NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1629933285|gb|TJI97519|]
View 

autoinducer 2 ABC transporter substrate-binding protein [Escherichia coli]

Protein Classification

autoinducer 2 ABC transporter substrate-binding protein( domain architecture ID 14448390)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
2-285 2.32e-165

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: 460.25  E-value: 2.32e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:cd20002    12 PWFNRMEQGVKKAGKEFGVNAYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVITHESPG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSANWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTRRMPVAESVDDS 161
Cdd:cd20002    92 QKGADWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKYPNMKQVTDRIPGGEDVDVS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 162 RRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVA 241
Cdd:cd20002   172 RQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGLKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDPADAGYAMVYIA 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1629933285 242 STLLKGEEIKPGLEMQNLGKADVDMDKRIIRFHKVLLVNKDNID 285
Cdd:cd20002   252 KMLLDGKRKEIGDGFEIPGKGTPDIDGNVIIFDAPLEITKENAD 295
 
Name Accession Description Interval E-value
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
2-285 2.32e-165

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: 460.25  E-value: 2.32e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:cd20002    12 PWFNRMEQGVKKAGKEFGVNAYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVITHESPG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSANWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTRRMPVAESVDDS 161
Cdd:cd20002    92 QKGADWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKYPNMKQVTDRIPGGEDVDVS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 162 RRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVA 241
Cdd:cd20002   172 RQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGLKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDPADAGYAMVYIA 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1629933285 242 STLLKGEEIKPGLEMQNLGKADVDMDKRIIRFHKVLLVNKDNID 285
Cdd:cd20002   252 KMLLDGKRKEIGDGFEIPGKGTPDIDGNVIIFDAPLEITKENAD 295
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
2-249 2.09e-66

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: 207.93  E-value: 2.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:pfam13407  11 PFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAGIPVVTFDSDA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSANWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTRRMPVAESVDDS 161
Cdd:pfam13407  91 PSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVAEVEGTNWDPEKA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 162 RRTTLDLMKTYPD-LKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAV 240
Cdd:pfam13407 171 QQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVLQDPYGQGYAAVEL 250

                  ....*....
gi 1629933285 241 ASTLLKGEE 249
Cdd:pfam13407 251 AAALLKGKK 259
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
2-250 5.20e-53

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 175.11  E-value: 5.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVgPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI-VVLTNESP 80
Cdd:COG1879    46 PFFVAVRKGAEAAAKELGVELIVV-DAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIpVVTVDSDV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  81 GQPSANWDIEIiDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEhYPDMHEVTRRmPVAESVDD 160
Cdd:COG1879   125 DGSDRVAYVGS-DNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANERTDGFKEALKE-YPGIKVVAEQ-YADWDREK 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 161 SRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAV 240
Cdd:COG1879   202 ALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDA 281
                         250
                  ....*....|
gi 1629933285 241 ASTLLKGEEI 250
Cdd:COG1879   282 ALKLLKGKEV 291
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
3-285 2.61e-23

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 97.17  E-value: 2.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   3 WFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPGQ 82
Cdd:PRK15408   37 FFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  83 PSA-NWDIEIIDNEKFAAEYVEHMAKRMGGKGGYV-IYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTRRMPVAESVdD 160
Cdd:PRK15408  117 PECrSYYINQGTPEQLGSMLVEMAAKQVGKDKAKVaFFYSSPTVTDQNQWVKEAKAKIAKEHPGWEIVTTQFGYNDAT-K 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 161 SRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVkEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAV 240
Cdd:PRK15408  196 SLQTAEGILKAYPDLDAIIAPDANALPAAAQAA-ENLKRDKVAIVGFSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVYV 274
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1629933285 241 ASTLLKGEEIKPG--LEMQNLGKADVDMDK-----------RIIRFHKVLLVNKDNID 285
Cdd:PRK15408  275 ANELLKKGKLNVGdsLDVPGIGKVEVSPNSvqgydyeakgnGIVLLPERVVFTKENID 332
 
Name Accession Description Interval E-value
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
2-285 2.32e-165

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: 460.25  E-value: 2.32e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:cd20002    12 PWFNRMEQGVKKAGKEFGVNAYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVITHESPG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSANWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTRRMPVAESVDDS 161
Cdd:cd20002    92 QKGADWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKYPNMKQVTDRIPGGEDVDVS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 162 RRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVA 241
Cdd:cd20002   172 RQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGLKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDPADAGYAMVYIA 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1629933285 242 STLLKGEEIKPGLEMQNLGKADVDMDKRIIRFHKVLLVNKDNID 285
Cdd:cd20002   252 KMLLDGKRKEIGDGFEIPGKGTPDIDGNVIIFDAPLEITKENAD 295
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
1-285 7.73e-106

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: 309.56  E-value: 7.73e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   1 MPWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESP 80
Cdd:cd06302    11 IPYFDAAEEGAKKAAKELGVEVVYTGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  81 GQPSA-NWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMhEVTRRMPVAESVD 159
Cdd:cd06302    91 APPSArDYFVNQADDEGLGEALVDSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKYPDI-ELVDTYYTDDDQQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 160 DSRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAA 239
Cdd:cd06302   170 KAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGKVAVTGIGLPNTARPYLKDGSVKEGVLWDPAKLGYLTVY 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1629933285 240 VASTLLKGEEIK-PGLEMQNLGKADVDMDKRIIRFHKVLLVNKDNID 285
Cdd:cd06302   250 AAYQLLKGKGFTeDSDDVGTGGKVKVDVAGGEILLGPPLVFTKDNVD 296
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
2-285 1.14e-100

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: 296.50  E-value: 1.14e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:cd20001    12 AWFDRMETGVEQFAKDTGVNVYQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDAGIVVITHEASN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSANWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTRRMPVAESVDDS 161
Cdd:cd20001    92 LKNVDYDVEAFDNAAYGAFIMDKLAEAMGGKGKYVTFVGSLTSTSHMEWANAAVAYQKANYPDMLLVTDRVETNDDSETA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 162 RRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVA 241
Cdd:cd20001   172 YEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGKIAVVGTGLPSVAGEYLEDGTIDYIQFWDPADAGYAMNALA 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1629933285 242 STLLKGEEIKPGLemqNLG-----KADVDmDKRIIRFHKVLLVNKDNID 285
Cdd:cd20001   252 VMVLEGEKITDGT---DLGvpgyeKVTVG-KGKVLYGNAWLIVTKDNVD 296
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
2-249 2.09e-66

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: 207.93  E-value: 2.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:pfam13407  11 PFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAGIPVVTFDSDA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSANWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTRRMPVAESVDDS 161
Cdd:pfam13407  91 PSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVAEVEGTNWDPEKA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 162 RRTTLDLMKTYPD-LKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAV 240
Cdd:pfam13407 171 QQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVLQDPYGQGYAAVEL 250

                  ....*....
gi 1629933285 241 ASTLLKGEE 249
Cdd:pfam13407 251 AAALLKGKK 259
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
2-285 1.89e-56

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: 183.63  E-value: 1.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:cd20003    12 PYFTAAGQGAQEAAKELGVDVTYDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVTWDSDV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSA-NWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTRRmPVAESVDD 160
Cdd:cd20003    92 NPDArDFFVNQATPEGIGKTLVDMVAEQTGEKGKVAIVTSSPTATNQNAWIKAMKAYIAEKYPDMKIVTTQ-YGQEDPAK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 161 SRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAV 240
Cdd:cd20003   171 SLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTGKVAVTGLSTPNVMRPYVKDGTVKSVVLWDVVDLGYLAVYV 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1629933285 241 ASTLLKGEEIKPG--LEMQNLGKADV-DMDKRIIRFHKVLLVNKDNID 285
Cdd:cd20003   251 ARALADGTLLKVGdfFVAGRLGTFTVvPKGNGIILLGEPLIFTKENID 298
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
2-250 5.20e-53

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 175.11  E-value: 5.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVgPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI-VVLTNESP 80
Cdd:COG1879    46 PFFVAVRKGAEAAAKELGVELIVV-DAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIpVVTVDSDV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  81 GQPSANWDIEIiDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEhYPDMHEVTRRmPVAESVDD 160
Cdd:COG1879   125 DGSDRVAYVGS-DNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANERTDGFKEALKE-YPGIKVVAEQ-YADWDREK 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 161 SRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAV 240
Cdd:COG1879   202 ALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDA 281
                         250
                  ....*....|
gi 1629933285 241 ASTLLKGEEI 250
Cdd:COG1879   282 ALKLLKGKEV 291
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
2-285 5.52e-42

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: 146.25  E-value: 5.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:cd20000    12 PYFDAARDGAKEAAKELGGELIFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAAGIKVVTFDSDV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSA-NWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKY-QKEHYPDMHEVTrrmpVA---E 156
Cdd:cd20000    92 APEArDLFVNQADADGIGRAQVDMMAELIGGEGEFAILSATPTATNQNAWIDAMKKElASPEYAGMKLVK----VAygdD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 157 SVDDSRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYa 236
Cdd:cd20000   168 DAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGKVKVTGLGLPSEMAKYVKDGTVPAFALWNPIDLGY- 246
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1629933285 237 LAAVASTLLKGEEI--KPG--LEMQNLGKADVDmDKRIIRFHKVLLVNKDNID 285
Cdd:cd20000   247 LAAYAAAALAQGEItgKEGetFTAGRLGEYTVG-EGGEVVLGPPFVFTADNID 298
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
2-252 2.69e-39

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: 138.47  E-value: 2.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSStDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:cd01536    12 PFWVAVKKGAEAAAKELGVELVVLDAQG-DVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAGIPVVAVDTDI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSANWDIEI-IDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEhYPDMHEVTRRmPVAESVDD 160
Cdd:cd01536    91 DGGGDVVAFVgTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKK-YPDIEIVAEQ-PANWDRAK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 161 SRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAV 240
Cdd:cd01536   169 ALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGDIKIVGVDGTPEALKAIKDGELDATVAQDPYLQGYLAVEA 248
                         250
                  ....*....|..
gi 1629933285 241 ASTLLKGEEIKP 252
Cdd:cd01536   249 AVKLLNGEKVPK 260
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
2-235 7.66e-29

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: 110.75  E-value: 7.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:cd06314    12 PFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFDSDA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSANWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEhYPDMHEVTRR-----MPVAE 156
Cdd:cd06314    92 PDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKG-SPGIEIVDPLsdnddIAKAV 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1629933285 157 SVddsrrtTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGY 235
Cdd:cd06314   171 QN------VEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVIAATVGQRPYEMGY 243
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
2-235 4.57e-28

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: 108.96  E-value: 4.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:cd19969    12 PYWDDVKEGFEDAGAELGVKTEYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSDA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 QPSANWDIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTvPQHNLWADLLVKYQKEhYPDMhEVTRRMPVAESVDDS 161
Cdd:cd19969    92 PESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQ-PNHEERVEGFKEAFAE-YPGI-EVVAVGDDNDDPEKA 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1629933285 162 RRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGY 235
Cdd:cd19969   169 AQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTGKVKIVAFDDDPETLDLIKDGVIDASIAQRPWMMGY 242
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
9-251 5.45e-26

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: 103.19  E-value: 5.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   9 EGVVEAGKAFGVNASQVGPSSTDAPQ-QVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPGQPSANW 87
Cdd:cd06310    19 EGAEAAAKDLGVKIIFVGPESEEDVAgQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPVIVIDSGIKGDAYL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  88 DIEIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTrrMPVAES-VDDSRRTTL 166
Cdd:cd06310    99 SYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIKVLA--SQYAGSdYAKAANETE 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 167 DLMKTYPDLKAVvsFGSNGP--IGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVASTL 244
Cdd:cd06310   177 DLLGKYPDIDGI--FATNEItaLGAAVAIKSRKLSGQIKIVGFDSQEELLDALKNGKIDALVVQNPYEIGYEGIKLALKL 254

                  ....*..
gi 1629933285 245 LKGEEIK 251
Cdd:cd06310   255 LKGEEVP 261
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
13-252 2.30e-25

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


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 101.55  E-value: 2.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  13 EAGKAFGVNASQVGP-SSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPGQPSANWDIEI 91
Cdd:cd20005    23 QAAKELGVKITFEGPdTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGVPSDLPLATVA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  92 IDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTrrmpVAESVDDSRR---TTLDL 168
Cdd:cd20005   103 TDNYAAGALAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDIKVVN----VQYGVGDHAKaadIAKAI 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 169 MKTYPDLKAVvsFGSNGP--IGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVASTLLK 246
Cdd:cd20005   179 LQANPDLKGI--YATNEGaaIGVANALKEMGKLGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAAVKALK 256

                  ....*.
gi 1629933285 247 GEEIKP 252
Cdd:cd20005   257 GEEVEK 262
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
3-285 2.61e-23

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 97.17  E-value: 2.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   3 WFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPGQ 82
Cdd:PRK15408   37 FFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  83 PSA-NWDIEIIDNEKFAAEYVEHMAKRMGGKGGYV-IYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTRRMPVAESVdD 160
Cdd:PRK15408  117 PECrSYYINQGTPEQLGSMLVEMAAKQVGKDKAKVaFFYSSPTVTDQNQWVKEAKAKIAKEHPGWEIVTTQFGYNDAT-K 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 161 SRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVkEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAV 240
Cdd:PRK15408  196 SLQTAEGILKAYPDLDAIIAPDANALPAAAQAA-ENLKRDKVAIVGFSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVYV 274
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1629933285 241 ASTLLKGEEIKPG--LEMQNLGKADVDMDK-----------RIIRFHKVLLVNKDNID 285
Cdd:PRK15408  275 ANELLKKGKLNVGdsLDVPGIGKVEVSPNSvqgydyeakgnGIVLLPERVVFTKENID 332
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
9-252 1.15e-22

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 94.20  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   9 EGVVEAGKAFGVNASQVGPSS-TDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPgQPSANW 87
Cdd:cd20006    21 SGAEAAAKEYGVDLEFLGPESeEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSP-VNSKKA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  88 DIEI-IDNEKFAAEYVEHMAKRMGGKGGYVI---YVGSLTVPQHnlwADLLVKYQKEHypDMHEVTRRMPVAESVDDSRR 163
Cdd:cd20006   100 DSFVaTDNYEAGKKAGEKLASLLGEKGKVAIvsfVKGSSTAIER---EEGFKQALAEY--PNIKIVETEYCDSDEEKAYE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 164 TTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVAST 243
Cdd:cd20006   175 ITKELLSKYPDINGIVALNEQSTLGAARALKELGLGGKVKVVGFDSSVEEIQLLEEGIIDALVVQNPFNMGYLSVQAAVD 254

                  ....*....
gi 1629933285 244 LLKGEEIKP 252
Cdd:cd20006   255 LLNGKKIPK 263
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
2-252 1.98e-21

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: 91.15  E-value: 1.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNES-- 79
Cdd:cd20007    12 PFYITMQCGAEAAAKELGVELDVQGPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVDTtl 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  80 --PGQPSANwdieII-DNE---KFAAEYvehMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEhYPDMHEVtrrmP 153
Cdd:cd20007    92 gdPSFVLSQ----IAsDNVaggALAAEA---LAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMKK-YPGIKVL----G 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 154 VAESVDDSRRT---TLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDP 230
Cdd:cd20007   160 VQYSENDPAKAasiVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGKVKVVGFDASPAQVEQLKAGTIDALIAQKP 239
                         250       260
                  ....*....|....*....|..
gi 1629933285 231 ASAGYALAAVASTLLKGEEIKP 252
Cdd:cd20007   240 AEIGYLAVEQAVAALTGKPVPK 261
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
2-252 3.75e-21

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: 90.03  E-value: 3.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSsTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPG 81
Cdd:cd06322    12 PFFVDIKDAMKKEAAELGVKVVVADAN-GDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFTVDVKA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 qPSANWDIEI-IDNE---KFAAEYvehMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEhYPDMhEVTRRMPVAES 157
Cdd:cd06322    91 -DGAKVVTHVgTDNYaggKLAGEY---ALKALLGGGGKIAIIDYPEVESVVLRVNGFKEAIKK-YPNI-EIVAEQPGDGR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 158 VDDSRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLI-KSGDITEGITYDPASAGYA 236
Cdd:cd06322   165 REEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDKIKVIGFDGNPEAIKAIaKGGKIKADIAQQPDKIGQE 244
                         250
                  ....*....|....*.
gi 1629933285 237 LAAVASTLLKGEEIKP 252
Cdd:cd06322   245 TVEAIVKYLAGETVEK 260
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
2-285 1.21e-20

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: 88.86  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNAS-QVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLT---- 76
Cdd:cd06320    12 PFWVAMKDGIEAEAKKLGVKVDvQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKKGIPVINldda 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  77 -NESPGQPSANWDIEII--DNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEhYPDMhEVTRRMP 153
Cdd:cd06320    92 vDADALKKAGGKVTSFIgtDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKK-APGL-KLVASQP 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 154 VAESVDDSRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASA 233
Cdd:cd06320   170 ADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTGKVLVVGTDGIPEAKKSIKAGELTATVAQYPYLE 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1629933285 234 GYALAAVASTLLKGEEIKPGLemqnlgkadvdmdkriirFHKVLLVNKDNID 285
Cdd:cd06320   250 GAMAVEAALRLLQGQKVPAVV------------------ATPQALITKDNVD 283
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
2-252 1.26e-20

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: 88.89  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGpSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESpg 81
Cdd:cd06305    12 DWDQQALQGAVAEAEKLGGTVIVFD-ANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAGIPVVTFDT-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 qPSANWDIEII--DNEKFAAEYVEHMAKRMGGKGGyVIYVGSLTVPQHNLWADLLVKYQKEHYPDMHEVTRRMPVAESV- 158
Cdd:cd06305    89 -DSQVPGVNNItqDDYALGTLSLGQLVKDLNGEGN-IAVFNVFGVPPLDKRYDIYKAVLKANPGIKKIVAELGDVTPNTa 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 159 DDSRRTTLDLMKTYPD--LKAVVSFGSNGPIGAGRAVKEKrAKNKVAVYGMMIPSQAASL-IKSGDITEG-ITYDPASAG 234
Cdd:cd06305   167 ADAQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEA-GRTDIKVYGVDISNQDLELmADEGSPWVAtAAQDPALIG 245
                         250
                  ....*....|....*...
gi 1629933285 235 YALAAVASTLLKGEEIKP 252
Cdd:cd06305   246 TVAVRNVARKLAGEDLPD 263
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
2-284 3.70e-20

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


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 87.80  E-value: 3.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNAsQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI-VVLTNesP 80
Cdd:cd06319    12 PFWQIMERGVQAAAEELGYEF-VTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIpVVIAD--I 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  81 GQPSANWDIEII-DNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADL----LVKYQKEhyPDMHEVTRRMPVA 155
Cdd:cd06319    89 GTGGGDYVSYIIsDNYDGGYQAGEYLAEALKENGWGGGSVGIIAIPQSRVNGQArtagFEDALEE--AGVEEVALRQTPN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 156 ESVDDSRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGY 235
Cdd:cd06319   167 STVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGDILVVGFDGDPEALDLIKDGKLDGTVAQQPFGMGA 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1629933285 236 ALAAVASTLLKGEEIkpglemqnlgkadvdmDKRIIRFHkVLLVNKDNI 284
Cdd:cd06319   247 RAVELAIQALNGDNT----------------VEKEIYLP-VLLVTSENV 278
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
29-249 4.72e-20

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


Pssm-ID: 380534 [Multi-domain]  Cd Length: 270  Bit Score: 87.04  E-value: 4.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  29 STDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVlTNESPGQPSANWDIEII-DNEKFAAEYVEHMAK 107
Cdd:cd06311    38 SSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPV-VNFDRGLNVLIYDLYVAgDNPGMGVVSAEYIGK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 108 RMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHYPDMheVTRRMPVAESVDDSRRTTLDLMKTYPDLKAVVSFGSNGPI 187
Cdd:cd06311   117 KLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNPGIK--ILAMQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAI 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1629933285 188 GAGRAVKE-KRAKNKVAVYGMmiPSQAA-SLIKSGD--ITEGITYDPASAGYALaAVASTLLKGEE 249
Cdd:cd06311   195 GVLQAIKEaGRTDIKVMTGGG--GSQEYfKRIMDGDpiWPASATYSPAMIADAI-KLAVLILKGGK 257
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
9-252 6.74e-20

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


Pssm-ID: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 86.90  E-value: 6.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   9 EGVVEAGKAFGVNASQVGPSS-TDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKArDAGIVVLTNESPgqpsANW 87
Cdd:cd20008    19 KGAEKAAKELGVEVTFLGPATeADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAA-DAGIPVVLVDSG----ANT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  88 DIEI----IDNEKFAAEYVEHMAKRM---GGKGGYVIYVGSLTVPQHNLwaDLL---VKYQKEHYPDMHEVTRRmPVAES 157
Cdd:cd20008    94 DDYDaflaTDNVAAGALAADELAELLkasGGGKGKVAIISFQAGSQTLV--DREegfRDYIKEKYPDIEIVDVQ-YSDGD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 158 VDDSRRTTLDLMKTYPDLKAVvsFGSNGP--IGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGY 235
Cdd:cd20008   171 IAKALNQTTDLLTANPDLVGI--FGANNPsaVGVAQALAEAGKAGKIVLVGFDSSPDEVALLKSGVIKALVVQDPYQMGY 248
                         250
                  ....*....|....*..
gi 1629933285 236 ALAAVASTLLKGEEIKP 252
Cdd:cd20008   249 EGVKTAVKALKGEEIVE 265
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
3-252 4.45e-19

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


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 84.74  E-value: 4.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   3 WFNRMGEGVVEAGKAFGVNASQVGPSStDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESP-- 80
Cdd:cd06317    13 FFNQINQGAQAAAKDLGVDLVVFNAND-DPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAVip 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  81 -GQPSANWDIEIIDNEKFAAEYV-EHMAKRMGGKG--GYVIYVGSL-TVPQHNLWADLLVKYQKEHYPDMHEVTRRMPVA 155
Cdd:cd06317    92 sDFQAAQVGVDNLEGGKEIGKYAaDYIKAELGGQAkiGVVGALSSLiQNQRQKGFEEALKANPGVEIVATVDGQNVQEKA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 156 ESVDDsrrttlDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGM-MIPSQAASLIKSGDITEGITYDPASAG 234
Cdd:cd06317   172 LSAAE------NLLTANPDLDAIYATGEPALLGAVAAVRSQGRQGKIKVFGWdLTKQAIFLGIDEGVLQAVVQQDPEKMG 245
                         250
                  ....*....|....*...
gi 1629933285 235 YALAAVASTLLKGEEIKP 252
Cdd:cd06317   246 YEAVKAAVKAIKGEDVEK 263
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
2-248 2.16e-16

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: 77.27  E-value: 2.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQ-QVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESP 80
Cdd:cd20004    12 DFWKSVKAGAEKAAQELGVEIYWRGPSREDDVEaQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDSD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  81 GQPSAnwDIEII--DNEKFAAEYVEHMAKRMGGKGGYVIY---VGSLTVPQHnlwADLLVKYQKEHYPDMHEVTRRMpVA 155
Cdd:cd20004    92 LGGDA--VISFVatDNYAAGRLAAKRMAKLLNGKGKVALLrlaKGSASTTDR---ERGFLEALKKLAPGLKVVDDQY-AG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 156 ESVDDSRRTTLDLMKTYPDLKAVvsFGSNGP--IGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASA 233
Cdd:cd20004   166 GTVGEARSSAENLLNQYPDVDGI--FTPNESttIGALRALRRLGLAGKVKFIGFDASDLLLDALRAGEISALVVQDPYRM 243
                         250
                  ....*....|....*..
gi 1629933285 234 GY--ALAAVAstLLKGE 248
Cdd:cd20004   244 GYlgVKTAVA--ALRGK 258
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
2-252 3.91e-16

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: 76.68  E-value: 3.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASqvgpsSTDA----PQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTN 77
Cdd:cd06318    12 PYYAALVAAAKAEAKKLGVELV-----VTDAqndlTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGIPVITV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  78 ESPGQPSANWDIEI-IDNEKFAAEYVEHMAKRMGGKGGYVIYV-GSL--TVPQHNLWADL--LVKYQKEHYPDMHEVTRR 151
Cdd:cd06318    87 DSALDPSANVATQVgRDNKQNGVLVGKEAAKALGGDPGKIIELsGDKgnEVSRDRRDGFLagVNEYQLRKYGKSNIKVVA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 152 MPVAESVDDSRRTTL-DLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDP 230
Cdd:cd06318   167 QPYGNWIRSGAVAAMeDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVKVAGADGQKEALKLIKDGKYVATGLNDP 246
                         250       260
                  ....*....|....*....|..
gi 1629933285 231 ASAGYALAAVASTLLKGEEIKP 252
Cdd:cd06318   247 DLLGKTAVDTAAKVVKGEESFP 268
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
3-253 8.58e-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: 75.81  E-value: 8.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   3 WFNRMGEGVVEAG---KAFGVNAS-QVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNE 78
Cdd:cd19999    13 WRAQMIADFEEVAaeyKEEGVISDlIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  79 spgQPSANWDIE--IIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQhnlwADLLVKYQKE---HYPDMhEVTRRMP 153
Cdd:cd19999    93 ---QPVSSPDAInvVIDQYKWAAIQAQWLAEQLGGKGNIVAINGVAGNPA----NEARVKAADDvfaKYPGI-KVLASVP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 154 VAESVDDSRRTTLDLMKTYPDLKAVVSFGSNGPiGAGRAVKEKRAKNKV----AVYGMMipSQAASLIKSGDITEGITYD 229
Cdd:cd19999   165 GGWDQATAQQVMATLLATYPDIDGVLTQDGMAE-GVLRAFQAAGKDPPVmtgdYRKGFL--RKWKELDLPDFESIGVVNP 241
                         250       260
                  ....*....|....*....|....
gi 1629933285 230 PASAGYALaAVASTLLKGEEIKPG 253
Cdd:cd19999   242 PGIGATAL-RIAVRLLQGKELKED 264
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
2-256 1.17e-15

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


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 74.98  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGK-AFGVN-ASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLT--N 77
Cdd:cd19970    12 EFFIEMEKGARKHAKeANGYElLVKGIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINidN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  78 ESPGQPSANWDIEI----IDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEHypDMHEVTRRMP 153
Cdd:cd19970    92 RLDADALKEGGINVpfvgPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAFEEA--GMKIVASQSA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 154 VAEsVDDSRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASA 233
Cdd:cd19970   170 NWE-IDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGKVLVVGFDNIPAVRPLLKDGKMLATIDQHPAKQ 248
                         250       260
                  ....*....|....*....|...
gi 1629933285 234 GYALAAVASTLLKGEEIkPGLEM 256
Cdd:cd19970   249 AVYGIEYALKMLNGEEV-PGWVK 270
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
31-252 1.69e-15

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


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 74.54  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPGQpsanwDIEII------DNekFAAEYV-- 102
Cdd:cd19971    40 DQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPVK-----DTDLVdstiasDN--YNAGKLcg 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 103 EHMAKRMGGKGGYVIyvgsLTVPQHNLWADLLVKYQKE--HYPDMhEVTRRMPVAESVDDSRRTTLDLMKTYPDLKAVvs 180
Cdd:cd19971   113 EDMVKKLPEGAKIAV----LDHPTAESCVDRIDGFLDAikKNPKF-EVVAQQDGKGQLEVAMPIMEDILQAHPDLDAV-- 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1629933285 181 FGSNGP--IGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVASTLLKGEEIKP 252
Cdd:cd19971   186 FALNDPsaLGALAALKAAGKLGDILVYGVDGSPDAKAAIKDGKMTATAAQSPIEIGKKAVETAYKILNGEKVEK 259
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
2-252 2.98e-15

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: 73.86  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSST-DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESP 80
Cdd:cd06321    12 PFFVAMVRGAEEAAAEINPGAKVTVVDARyDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVVAVDVA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  81 GQPSanwDIEIIDNEKFAAEYV-EHMAKRMGGKGGYVIYVGsltvPQHNLWADLLVKYQKE--HYPDMhEVTRRMPVAES 157
Cdd:cd06321    92 AEGA---DATVTTDNVQAGYLAcEYLVEQLGGKGKVAIIDG----PPVSAVIDRVNGCKEAlaEYPGI-KLVDDQNGKGS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 158 VDDSRRTTLDLMKTYPDLKAVvsFGSNGP--IGAGRAVKEkRAKNKVAVYGMMIPSQAASLIKSGD--ITEGITYDPASA 233
Cdd:cd06321   164 RAGGLSVMTRMLTAHPDVDGV--FAINDPgaIGALLAAQQ-AGRDDIVITSVDGSPEAVAALKREGspFIATAAQDPYDM 240
                         250
                  ....*....|....*....
gi 1629933285 234 GYALAAVASTLLKGEEIKP 252
Cdd:cd06321   241 ARKAVELALKILNGQEPAP 259
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
2-222 3.09e-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: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 73.81  E-value: 3.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAItIVPN-DANVLEPVFKKARDAGIVVLTNESP 80
Cdd:cd06312    13 PFWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQARLIEQAIAAKPDGI-IVTIpDPDALEPALKRAVAAGIPVIAINSG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  81 GQPSANwDIEII----DNEKFAAEYVEHMAKRMGGKGGYVIyvgsLTVPQH-NL------WADLLvkyQKEHYPdmhevT 149
Cdd:cd06312    92 DDRSKE-RLGALtyvgQDEYLAGQAAGERALEAGPKNALCV----NHEPGNpGLearckgFADAF---KGAGIL-----V 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1629933285 150 RRMPVAESVDDSRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDI 222
Cdd:cd06312   159 ELLDVGGDPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKVKIGTFDLSPETLEAIKDGKI 231
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
5-252 3.62e-15

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: 73.90  E-value: 3.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   5 NRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPgqPS 84
Cdd:cd06300    19 ASLKADAAQSGQKGLVKELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGA--VT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  85 ANWDIEIIDNEKFAAEYV-EHMAKRMGGKGGYVIYVGsltVPQHNLWADLLVKYQK--EHYPDMHEVTRrmpVAESVDDS 161
Cdd:cd06300    97 SPDAYNVSNDQVEWGRLGaKWLFEALGGKGNVLVVRG---IAGAPASADRHAGVKEalAEYPGIKVVGE---VFGGWDEA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 162 --RRTTLDLMKTYPDLKAVVSFGSNGpIGAGRAVKEkRAKNKVAVYGMMIPSQAASLIKSGDI--TEGITYDPASAGYAL 237
Cdd:cd06300   171 taQTAMLDFLATHPQVDGVWTQGGED-TGVLQAFQQ-AGRPPVPIVGGDENGFAKQWWKHPKKglTGAAVWPPPAIGAAG 248
                         250
                  ....*....|....*
gi 1629933285 238 AAVASTLLKGEEIKP 252
Cdd:cd06300   249 LEVALRLLEGQGPKP 263
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
2-249 4.69e-15

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: 73.51  E-value: 4.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGpSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI-VVLTN-ES 79
Cdd:cd19967    12 PFFVVEAEGAKEKAKELGYEVTVFD-HQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIpVFLIDrEI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  80 PGQPSANWDIeIIDNEKFAAEYVEHMAKRMGGKGGYVIYVGSLTvpQHNLWadllVKYQKEH-----YPDMhevtrRMPV 154
Cdd:cd19967    91 NAEGVAVAQI-VSDNYQGAVLLAQYFVKLMGEKGLYVELLGKES--DTNAQ----LRSQGFHsvidqYPEL-----KMVA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 155 AESVDDSRRTTLDLM----KTYPDLKAVvsFGSNGP--IGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITY 228
Cdd:cd19967   159 QQSADWDRTEAFEKMesilQANPDIKGV--ICGNDEmaLGAIAALKAAGRAGDVIIVGFDGSNDVRDAIKEGKISATVLQ 236
                         250       260
                  ....*....|....*....|.
gi 1629933285 229 DPASAGYALAAVASTLLKGEE 249
Cdd:cd19967   237 PAKLIARLAVEQADQYLKGGS 257
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
2-250 5.49e-15

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: 73.10  E-value: 5.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNAsQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESpg 81
Cdd:cd06323    12 PFFVSLKDGAQAEAKELGVEL-VVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDR-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  82 qpSANwDIEII-----DNEKFAAEYVEHMAKRMGGKGGYVIYVGsltVPQHNLWADLLVKYQK--EHYPDMHEVTRrmpv 154
Cdd:cd06323    89 --SVT-GGKVVshiasDNVAGGEMAAEYIAKKLGGKGKVVELQG---IPGTSAARERGKGFHNaiAKYPKINVVAS---- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 155 aESVDDSRRTTLDLMK----TYPDLKAVVSFGSNGPIGAGRAVKEkRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDP 230
Cdd:cd06323   159 -QTADFDRTKGLNVMEnllqAHPDIDAVFAHNDEMALGAIQALKA-AGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQP 236
                         250       260
                  ....*....|....*....|
gi 1629933285 231 ASAGYALAAVASTLLKGEEI 250
Cdd:cd06323   237 EEMGAKAVETADKYLKGEKV 256
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
31-250 5.90e-15

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: 73.03  E-value: 5.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI-VVLTNESPGQPSANWDIEIIDNEKFAAEYVEHMAKRM 109
Cdd:cd06301    42 DAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIpLVYVNREPDSKPKGVAFVGSDDIESGELQMEYLAKLL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 110 GGKGGYVIYVGsltVPQHNlwADLL----VKYQKEHYPDMHEVTRrmpvaESVDDSRRTTLDLM----KTYPDLKAVVSF 181
Cdd:cd06301   122 GGKGNIAILDG---VLGHE--AQILrtegNKDVLAKYPGMKIVAE-----QTANWSREKAMDIVenwlQSGDKIDAIVAN 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1629933285 182 GSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVASTLLKGEEI 250
Cdd:cd06301   192 NDEMAIGAILALEAAGKKDDILVAGIDATPDALKAMKAGRLDATVFQDAAGQGETAVDVAVKAAKGEEV 260
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
31-251 1.70e-14

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: 71.81  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI--VVLTNESPGqpsANWDIEI-IDNEKFAAEYVEHMAK 107
Cdd:cd06308    41 DAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIpvIVLDRKVSG---DDYTAFIgADNVEIGRQAGEYIAE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 108 RMGGKGGYVIYVG----SLTVPQHNLWADLLVKyqkehYPDMHEVTRRmPVAESVDDSRRTTLDLMKTYPDLKAVVSFGS 183
Cdd:cd06308   118 LLNGKGNVVEIQGlpgsSPAIDRHKGFLEAIAK-----YPGIKIVASQ-DGDWLRDKAIKVMEDLLQAHPDIDAVYAHND 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1629933285 184 NGPIGAGRAVKEKRAKNKVAVYGM-MIPSQAASLIKSGDITEGITYDpaSAGYALAAVASTLLKGEEIK 251
Cdd:cd06308   192 EMALGAYQALKKAGREKEIKIIGVdGLPEAGEKAVKDGILAATFLYP--TGGKEAIEAALKILNGEKVP 258
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
2-112 4.35e-14

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: 70.96  E-value: 4.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVN-ASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESP 80
Cdd:cd19973    12 PFFVKMKEGAQKAAKALGIKlMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVLVIALDTP 91
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1629933285  81 GQPSANWDIEIIDNEKFAAEYVEHMAK-RMGGK 112
Cdd:cd19973    92 TDPIDAADATFATDNFKAGVLIGEWAKaALGAK 124
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
2-235 4.60e-14

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


Pssm-ID: 380620 [Multi-domain]  Cd Length: 272  Bit Score: 70.38  E-value: 4.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI-VVLTN-ES 79
Cdd:cd19965    12 PFFQPVKKGMDDACELLGAECQFTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIpVVAFNvDA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  80 PGQPSAnwDIEIIDNEKFAAEYV--EHMAKRMGGKGGYVIyvGSLTVPQHNlW----ADLLVKYQKEHYPDmhEVTRRMP 153
Cdd:cd19965    92 PGGENA--RLAFVGQDLYPAGYVlgKRIAEKFKPGGGHVL--LGISTPGQS-AleqrLDGIKQALKEYGRG--ITYDVID 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 154 VAESVDDSRRTTLDLMKTYPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASA 233
Cdd:cd19965   165 TGTDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGKVLVGGFDLVPEVLQGIKAGYIDFTIDQQPYLQ 244

                  ..
gi 1629933285 234 GY 235
Cdd:cd19965   245 GF 246
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
4-258 5.62e-14

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: 70.16  E-value: 5.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   4 FNRMGEGVVEAGKAFGVNASQVGpSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI-VVLTNESPgq 82
Cdd:cd19972    14 FNQIKQSVEAEAKKKGYKVITVD-AKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIpVIAVDRNP-- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  83 PSANWDIEI-IDNEKFAAEYVEHMAKRMGGKGGYVIYVGSL-TVPQHNL---WADLLVKyqkehYPDMhEVTRRMPVAES 157
Cdd:cd19972    91 EDAPGDTFIaTDSVAAAKELGEWVIKQTGGKGEIAILHGQLgTTPEVDRtkgFQEALAE-----APGI-KVVAEQTADWD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 158 VDDSRRTTLDLMKTYPDLKAVvsFG-SNGP-IGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGY 235
Cdd:cd19972   165 QDEGFKVAQDMLQANPNITVF--FGqSDAMaLGAAQAVKVAGLDHKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKMGR 242
                         250       260
                  ....*....|....*....|...
gi 1629933285 236 ALAAVASTLLKGEEIkPGLEMQN 258
Cdd:cd19972   243 LAVDSAIDLLNGKAV-PKEQLQD 264
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
2-252 6.52e-14

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: 70.33  E-value: 6.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGV-----NASQvgpsstDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI-VVL 75
Cdd:cd06309    12 PWRVANTKSIKEAAKKRGYelvytDANQ------DQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIpVIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  76 TNES-PGQPSANWDIEIIDNE----KFAAEYVehmAKRMGGKGGYVIyvgSLTVPQHNLWADLLVKYQKE---HYPDMHE 147
Cdd:cd06309    86 VDRTiDGEDGSLYVTFIGSDFveegRRAAEWL---VKNYKGGKGNVV---ELQGTAGSSVAIDRSKGFREvikKHPNIKI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 148 VTRRmPVAESVDDSRRTTLDLMKTYP-DLKAVVSFGSNGPIGAGRAVKE--KRAKNKVAVYGMMIPSQAASLIKSGDITE 224
Cdd:cd06309   160 VASQ-SGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEagLKPGKDVLVVGIDGQKDALEAIKAGELNA 238
                         250       260
                  ....*....|....*....|....*...
gi 1629933285 225 GITYDPASAGYALAAVAsTLLKGEEIKP 252
Cdd:cd06309   239 TVECNPLFGPTAFDTIA-KLLAGEKVPK 265
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
31-195 1.75e-12

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


Pssm-ID: 380651 [Multi-domain]  Cd Length: 302  Bit Score: 66.11  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI-VVLTNESPGqpSANWDIEI-IDNEKFAAEYVEHMAKR 108
Cdd:cd19996    43 DTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIpVVLFDSGVG--SDKYTAFVgVDDAAFGRVGAEWLVKQ 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 109 MGGKGGYVIYVGSLTVPQHNLWADLLVKYQKEhYPDMHEVTRRmpVAE-SVDDSRRTTLDLMKTYPDLKAVVSFGSNGPI 187
Cdd:cd19996   121 LGGKGNIIALRGIAGVSVSEDRWAGAKEVFKE-YPGIKIVGEV--YADwDYAKAKQAVESLLAAYPDIDGVWSDGGAMTL 197

                  ....*...
gi 1629933285 188 GAGRAVKE 195
Cdd:cd19996   198 GAIEAFEE 205
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
28-288 6.14e-12

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


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 64.60  E-value: 6.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  28 SSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI-VVLTNESpgqpsanwdieiIDNEKFAAeYV---- 102
Cdd:cd06313    37 GNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAGIpLVGVNAL------------IENEDLTA-YVgsdd 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 103 --------EHMAKRMGGKGGYVIYVG----SLTVPQHNLWADLLVKyqkehYPDMhEVTRRMPVAESVDDSRRTTLDLMK 170
Cdd:cd06313   104 vvagelegQAVADRLGGKGNVVILEGpigqSAQIDRGKGIENVLKK-----YPDI-KVLAEQTANWSRDEAMSLMENWLQ 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 171 TYPD-LKAVVSFGSNGPIGAGRAVKEkRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVASTLLKGEE 249
Cdd:cd06313   178 AYGDeIDGIIAQNDDMALGALQAVKA-AGRDDIPVVGIDGIEDALQAVKSGELIATVLQDAEAQGKGAVEVAVDAVKGEG 256
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1629933285 250 IKPglemqnlgKADVDMdkriirfhkvLLVNKDNIDSLY 288
Cdd:cd06313   257 VEK--------KYYIPF----------VLVTKDNVDDYL 277
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
2-249 1.53e-11

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


Pssm-ID: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 63.41  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGI--VVLTNES 79
Cdd:cd06316    12 DWSRLQVAGIKDTFEELGIEVVAVTDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIklVFMDNVP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  80 PGQPSANWDIEII--DNE---KFAAEYvehMAKRMGGKGgyviYVGSLTvpqHNlwADLLVKYQ---------KEHYPDM 145
Cdd:cd06316    92 DGLEAGKDYVSVVssDNRgngQIAAEL---LAEAIGGKG----KVGIIY---HD--ADFYATNQrdkafkdtlKEKYPDI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 146 HEVTRRmpVAESVDDSRRTTLDLMKTYPDLKAV-VSFGSNGpIGAGRAVKEKRAKNkVAVYGMMIPSQAASLIKSGDITE 224
Cdd:cd06316   160 KIVAEQ--GFADPNDAEEVASAMLTANPDIDGIyVSWDTPA-LGVISALRAAGRSD-IKITTVDLGTEIALDMAKGGNVK 235
                         250       260
                  ....*....|....*....|....*.
gi 1629933285 225 GITYD-PASAGYALAAVASTLLKGEE 249
Cdd:cd06316   236 GIGAQrPYDQGVAEALAAALALLGKE 261
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
31-119 3.61e-11

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


Pssm-ID: 380652 [Multi-domain]  Cd Length: 305  Bit Score: 62.31  E-value: 3.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPGQPSANWDIEiIDNEKFAAEYVEHMAKRMG 110
Cdd:cd19997    45 SATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGVTEPCAYILN-NDFEDYGAASVEYVADRLG 123

                  ....*....
gi 1629933285 111 GKGGyVIYV 119
Cdd:cd19997   124 GKGN-VLEV 131
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
31-265 1.35e-10

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: 60.71  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNEspgQPSANWDIEI---IDNEKFAAEYVEHMAK 107
Cdd:cd19991    40 DDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYD---RLILNADVDLyvsFDNEKVGELQAEALVK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 108 rMGGKGGYVIYVGSLTvpQHNlwADLLVKYQKE---HYPDMHEVTRrmpVAESV--DDSRRTTLDLMKTY-----PDLKA 177
Cdd:cd19991   117 -AKPKGNYVLLGGSPT--DNN--AKLFREGQMKvlqPLIDSGDIKV---VGDQWvdDWDPEEALKIMENAltannNKIDA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 178 VVSfgSNGPI--GAGRAVKEKRAKNKVAVYGmmipsQAASLIKSGDITEGI----TYDP-ASAGYALAAVASTLLKGEEI 250
Cdd:cd19991   189 VIA--SNDGTagGAIQALAEQGLAGKVAVSG-----QDADLAACQRIVEGTqtmtIYKPiKELAEKAAELAVALAKGEKN 261
                         250
                  ....*....|....*
gi 1629933285 251 KPGLEMQNlGKADVD 265
Cdd:cd19991   262 EANRTINN-GKKEVP 275
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
28-251 6.67e-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: 380653 [Multi-domain]  Cd Length: 302  Bit Score: 58.84  E-value: 6.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  28 SSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPGQPSANWDIEiIDNEKFAAEYVEHMAK 107
Cdd:cd19998    41 SGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVVDEPCAYNVN-TDQAKAGEQTAQWLVD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 108 RMGGKGGYVIYVG----SLTVPQHNLWADLLVKyqkehYPDMHEVTRrmpVAESVDD--SRRTTLDLMKTYPDLKAVVSF 181
Cdd:cd19998   120 KLGGKGNILMVRGvpgtSVDRDRYEGAKEVFKK-----YPDIKVVAE---YYGNWDDgtAQKAVADALAAHPDVDGVWTQ 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1629933285 182 GsnGPIGAGRAVKEkrAKNKVAVY------GMMIPSQAASLIKSGDITEGitYDPASAGYAL-AAVAstLLKGEEIK 251
Cdd:cd19998   192 G--GETGVIKALQA--AGHPLVPVggeaenGFRKAMLEPLANGLPGISAG--SPPALSAVALkLAVA--VLEGEKEP 260
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
1-76 1.37e-08

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: 54.70  E-value: 1.37e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1629933285   1 MPWFNRMGEGVVEAGKAFGVNAsQVGPSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLT 76
Cdd:cd19968    11 FPFFVYMHEQAVDEAAKLGVKL-VVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAGIPVVT 85
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
30-265 1.68e-08

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


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 54.51  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  30 TDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESpGQPSANWDIEI-IDNEKFAAEYVEHMAKr 108
Cdd:cd19992    39 NDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDR-LILNADVDLYVgRDNYKVGQLQAEYALE- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 109 MGGKGGYVIYVG----SLTVPQHNLWADLLvkyqkEHYPDMHEVTrrmPVAE------SVDDSRRTTLD-LMKTYPDLKA 177
Cdd:cd19992   117 AVPKGNYVILSGdpgdNNAQLITAGAMDVL-----QPAIDSGDIK---IVLDqyvkgwSPDEAMKLVENaLTANNNNIDA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 178 VVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVASTLLKGEEIKPGLEMQ 257
Cdd:cd19992   189 VLAPNDGMAGGAIQALKAQGLAGKVFVTGQDAELAALKRIVEGTQTMTVWKDLKELARAAADAAVKLAKGEKPQTTDETI 268

                  ....*...
gi 1629933285 258 NLGKADVD 265
Cdd:cd19992   269 NNGGKDVP 276
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
31-123 1.94e-08

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 54.37  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVV-----LTNESPGqpsanwDIEII-DNEKFA---AEY 101
Cdd:COG4213    43 DVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPViaydrLILNSDV------DYYVSfDNVKVGelqGQY 116
                          90       100
                  ....*....|....*....|...
gi 1629933285 102 -VEHMAKRmgGKGGYVIYVGSLT 123
Cdd:COG4213   117 lVDGLPLK--GKGNIELFGGSPT 137
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
10-254 1.25e-07

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: 51.81  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  10 GVVEAGKAFGVNAS--QVGpSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVV--LTN--ESP--- 80
Cdd:cd06306    20 GIVDEAKRLGVKLTvyEAG-GYTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVidLVNgiDSPkva 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  81 GQPSANWDieiiDNEKFAAEYvehMAKRMGGKGGYVIYV-GsltvPQHNLWADLLVKYQKEHY--PDMHEVTRRMPvaes 157
Cdd:cd06306    99 ARVLVDFY----DMGYLAGEY---LVEHHPGKPVKVAWFpG----PAGAGWAEDREKGFKEALagSNVEIVATKYG---- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 158 vDDSRRTTLDLM----KTYPDLKAVVsfGSNGPI-GAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPAS 232
Cdd:cd06306   164 -DTGKAVQLNLVedalQAHPDIDYIV--GNAVAAeAAVGALREAGLTGKVKVVSTYLTPGVYRGIKRGKILAAPSDQPVL 240
                         250       260
                  ....*....|....*....|..
gi 1629933285 233 AGYALAAVASTLLKGEEIKPGL 254
Cdd:cd06306   241 QGRIAVDQAVRALEGKPVPKHV 262
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
5-261 5.30e-07

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: 49.73  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   5 NRMGEGVVEAGKAFGVNASQvgpssTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNEspgQPS 84
Cdd:cd01538    19 DIMVEQLEEKGAKVLVQSAD-----GDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYD---RLI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  85 ANWDIEI---IDNEKFAAEYVEHMAKRMGGkGGYVIYVGSLTVPQhnlwADLLVKYQKEHYPDMHEVTRRMPVAES-VDD 160
Cdd:cd01538    91 LNADVDYyisFDNEKVGELQAQALLDAKPE-GNYVLIGGSPTDNN----AKLFRDGQMKVLQPAIDSGKIKVVGDQwVDD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 161 -SRRTTLDLMKT-----YPDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAG 234
Cdd:cd01538   166 wLPANAQQIMENaltanGNNVDAVVASNDGTAGGAIAALKAQGLSGGVPVSGQDADLAAIKRILAGTQTMTVYKDIRLLA 245
                         250       260
                  ....*....|....*....|....*..
gi 1629933285 235 YALAAVASTLLKGEEIKPGLEMQNLGK 261
Cdd:cd01538   246 DAAAEVAVALMRGEKPPINGTTNNGLK 272
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
29-252 2.34e-06

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


Pssm-ID: 380530 [Multi-domain]  Cd Length: 275  Bit Score: 47.94  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  29 STDAPQQVKIIEDLiARKVNAITIVPNDAN-VLEPVfKKARDAGI-VV-LTNESPGQPSANWdieI-IDNEK---FAAEY 101
Cdd:cd06307    42 SLDPEALAAALRRL-AAGCDGVALVAPDHPlVRAAI-DELAARGIpVVtLVSDLPGSRRLAY---VgIDNRAagrTAAWL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 102 VEHMAKRMGGKGGyvIYVGSLTVPQHNL----WADLLvkyqKEHYPDmHEVTRRMPVAESVDDSRRTTLDLMKTYPDLKA 177
Cdd:cd06307   117 MGRFLGRRPGKVL--VILGSHRFRGHEEreagFRSVL----RERFPD-LTVLEVLEGLDDDELAYELLRELLARHPDLVG 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1629933285 178 VVSFGSnGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGY-ALAAVASTLLKGEEIKP 252
Cdd:cd06307   190 IYNAGG-GNEGIARALREAGRARRVVFIGHELTPETRRLLRDGTIDAVIDQDPELQARrAIEVLLAHLGGKGPAPP 264
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
2-114 7.66e-06

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: 46.51  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGpSSTDAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNespg 81
Cdd:cd01540    12 PWFQDEWKGAKKAAKELGFEVIKID-AKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAGIPVIAV---- 86
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1629933285  82 qpsanwDIEIID-NEKFAAEYVEHMAKRMGGKGG 114
Cdd:cd01540    87 ------DDQLVDaDPMKIVPFVGIDAYKIGEAVG 114
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
2-109 2.34e-04

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: 41.93  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285   2 PWFNRMGEGVVEAGKAFGVNASQVGpSSTDAPQQVKIIEDLIARKVNAITIV-PNDANVLEPVFKKARDAGIVVLT--NE 78
Cdd:cd19966    13 PFWTVVYNGAKDAAADLGVDLDYVF-SSWDPEKMVEQFKEAIAAKPDGIAIMgHPGDGAYTPLIEAAKKAGIIVTSfnTD 91
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1629933285  79 SPGQPSANWDIEIIDNEKFAAEYVehMAKRM 109
Cdd:cd19966    92 LPKLEYGDCGLGYVGADLYAAGYT--LAKEL 120
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
31-250 9.47e-04

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: 40.15  E-value: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPGQPSANWDIEiIDNekfaAEYVEHMAK--- 107
Cdd:cd19993    40 SAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDRLIENPIAFYIS-FDN----VEVGRMQARgvl 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 108 RMGGKGGYVIYVGSLTVPQhnlwADLLVKYQKEHYPDMHEVTRRMPVAESVDDS-------RRTTLDLMKTYPDLKAVVS 180
Cdd:cd19993   115 KAKPEGNYVFIKGSPTDPN----ADFLRAGQMEVLQPAIDSGKIKIVGEQYTDGwkpanaqKNMEQILTANNNKVDAVVA 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 181 FGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVASTLLKGEEI 250
Cdd:cd19993   191 SNDGTAGGAVAALAAQGLAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKGTKI 260
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
31-123 2.30e-03

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


Pssm-ID: 380649 [Multi-domain]  Cd Length: 304  Bit Score: 38.77  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNES--PGQPSANWDIEiIDNEKFA---AEYVEHM 105
Cdd:cd19994    40 DVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYDRliMNTDAVDYYVT-FDNEKVGelqGQYLVDK 118
                          90       100
                  ....*....|....*....|
gi 1629933285 106 AKRMGGKGGYVIYV--GSLT 123
Cdd:cd19994   119 LGLKDGKGPFNIELfaGSPD 138
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
31-286 4.56e-03

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 38.18  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNEspgQPSANWDIEI---IDNEKFAAEYVEHMAK 107
Cdd:PRK10355   66 NEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYD---RMINNADIDFyisFDNEKVGELQAKALVD 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 108 RMgGKGGYVIYVGSltvPQHNLwADLLVKYQkehypdmhevtrrMPVAESVDDSRR---------------TTLDLMKTY 172
Cdd:PRK10355  143 KV-PQGNYFLMGGS---PVDNN-AKLFRAGQ-------------MKVLKPYIDSGKikvvgdqwvdgwlpeNALKIMENA 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 173 -----PDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGmmipsQAASLIKSGDITEG----ITYDPASAGYALAA-VAS 242
Cdd:PRK10355  205 ltannNKIDAVVASNDATAGGAIQALSAQGLSGKVAISG-----QDADLAAIKRIVAGtqtmTVYKPITKLANTAAeIAV 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1629933285 243 TLLKGEEIKPGLEMQNlGKADVDMdkriiRFHKVLLVNKDNIDS 286
Cdd:PRK10355  280 ELGNGEEPKANTTLNN-GLKDVPS-----RLLTPIDVNKNNIDS 317
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
31-268 5.51e-03

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


Pssm-ID: 380650 [Multi-domain]  Cd Length: 294  Bit Score: 37.65  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285  31 DAPQQVKIIEDLIARKVNAITIVPNDANVLEPVFKKARDAGIVVLTNESPGQpSANWDIEII-DNE---KFAAEYVEHMA 106
Cdd:cd19995    43 DASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLIL-GGPADYYVSfDNVavgEAQAQSLVDHL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 107 KRMGGKGGYVIYV-GSLTVP--------QHN----LWADLLVKYQKEHY-PDMHEVTRRMpvaeSVDDSrrttldLMKTY 172
Cdd:cd19995   122 KAIGKKGVNIVMInGSPTDNnaglfkkgAHEvldpLGDSGELKLVCEYDtPDWDPANAQT----AMEQA------LTKLG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1629933285 173 PDLKAVVSFGSNGPIGAGRAVKEKRAKNKVAVYGMMIPSQAASLIKSGDITEGITYDPASAGYALAAVASTLLKGEeiKP 252
Cdd:cd19995   192 NNIDGVLSANDGLAGGAIAALKAQGLAGKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGE--TP 269
                         250
                  ....*....|....*.
gi 1629933285 253 GLEMQNlGKADVDMDK 268
Cdd:cd19995   270 PSDLVT-GTVTNGGDK 284
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH