP--EGAKIAVLD----HPTAESCVDRIDGFLDAIKKNPK------------ 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 206 FSQIATLRWDGSTAQAR--MDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYGSESKplpvITGQDATVAGVKSII 283
Cdd:cd19971  153 FEVVAQQDGKGQLEVAMpiMEDILQAH---PDLDAVFALNDPSALGALAALKAAGKLGDIL----VYGVDGSPDAKAAIK 225

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488216789 284 AGEQTQTIFKDTRILAKNTIEMIKAISDGEEVP 316
Cdd:cd19971  226 DGKMTATAAQSPIEIGKKAVETAYKILNGEKVE 258
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 37-305 3.89e-17

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: 80.44  E-value: 3.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd19967    2 VAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSENVDYYATFDNFGVGVSQAAYIEEHLGlkeGKGPFtIELFgGSPDDNNALINYNGVMSVLQPYMDNGQ 196
Cdd:cd19967   82 PVFLIDREINAEGVAVAQIVSDNYQGAVLLAQYFVKLMG---EKGLY-VELL-GKESDTNAQLRSQGFHSVIDQYPELKM 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 197 LVvpsgqtsfSQIATlrWDGSTAQARMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYGSESKplpvITGQDATV 276
Cdd:cd19967  157 VA--------QQSAD--WDRTEAFEKMESILQAN---PDIKGVICGNDEMALGAIAALKAAGRAGDVI----IVGFDGSN 219

                        250       260
                 ....*....|....*....|....*....
gi 488216789 277 AGVKSIIAGEQTQTIFKDTRILAKNTIEM 305
Cdd:cd19967  220 DVRDAIKEGKISATVLQPAKLIARLAVEQ 248
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 33-276 5.02e-16

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: 77.73  E-value: 5.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  33 STGYVG-------IAMPTKSAERWIADGnnMVSELEKLGYKTDlqygedkVENQVAQIENMITKGVDTLVIASIDGSALT 105
Cdd:cd19999    5 SNGYVGnewraqmIADFEEVAAEYKEEG--VISDLIVQNADAD-------ATGQISQIRNMINEGVDAILIDPVSATALN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 106 DVLAKAKEADIKVIAYDRLLmNSENVdYYATFDNFGVGVSQAAYIEEHLGlkeGKGPF-TIELFGGSPDDNnalINYNGV 184
Cdd:cd19999   76 PVIEKAQAAGILVVSFDQPV-SSPDA-INVVIDQYKWAAIQAQWLAEQLG---GKGNIvAINGVAGNPANE---ARVKAA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 185 MSVLQPYMDnGQLV--VPSGqtsfsqiatlrWDGSTAQARMDNLLSANytdQTLDAVLSPyDPISLGIISSLKgvgygSE 262
Cdd:cd19999  148 DDVFAKYPG-IKVLasVPGG-----------WDQATAQQVMATLLATY---PDIDGVLTQ-DGMAEGVLRAFQ-----AA 206

                        250
                 ....*....|....
gi 488216789 263 SKPLPVITGqDATV 276
Cdd:cd19999  207 GKDPPVMTG-DYRK 219
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 37-291 1.64e-15

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: 75.50  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd19968    2 IGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRllmNSENVDY--YATFDNFGVGVSQAAYIEEHLGlkeGKGpfTIELFGGSPDDNNALINYNGVMSVLQPYmDN 194
Cdd:cd19968   82 PVVTVDR---RAEGAAPvpHVGADNVAGGREVAKFVVDKLP---NGA--KVIELTGTPGSSPAIDRTKGFHEELAAG-PK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 195 GQLVvpsgqtsFSQiaTLRWDGSTAQARMDNLLSANYTDqtLDAVLSPYDPISLGIISSLKGVGYGSESKplpVITGQDA 274
Cdd:cd19968  153 IKVV-------FEQ--TGNFERDEGLTVMENILTSLPGP--PDAIICANDDMALGAIEAMRAAGLDLKKV---KVIGFDA 218

                        250
                 ....*....|....*..
gi 488216789 275 TVAGVKSIIAGEQTQTI 291
Cdd:cd19968  219 VPDALQAIKDGELYATV 235
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 37-344 2.02e-15

periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.


Pssm-ID: 380543 [Multi-domain]  Cd Length: 283  Bit Score: 75.38  E-value: 2.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQY--GEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEA 114
Cdd:cd06320    2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAapSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 115 DIKVIAYDRLLMNSE------NVDYYATFDNFGVGVSQAAYIEEHLGlkeGKGPftIELFGGSPDDNNALINYNGVMSVL 188
Cdd:cd06320   82 GIPVINLDDAVDADAlkkaggKVTSFIGTDNVAAGALAAEYIAEKLP---GGGK--VAIIEGLPGNAAAEARTKGFKETF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 189 QPYmDNGQLVVpsgqtsfSQIATlrWDGSTAQARMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYGSEskpLPV 268
Cdd:cd06320  157 KKA-PGLKLVA-------SQPAD--WDRTKALDAATAILQAH---PDLKGIYAANDTMALGAVEAVKAAGKTGK---VLV 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488216789 269 ItGQDATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPVNDtetydngvkTVPTYLantvsVDKDN 344
Cdd:cd06320  221 V-GTDGIPEAKKSIKAGELTATVAQYPYLEGAMAVEAALRLLQGQKVPAVV---------ATPQAL-----ITKDN 281
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 37-258 6.35e-15

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: 73.94  E-value: 6.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTkSAERWIAdGNNMVSE--LEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEA 114
Cdd:cd06311    2 IGISIPS-ADHGWTA-GVAYYAEkqAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 115 DIKVIAYDRLLmNSENVDYYATFDNFGVGVSQAAYIEEHLGlkeGKG-PFTIELFGGSPDDNNALINYNGVMSVLQPYMd 193
Cdd:cd06311   80 GIPVVNFDRGL-NVLIYDLYVAGDNPGMGVVSAEYIGKKLG---GKGnVVVLEVPSSGSVNEERVAGFKEVIKGNPGIK- 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488216789 194 ngqlVVPSGQTSFSqiatlRWDGSTAqarMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVG 258
Cdd:cd06311  155 ----ILAMQAGDWT-----REDGLKV---AQDILTKN---KKIDAVWAADDDMAIGVLQAIKEAG 204
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 73-285 7.56e-14

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


Pssm-ID: 380653 [Multi-domain]  Cd Length: 302  Bit Score: 71.17  E-value: 7.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  73 EDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLmnSENVDYYATFDNFGVGVSQAAYIEE 152
Cdd:cd19998   42 GTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVV--DEPCAYNVNTDQAKAGEQTAQWLVD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 153 HLGlkeGKGpfTIELFGGSPDDNNALINYNGVMSVLQPYMDNGQLVVPSGQtsfsqiatlrWDGSTAQARMDNLLSANyt 232
Cdd:cd19998  120 KLG---GKG--NILMVRGVPGTSVDRDRYEGAKEVFKKYPDIKVVAEYYGN----------WDDGTAQKAVADALAAH-- 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488216789 233 dQTLDAVLSPYDpiSLGIISSLKGVGygsesKPLPVITGQ----------DATVAGVKSIIAG 285
Cdd:cd19998  183 -PDVDGVWTQGG--ETGVIKALQAAG-----HPLVPVGGEaengfrkamlEPLANGLPGISAG 237
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 61-316 9.52e-13

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


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 67.66  E-value: 9.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQYG--EDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYD-RL---LMNSENVDY- 133
Cdd:cd19970   27 EANGYELLVKGIkqETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDnRLdadALKEGGINVp 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 134 YATFDNFGVGVSQAAYIEEHLGlkEGKGPFTIElfgGSPDDNNALINYNGvmsvLQPYMDNGQLVVPSGQTSfsqiatlR 213
Cdd:cd19970  107 FVGPDNRQGAYLAGDYLAKKLG--KGGKVAIIE---GIPGADNAQQRKAG----FLKAFEEAGMKIVASQSA-------N 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 214 WDGSTAQARMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYGSEskplPVITGQDATVAGVKSIIAGEQTQTIFK 293
Cdd:cd19970  171 WEIDEANTVAANLLTAH---PDIRGILCANDNMALGAIKAVDAAGKAGK----VLVVGFDNIPAVRPLLKDGKMLATIDQ 243

                        250       260
                 ....*....|....*....|....
gi 488216789 294 DTRILAKNTIEM-IKAIsDGEEVP 316
Cdd:cd19970  244 HPAKQAVYGIEYaLKML-NGEEVP 266
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
3-318 1.25e-12

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 67.59  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789   3 NKFRKIVgtiAILTASILLSaCGNSGSADdstgyVGIAMPTKSAERWIADGNNMVSELEKLGYKTDL--QYGEDKVENQV 80
Cdd:PRK09701   2 NKYLKYF---SGTLVGLMLS-TSAFAAAE-----YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIfaSPSEGDFQSQL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  81 AQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYD-RLLMNS-----ENVDYYATFDNFGVGVSQAAYIEEHL 154
Cdd:PRK09701  73 QLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDeKIDMDNlkkagGNVEAFVTTDNVAVGAKGASFIIDKL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 155 GLKEGKgpftIELFGGSPDDNNALINYNGVMSVlqpYMDNGQLVVPSGQTSfsqiatlRWDGSTAQARMDNLLSANytdQ 234
Cdd:PRK09701 153 GAEGGE----VAIIEGKAGNASGEARRNGATEA---FKKASQIKLVASQPA-------DWDRIKALDVATNVLQRN---P 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 235 TLDAVLSPYDPISLGIISSLKGVGYGSESkplpVITGQDATVAGVKSIIAGEQTQTIFKD-TRILAKNTIEMIKAISDGE 313
Cdd:PRK09701 216 NIKAIYCANDTMAMGVAQAVANAGKTGKV----LVVGTDGIPEARKMVEAGQMTATVAQNpADIGATGLKLMVDAEKSGK 291


                 ....*
gi 488216789 314 EVPVN 318
Cdd:PRK09701 292 VIPLD 296
PRK15395 PRK15395
galactose/glucose ABC transporter substrate-binding protein MglB;
79-344 1.54e-12

galactose/glucose ABC transporter substrate-binding protein MglB;


Pssm-ID: 185293 [Multi-domain]  Cd Length: 330  Bit Score: 67.83  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  79 QVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYD----RLLMNSENVDYYATFDNFGVGVSQAAYIEEH- 153
Cdd:PRK15395  70 QNDQIDVLLAKGVKALAINLVDPAAAPTVIEKARGQDVPVVFFNkepsRKALDSYDKAYYVGTDSKESGIIQGDLIAKHw 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 154 -----LGL-KEGKGPFTieLFGGSPD--DNNALINYngvmsVLQPYMDNGQlvvpsgQTSFSQIATLRWDGSTAQARMDN 225
Cdd:PRK15395 150 kanpaWDLnKDGKIQYV--LLKGEPGhpDAEARTTY-----VIKELNDKGI------KTEQLQLDTAMWDTAQAKDKMDA 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 226 LLSANYTDQtLDAVLSPYDPISLGIISSLKGVGYGSeskpLPVItGQDATVAGVKSIIAGEQTQTIFKDTRILAKNTIEM 305
Cdd:PRK15395 217 WLSGPNANK-IEVVIANNDAMAMGAVEALKAHNKSS----IPVF-GVDALPEALALVKSGAMAGTVLNDANNQAKATFDL 290

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 488216789 306 IKAISDGEEVPVNDTETYDNGVKTVPtylanTVSVDKDN 344
Cdd:PRK15395 291 AKNLADGKGAAEGTNWKIENKVVRVP-----YVGVDKDN 324
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 61-230 3.13e-12

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: 66.07  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQYGEDK-VENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLMNSENVDYYATfDN 139
Cdd:cd06314   26 KELGVNVEFVGPQKSdAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFDSDAPDSKRLAYIGT-DN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 140 FGVGVSQAAYIEEHLGlKEGKgpftIELFGGSPDDNNALINYNGVMSVLQPYMDngqlvVPSGQTSFSQIatlrwDGSTA 219
Cdd:cd06314  105 YEAGREAGELMKKALP-GGGK----VAIITGGLGADNLNERIQGFKDALKGSPG-----IEIVDPLSDND-----DIAKA 169

                        170
                 ....*....|.
gi 488216789 220 QARMDNLLSAN 230
Cdd:cd06314  170 VQNVEDILKAN 180
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 77-285 3.63e-12

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: 65.95  E-value: 3.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  77 ENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLMNSENVD-YYATfDNFGVGVSQAAYIEEHLG 155
Cdd:cd19973   44 ATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVLVIALDTPTDPIDAADaTFAT-DNFKAGVLIGEWAKAALG 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 156 LKEGKgpftIELFGGSPDDNNALINYNGVMS-----VLQP---YMDNGQLVVPSGQTSFSQiatlrwdgSTAQARMDNLL 227
Cdd:cd19973  123 AKDAK----IATLDLTPGHTVGVLRHQGFLKgfgidEKDPesnEDEDDSQVVGSADTNGDQ--------AKGQTAMENLL 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488216789 228 SAnytDQTLDAVLSPYDPISLGIISSLKGVGYGSESkplpVITGQDATVAGVKSIIAG 285
Cdd:cd19973  191 QK---DPDINLVYTINEPAAAGAYQALKAAGKEKGV----LIVSVDGGCPGVKDVKDG 241
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
 49-160 7.55e-12

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


Pssm-ID: 380529 [Multi-domain]  Cd Length: 269  Bit Score: 64.91  E-value: 7.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  49 WIADGNNMVSELEKLGykTDLQY----GEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRl 124
Cdd:cd06306   14 WVGVNYGIVDEAKRLG--VKLTVyeagGYTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVN- 90

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488216789 125 LMNSENVDYYATFDNFGVGVSQAAYIEEHLGLKEGK 160
Cdd:cd06306   91 GIDSPKVAARVLVDFYDMGYLAGEYLVEHHPGKPVK 126
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
 79-271 9.59e-12

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


Pssm-ID: 380523 [Multi-domain]  Cd Length: 302  Bit Score: 65.04  E-value: 9.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  79 QVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLmnSENVDYYATFDNFGVGVSQAAYIEEHLGlke 158
Cdd:cd06300   49 QIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGAV--TSPDAYNVSNDQVEWGRLGAKWLFEALG--- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 159 GKGP-FTIELFGGSPDDNNaliNYNGVMSVLQPYmdngqlvvpsGQTSFSQIATLRWDGSTAQARMDNLLSANytdQTLD 237
Cdd:cd06300  124 GKGNvLVVRGIAGAPASAD---RHAGVKEALAEY----------PGIKVVGEVFGGWDEATAQTAMLDFLATH---PQVD 187

                        170       180       190
                 ....*....|....*....|....*....|....
gi 488216789 238 AVLSpYDPISLGIISSLKGVGygseSKPLPVITG 271
Cdd:cd06300  188 GVWT-QGGEDTGVLQAFQQAG----RPPVPIVGG 216
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 37-316 2.06e-11

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: 63.46  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYK---TDLQYGEDkVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKE 113
Cdd:cd06321    2 IGVTVQDLGNPFFVAMVRGAEEAAAEINPGakvTVVDARYD-LAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 114 ADIKVIAYDrllMNSENVDYYATFDNFGVGVSQAAYIEEHLGlkeGKGPFTIElfGGSPddNNALIN-YNGVMSVLQPYM 192
Cdd:cd06321   81 AGIIVVAVD---VAAEGADATVTTDNVQAGYLACEYLVEQLG---GKGKVAII--DGPP--VSAVIDrVNGCKEALAEYP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 193 DngqLVVPSGQTSfsqiatlrwDGSTAQAR--MDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYGSeskplPVIT 270
Cdd:cd06321  151 G---IKLVDDQNG---------KGSRAGGLsvMTRMLTAH---PDVDGVFAINDPGAIGALLAAQQAGRDD-----IVIT 210

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488216789 271 GQD------ATVAGVKSIIAGEQTQtifkDTRILAKNTIEMIKAISDGEEVP 316
Cdd:cd06321  211 SVDgspeavAALKREGSPFIATAAQ----DPYDMARKAVELALKILNGQEPA 258
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 57-258 8.73e-11

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: 61.93  E-value: 8.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  57 VSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLMNSENVdyYAT 136
Cdd:cd06305   22 VAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAGIPVVTFDTDSQVPGVN--NIT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 137 FDNFGVGVSQAAYIEEHLGlkeGKGpftielfggspddNNALINYNGV----------MSVLQPYMDnGQLVVPSGQTSF 206
Cdd:cd06305  100 QDDYALGTLSLGQLVKDLN---GEG-------------NIAVFNVFGVppldkrydiyKAVLKANPG-IKKIVAELGDVT 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488216789 207 SQIAtlrwdgSTAQARMDNLLSAnYTDQTLDAVLSPYDPISLGIISSLKGVG 258
Cdd:cd06305  163 PNTA------ADAQTQVEALLKK-YPEGGIDAIWAAWDEPAKGAVQALEEAG 207
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 72-271 1.00e-10

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


Pssm-ID: 380652 [Multi-domain]  Cd Length: 305  Bit Score: 61.92  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  72 GEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDrLLMNSENVdYYATFDNFGVGVSQAAYIE 151
Cdd:cd19997   42 ADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFD-SGVTEPCA-YILNNDFEDYGAASVEYVA 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 152 EHLGlkeGKGPfTIELFG--GSPDDNNAlinYNGVMSVLQPYMD-------NGQlvvpsgqtsfsqiatlrWDGSTAQAR 222
Cdd:cd19997  120 DRLG---GKGN-VLEVRGvaGTSPDEEI---YAGQVEALKKYPDlkvvaevYGN-----------------WTQSVAQKA 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488216789 223 MDNLLSanyTDQTLDAVlspydpISLGiisslkGVGYG------SESKPLPVITG 271
Cdd:cd19997  176 VTGILP---SLPEVDAV------ITQG------GDGYGaaqafeAAGRPLPIIIG 215
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 73-162 2.25e-10

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


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 60.71  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  73 EDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLMNSENVDYYATfDNFGVGVSQAAYIEE 152
Cdd:cd20004   40 EDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDSDLGGDAVISFVAT-DNYAAGRLAAKRMAK 118

                         90
                 ....*....|
gi 488216789 153 HLGlkeGKGP 162
Cdd:cd20004  119 LLN---GKGK 125
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 37-317 2.28e-10

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


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 60.53  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd19972    2 IGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 117 KVIAYDRLLMNSENVDYYATfDNFGVGVSQAAYIEEHLGlkeGKGPFTI--ELFGGSPDDNNAlinyNGVMSVLQPYMDn 194
Cdd:cd19972   82 PVIAVDRNPEDAPGDTFIAT-DSVAAAKELGEWVIKQTG---GKGEIAIlhGQLGTTPEVDRT----KGFQEALAEAPG- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 195 gqLVVPSGQTSfsqiatlRWDGSTAQARMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYGSESkplpVITGQDA 274
Cdd:cd19972  153 --IKVVAEQTA-------DWDQDEGFKVAQDMLQAN---PNITVFFGQSDAMALGAAQAVKVAGLDHKI----WVVGFDG 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 488216789 275 TVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPV 317
Cdd:cd19972  217 DVAGLKAVKDGVLDATMTQQTQKMGRLAVDSAIDLLNGKAVPK 259
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 61-318 3.13e-10

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


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 60.05  E-value: 3.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQY--GEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLMNSENVDYYATfD 138
Cdd:cd06310   26 KDLGVKIIFVGpeSEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPVIVIDSGIKGDAYLSYIAT-D 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 139 NFGVGVSQAAYIEEHLGlKEGKgpftIELFGGSPDDNNALINYNGVMSVLQPYmDNGQLVVPSGQTSFsqiatlrwDGST 218
Cdd:cd06310  105 NYAAGRLAAQKLAEALG-GKGK----VAVLSLTAGNSTTDQREEGFKEYLKKH-PGGIKVLASQYAGS--------DYAK 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 219 AQARMDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVGygsESKPLPVItGQDATVAGVKSIIAGEQTQTIFKDTRIL 298
Cdd:cd06310  171 AANETEDLLGKY---PDIDGIFATNEITALGAAVAIKSRK---LSGQIKIV-GFDSQEELLDALKNGKIDALVVQNPYEI 243

                        250       260
                 ....*....|....*....|
gi 488216789 299 AKNTIEMIKAISDGEEVPVN 318
Cdd:cd06310  244 GYEGIKLALKLLKGEEVPKN 263
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 61-258 1.26e-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: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 58.54  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLmNSENVDYYATFDN- 139
Cdd:cd06317   26 KDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAVI-PSDFQAAQVGVDNl 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 140 -FGVGVSQAA--YIEEHLGlkegkGPFTIELFGGSpddnNALIN---YNGVMSVLQPymdngqlvVPSGQTSFSQIATLR 213
Cdd:cd06317  105 eGGKEIGKYAadYIKAELG-----GQAKIGVVGAL----SSLIQnqrQKGFEEALKA--------NPGVEIVATVDGQNV 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488216789 214 WDGSTAQArmDNLLSANytdQTLDAVLSPYDPISLGIISSLKGVG 258
Cdd:cd06317  168 QEKALSAA--ENLLTAN---PDLDAIYATGEPALLGAVAAVRSQG 207
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 37-270 7.16e-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: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 56.09  E-value: 7.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAErWIA---DGnnMVSELEKLGYK----TDLQYgedKVENQVAQIENMITKGVDTLVIASIDGSALTDVLA 109
Cdd:cd06316    2 VAIAMHTTGSD-WSRlqvAG--IKDTFEELGIEvvavTDANF---DPAKQITDLETLIALKPDIIISIPVDPVATAAAYK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 110 KAKEADIKVIAYDRLLMNSENVDYYATF---DNFGVGVSQAAYIEEHLGlkeGKGPFTIELFggspDDNNALIN--YNGV 184
Cdd:cd06316   76 KVADAGIKLVFMDNVPDGLEAGKDYVSVvssDNRGNGQIAAELLAEAIG---GKGKVGIIYH----DADFYATNqrDKAF 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 185 MSVLQPYMDNGQLVVPSGQTSFSQIatlrwdGSTAQArmdnLLSANytdQTLDAVLSPYDPISLGIISSLKGVGYgsesK 264
Cdd:cd06316  149 KDTLKEKYPDIKIVAEQGFADPNDA------EEVASA----MLTAN---PDIDGIYVSWDTPALGVISALRAAGR----S 211


                 ....*.
gi 488216789 265 PLPVIT 270
Cdd:cd06316  212 DIKITT 217
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
 76-122 1.17e-08

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: 55.71  E-value: 1.17e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488216789  76 VENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYD 122
Cdd:cd06302   42 AAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWD 88
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
 58-318 1.23e-08

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: 55.33  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  58 SELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSAlTDVLAKAKEADIKVIAYDRLLMNSENVdYYATF 137
Cdd:cd01537   23 QDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAA-AGVAEKARGQNVPVVFFDKEPSRYDKA-YYVIT 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 138 DNFGVGVSQAAYIEEHlglkegkGPFTIELFGGSPDDNNALINYNGVMSvlqpYMDNGQLVVPSgqtsfSQIATLRWDGS 217
Cdd:cd01537  101 DSKEGGIIQGDLLAKH-------GHIQIVLLKGPLGHPDAEARLAGVIK----ELNDKGIKTEQ-----LQLDTGDWDTA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 218 TAQARMDNLLSANYtdqTLDAVLSPYDPISLGIISSLKGVGYGSESKpLPVItGQDATVAGVKSIIAgeqTQTIFKDTRI 297
Cdd:cd01537  165 SGKDKMDQWLSGPN---KPTAVIANNDAMAMGAVEALKEHGLRVPSD-ISVF-GYDALPEALKSGPL---LTTILQDANN 236

                        250       260
                 ....*....|....*....|..
gi 488216789 298 LAKNTIEMIKAISD-GEEVPVN 318
Cdd:cd01537  237 LGKTTFDLLLNLADnWKIDNKV 258
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 73-160 1.55e-08

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: 54.94  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  73 EDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLmNSENVDYYATFDNFGVGVSQAAYIEE 152
Cdd:cd20005   40 ESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGV-PSDLPLATVATDNYAAGALAADHLAE 118


                 ....*...
gi 488216789 153 HLGlKEGK 160
Cdd:cd20005  119 LIG-GKGK 125
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 61-172 6.57e-08

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: 53.10  E-value: 6.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGS-ALTDVLAKAKEADIKVIAYDRLLMNSENVD---YYAT 136
Cdd:cd19966   27 ADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDgAYTPLIEAAKKAGIIVTSFNTDLPKLEYGDcglGYVG 106

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488216789 137 FDNFGVGVSQAAYIEEHLGLKEGKGPFTIELFGGSP 172
Cdd:cd19966  107 ADLYAAGYTLAKELVKRGGLKTGDRVFVPGLLPGQP 142
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 79-160 1.64e-07

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: 52.28  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  79 QVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRllMNSENVDY-YATFDNFGVGVSQAAYIEEHLGlK 157
Cdd:cd20001   45 QVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDAGIVVITHEA--SNLKNVDYdVEAFDNAAYGAFIMDKLAEAMG-G 121


                 ...
gi 488216789 158 EGK 160
Cdd:cd20001  122 KGK 124
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
 76-160 3.59e-07

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: 50.80  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  76 VENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLMNSENVDYYATfDNFGVGVSQAAYIEEHLG 155
Cdd:cd19969   42 VNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSDAPESKRISYVGT-DNYEAGYAAAEKLAELLG 120


                 ....*
gi 488216789 156 lKEGK 160
Cdd:cd19969  121 -GKGK 124
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 72-191 1.22e-06

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: 49.52  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  72 GEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLmNSENVDYYATFDNFGVGVSQAAYIE 151
Cdd:cd20006   41 SEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSPV-NSKKADSFVATDNYEAGKKAGEKLA 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488216789 152 EHLGlKEGKgpftIELFGGSPDDNNALINYNGVMSVLQPY 191
Cdd:cd20006  120 SLLG-EKGK----VAIVSFVKGSSTAIEREEGFKQALAEY 154
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
12-316 2.35e-06

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 48.55  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  12 IAILTASILLSAC-GNSGSADDStgyVGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKG 90
Cdd:PRK10653   6 LATLVSAVALSATvSANAMAKDT---IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  91 VDTLVIASIDGSALTDVLAKAKEADIKVIAYDRLLMNSENVDYYATfDNFGVGVSQAAYIEEhlglKEGKGPFTIELFG- 169
Cdd:PRK10653  83 TKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIAS-DNVAGGKMAGDFIAK----KLGEGAKVIQLEGi 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 170 -GSpddNNALINYNGVMSVlqpyMDNGQLVVPSGQTSfsqiatlRWDGSTAQARMDNLLSANYTDQtldAVLSPYDPISL 248
Cdd:PRK10653 158 aGT---SAARERGEGFKQA----VAAHKFNVLASQPA-------DFDRTKGLNVMQNLLTAHPDVQ---AVFAQNDEMAL 220

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488216789 249 GIISSLKGVGygsesKPLPVITGQDATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVP 316
Cdd:PRK10653 221 GALRALQTAG-----KSDVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGVETADKVLKGEKVE 283
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 61-291 2.43e-06

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: 48.75  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQYGEDKVENQVAQIENMIT--KGVDTLVIASIDGSAlTDVLAKAKEADIKVIAYDRLLMNSENVDYYA--- 135
Cdd:cd06324   27 KDLGIELEVLYANRNRFKMLELAEELLArpPKPDYLILVNEKGVA-PELLELAEQAKIPVFLINNDLTDEERALLGKpre 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 136 ---------TFDNFGVGVSQAAYIEEHLGLKEGKGPFTIELFGGSPDDNNALINYNGVMSVLQPYmDNGQLVvpsgqtsf 206
Cdd:cd06324  106 kfkywlgsiVPDNEQAGYLLAKALIKAARKKSDDGKIRVLAISGDKSTPASILREQGLRDALAEH-PDVTLL-------- 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 207 sQIATLRWDGSTAQARMDNLLSAnYTDqtLDAVLSPYDPISLGIISSLKgvGYGSESKPLPVITGQDATVAGVKSIIAGE 286
Cdd:cd06324  177 -QIVYANWSEDEAYQKTEKLLQR-YPD--IDIVWAANDAMALGAIDALE--EAGLKPGKDVLVGGIDWSPEALQAVKDGE 250


                 ....*
gi 488216789 287 QTQTI 291
Cdd:cd06324  251 LTASV 255
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
 73-141 3.33e-06

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: 48.04  E-value: 3.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488216789  73 EDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDRlLMNSENVDYY---ATFDNFG 141
Cdd:cd20003   39 EASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVTWDS-DVNPDARDFFvnqATPEGIG 109
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
 76-165 4.39e-06

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: 47.64  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  76 VENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYDR--------LLMNSenvdyyATFDnfGVGVSQA 147
Cdd:cd20000   42 AEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAAGIKVVTFDSdvapeardLFVNQ------ADAD--GIGRAQV 113

                         90
                 ....*....|....*...
gi 488216789 148 AYIEEHLGlkeGKGPFTI 165
Cdd:cd20000  114 DMMAELIG---GEGEFAI 128
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 61-230 1.23e-05

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: 46.11  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQYGED-KVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYdrllmnseNVD--YYATF 137
Cdd:cd19965   26 ELLGAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAF--------NVDapGGENA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 138 -------DNFGVGVSQAAYIEEHLGLKEGKgpftIELFGGSPDDNNALINYNGVMSVLQPYMDNGQL-VVPSGQtsfsqi 209
Cdd:cd19965   98 rlafvgqDLYPAGYVLGKRIAEKFKPGGGH----VLLGISTPGQSALEQRLDGIKQALKEYGRGITYdVIDTGT------ 167

                        170       180
                 ....*....|....*....|.
gi 488216789 210 atlrwDGSTAQARMDNLLSAN 230
Cdd:cd19965  168 -----DLAEALSRIEAYYTAH 183
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 37-161 1.41e-05

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: 46.20  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  37 VGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADI 116
Cdd:cd06319    2 IGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKI 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488216789 117 KVIAYDrLLMNSENVDYYATFDNFGVGVSQAAYIEEHLGLKEGKG 161
Cdd:cd06319   82 PVVIAD-IGTGGGDYVSYIISDNYDGGYQAGEYLAEALKENGWGG 125
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 34-150 5.42e-05

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: 44.42  E-value: 5.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789   34 TGYVGIAMPTKSAERWIADGNNMVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSAlTDVLAKAKE 113
Cdd:pfam00532   1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSG-DDITAKAEG 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 488216789  114 ADIKVIAYDRLLMNSENVDYYaTFDNFGVGVSQAAYI 150
Cdd:pfam00532  80 YGIPVIAADDAFDNPDGVPCV-MPDDTQAGYESTQYL 115
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 61-161 1.96e-04

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: 42.60  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQYGEDK--VENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKeADIKVIAYDRLLmNSENVD-YYATf 137
Cdd:cd20008   26 KELGVEVTFLGPATEadIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD-AGIPVVLVDSGA-NTDDYDaFLAT- 102

                         90       100
                 ....*....|....*....|....
gi 488216789 138 DNFGVGVSQAAYIEEHLGLKEGKG 161
Cdd:cd20008  103 DNVAAGALAADELAELLKASGGGK 126
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
 49-170 2.02e-04

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 43.01  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  49 WIADGNNMVSELEKLGYKTDLqY---GEDKVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKeADIKVIAydrlL 125
Cdd:PRK10936  61 WLSVNYGMVEEAKRLGVDLKV-LeagGYYNLAKQQQQLEQCVAWGADAILLGAVTPDGLNPDLELQA-ANIPVIA----L 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488216789 126 MNSENVDYYATfdnfGVGVS------QAA-YIEEHlgLKEGKGPFTIELFGG 170
Cdd:PRK10936 135 VNGIDSPQVTT----RVGVSwyqmgyQAGrYLAQW--HPKGSKPLNVALLPG 180
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 61-349 2.06e-04

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


Pssm-ID: 380482 [Multi-domain]  Cd Length: 294  Bit Score: 42.66  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASID---GSAltdVLAKAKEADIKVIAYDRLLMNSENVDY--YA 135
Cdd:cd01540   26 KELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDqklGPA---IAAKAKAAGIPVIAVDDQLVDADPMKIvpFV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 136 TFDNFGVGVSQAAYIEEHLglkegkgpftielfggspdDNNALINYN--GVMSVlqpYMDNgqlvVPSgqtsfsqiATLR 213
Cdd:cd01540  103 GIDAYKIGEAVGEWLAKEM-------------------KKRGWDDVKevGVLAI---TMDT----LSV--------CVDR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 214 WDGSTAQARM-----DNLLSANY----TDQTLDA---------------VLSPYDPISLGIISSLKGVGYGSESKPLPVI 269
Cdd:cd01540  149 TDGAKDALKAagfpeDQIFQAPYkgtdTEGAFNAanavitahpevkhwlVVGCNDEGVLGAVRALEQAGFDAEDIIGVGI 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 270 TGQDATVAGVKSIIAGEQTQTIFKDTRILAKNTIEMIKAISDGEEVPvndtetydngvktvPTYLANTVSVDKDNYQAEL 349
Cdd:cd01540  229 GGYLAADEEFKKQPTGFKASLYISPDKHGYIAAEELYNWITDGKPPP--------------AETLTDGVIVTRDNYKEVM 294
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 79-119 3.66e-04

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: 41.92  E-value: 3.66e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 488216789  79 QVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVI 119
Cdd:cd20002   45 QVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVI 85
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 58-259 4.35e-04

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


Pssm-ID: 380491 [Multi-domain]  Cd Length: 264  Bit Score: 41.35  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  58 SELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSalTDVLAKAKEADIKVIAYDRLLmNSENVDyYATF 137
Cdd:cd06267   23 DAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLD--DELLEELLAAGIPVVLIDRRL-DGLGVD-SVVV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 138 DNFGvGVSQAAyieEHLglkegkgpftIEL-------FGGSPDDNNALINYNGVMSVLQpymDNGQLVVPsgqtsfSQIA 210
Cdd:cd06267   99 DNYA-GAYLAT---EHL----------IELghrriafIGGPLDLSTSRERLEGYRDALA---EAGLPVDP------ELVV 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488216789 211 TLRWDGSTAQARMDNLLSAnytDQTLDAVLSPYDPISLGIISSLKGVGY 259
Cdd:cd06267  156 EGDFSEESGYEAARELLAL---PPRPTAIFAANDLMAIGALRALRELGL 201
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 61-161 4.81e-04

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: 41.45  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  61 EKLGYKTDLQYGED-KVENQVAQIENMITKGVDTLVIASIDGSALTDVLAKAKEADIKVIAYD-RLLMNSENVDYYATfD 138
Cdd:cd20007   26 KELGVELDVQGPPTfDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVDtTLGDPSFVLSQIAS-D 104

                         90       100
                 ....*....|....*....|...
gi 488216789 139 NFGVGVSQAAYIEEHLGlkeGKG 161
Cdd:cd20007  105 NVAGGALAAEALAELIG---GKG 124
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
59-259 5.34e-04

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 41.34  E-value: 5.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  59 ELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSAltDVLAKAKEADIKVIAYDRLLmNSENVDyYATFD 138
Cdd:COG1609   86 AARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDD--ARLERLAEAGIPVVLIDRPL-PDPGVP-SVGVD 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789 139 NFGvGVSQAAyieEHLglkEGKGPFTIELFGGSPDDNNALINYNGVMSVLQpymDNGQLVVPsgqtsfSQIATLRWDGST 218
Cdd:COG1609  162 NRA-GARLAT---EHL---IELGHRRIAFIGGPADSSSARERLAGYREALA---EAGLPPDP------ELVVEGDFSAES 225

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488216789 219 AQARMDNLLSAnytDQTLDAVLSPYDPISLGIISSLKGVGY 259
Cdd:COG1609  226 GYEAARRLLAR---GPRPTAIFCANDLMALGALRALREAGL 263
ProX COG2113
ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport ...
 6-73 3.18e-03

ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport and metabolism];


Pssm-ID: 441716 [Multi-domain]  Cd Length: 297  Bit Score: 39.06  E-value: 3.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488216789   6 RKIVGTIAILTASILLSACGNSGSADDSTGYVGIAMPTksaerWiADG---NNMVSE-LEKLGYKTDLQYGE 73
Cdd:COG2113    2 KKLLLLLLAAALALALAGCAAAAAAPGSCKTVTIADVG-----W-TSAtatTAVAKQiLEELGYEVELVELD 67
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
 56-154 4.90e-03

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: 38.32  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216789  56 MVSELEKLGYKTDLQYGEDKVENQVAQIENMITKGVDTLVIASIDGSAlTDVLAKAKEADIKVIAYDRLLMNSEnVDYYA 135
Cdd:cd06289   21 IEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTT-AELLRRLKAWGIPVVLALRDVPGSD-LDYVG 98

                         90
                 ....*....|....*....
gi 488216789 136 TfDNFgVGVSQAAyieEHL 154
Cdd:cd06289   99 I-DNR-LGAQLAT---EHL 112
 
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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