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Conserved domains on  [gi|1177747929|gb|ORC45330|]
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rhamnose ABC transporter substrate-binding protein [Burkholderia sp. A27]

Protein Classification

rhamnose ABC transporter substrate-binding protein( domain architecture ID 14448388)

rhamnose ABC transporter substrate-binding protein functions as the initial receptor in the transport of sugar substrates like the methyl-pentose rhamnose; a periplasmic binding component of ABC transporter complex (RhaSTPQ)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
34-331 1.81e-172

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: 480.60  E-value: 1.81e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd20000     1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKPEYSKIKLV 193
Cdd:cd20000    81 GIKVVTFDSDVAPEARDLFVNQADADGIGRAQVDMMAELIGGEGEFAILSATPTATNQNAWIDAMKKELASPEYAGMKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWD 273
Cdd:cd20000   161 KVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGKVKVTGLGLPSEMAKYVKDGTVPAFALWN 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1177747929 274 PNQLGYLAGYAAASLASGAITGKEGESFDAGKLGKRTIGPQGEIILGPPTTFDSSNID 331
Cdd:cd20000   241 PIDLGYLAAYAAAALAQGEITGKEGETFTAGRLGEYTVGEGGEVVLGPPFVFTADNID 298
 
Name Accession Description Interval E-value
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
34-331 1.81e-172

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: 480.60  E-value: 1.81e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd20000     1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKPEYSKIKLV 193
Cdd:cd20000    81 GIKVVTFDSDVAPEARDLFVNQADADGIGRAQVDMMAELIGGEGEFAILSATPTATNQNAWIDAMKKELASPEYAGMKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWD 273
Cdd:cd20000   161 KVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGKVKVTGLGLPSEMAKYVKDGTVPAFALWN 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1177747929 274 PNQLGYLAGYAAASLASGAITGKEGESFDAGKLGKRTIGPQGEIILGPPTTFDSSNID 331
Cdd:cd20000   241 PIDLGYLAAYAAAALAQGEITGKEGETFTAGRLGEYTVGEGGEVVLGPPFVFTADNID 298
RhaS TIGR02637
rhamnose ABC transporter, rhamnose-binding protein; This sugar-binding component of ABC ...
35-335 2.18e-141

rhamnose ABC transporter, rhamnose-binding protein; This sugar-binding component of ABC transporter complexes is found in rhamnose catabolism operon contexts. Mutation of this gene in Rhizobium leguminosarum abolishes rhamnose transport and prevents growth on rhamnose as a carbon source.


Pssm-ID: 131685  Cd Length: 302  Bit Score: 401.93  E-value: 2.18e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  35 IAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVV-GPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:TIGR02637   1 IGLVVKSLGNPFFEAANKGAEEAAKELGSVYIIYtGPTGTTAEGQIEVVNSLIAQKVDAIAISANDPDALVPALKKAMKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKPEYSKIKLV 193
Cdd:TIGR02637  81 GIKVVTWDSGVAPEGRNLFLNQASADLIGRTQVQLAAEQIGNGGEIAILSAASTATNQNAWIEIMKKELKDPKYPKVKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWD 273
Cdd:TIGR02637 161 ATVYGDDDAQKSYQEAQGLLKSYPNLKGIIAPTTVGIKAAAQAVSDAKLIGKVKLTGLGLPSEMAKYVKNGTVKAFALWN 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1177747929 274 PNQLGYLAGYAAASLASGAITGKEGESFDAGKLGKRTIGPQGEIILGPPTTFDSSNIDNFNF 335
Cdd:TIGR02637 241 PIDLGYSAAYTAYRLSSGEITGKPGETFKAGRMGEYTIGDNGVAALGPPFVFDADNIDQFSK 302
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
12-335 2.67e-64

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 206.57  E-value: 2.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  12 ALCVALVAISCAASAaglknglKIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQD 91
Cdd:PRK15408   10 ALGIALISMTVQAAE-------RIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  92 AIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGE-GEFAVLSATPNATN 170
Cdd:PRK15408   83 AIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMAAKQVGKDkAKVAFFYSSPTVTD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 171 QNTWIKWMQEELKKpEYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARyISSSSSKGKVAVTG 250
Cdd:PRK15408  163 QNQWVKEAKAKIAK-EHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQ-AAENLKRDKVAIVG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 251 LGTPNQMRAFVKNGTVKAFQLWDPNQLGYLAGYAAASLASGAITgKEGESFDAGKLGKRTIGP---QGE--------IIL 319
Cdd:PRK15408  241 FSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLKKGKL-NVGDSLDVPGIGKVEVSPnsvQGYdyeakgngIVL 319
                         330
                  ....*....|....*..
gi 1177747929 320 GPP-TTFDSSNIDNFNF 335
Cdd:PRK15408  320 LPErVVFTKENIDKYDF 336
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
35-291 6.52e-64

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: 203.31  E-value: 6.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  35 IAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQG 114
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 115 IKVVTFDSDtAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpEYSKIKLVK 194
Cdd:pfam13407  81 IPVVTFDSD-APSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKE-KYPGIKVVA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 195 IAYGNDDDQ-KSFVETQGLLQAYPN-LKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLW 272
Cdd:pfam13407 159 EVEGTNWDPeKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVLQ 238
                         250
                  ....*....|....*....
gi 1177747929 273 DPNQLGYLAGYAAASLASG 291
Cdd:pfam13407 239 DPYGQGYAAVELAAALLKG 257
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
6-291 1.17e-62

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: 201.69  E-value: 1.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929   6 RHTGTAALCVALVAISC----AASAAGLKNGLKIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVgPSDAGASSQVQY 81
Cdd:COG1879     3 LALLAAVLALALALAACgsaaAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVV-DAEGDAAKQISQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  82 INTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQLFVNQaNAEGIGRGQIQLVSKLIGGEGEFAV 161
Cdd:COG1879    82 IEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGS-DNYAAGRLAAEYLAKALGGKGKVAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 162 LSATPNATNQNTWIKWMQEELKkpEYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSS 241
Cdd:COG1879   161 LTGSPGAPAANERTDGFKEALK--EYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAG 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1177747929 242 SKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWDPNQLGYLAGYAAASLASG 291
Cdd:COG1879   239 RKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKG 288
 
Name Accession Description Interval E-value
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
34-331 1.81e-172

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: 480.60  E-value: 1.81e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd20000     1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKPEYSKIKLV 193
Cdd:cd20000    81 GIKVVTFDSDVAPEARDLFVNQADADGIGRAQVDMMAELIGGEGEFAILSATPTATNQNAWIDAMKKELASPEYAGMKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWD 273
Cdd:cd20000   161 KVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGKVKVTGLGLPSEMAKYVKDGTVPAFALWN 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1177747929 274 PNQLGYLAGYAAASLASGAITGKEGESFDAGKLGKRTIGPQGEIILGPPTTFDSSNID 331
Cdd:cd20000   241 PIDLGYLAAYAAAALAQGEITGKEGETFTAGRLGEYTVGEGGEVVLGPPFVFTADNID 298
RhaS TIGR02637
rhamnose ABC transporter, rhamnose-binding protein; This sugar-binding component of ABC ...
35-335 2.18e-141

rhamnose ABC transporter, rhamnose-binding protein; This sugar-binding component of ABC transporter complexes is found in rhamnose catabolism operon contexts. Mutation of this gene in Rhizobium leguminosarum abolishes rhamnose transport and prevents growth on rhamnose as a carbon source.


Pssm-ID: 131685  Cd Length: 302  Bit Score: 401.93  E-value: 2.18e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  35 IAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVV-GPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:TIGR02637   1 IGLVVKSLGNPFFEAANKGAEEAAKELGSVYIIYtGPTGTTAEGQIEVVNSLIAQKVDAIAISANDPDALVPALKKAMKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKPEYSKIKLV 193
Cdd:TIGR02637  81 GIKVVTWDSGVAPEGRNLFLNQASADLIGRTQVQLAAEQIGNGGEIAILSAASTATNQNAWIEIMKKELKDPKYPKVKLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWD 273
Cdd:TIGR02637 161 ATVYGDDDAQKSYQEAQGLLKSYPNLKGIIAPTTVGIKAAAQAVSDAKLIGKVKLTGLGLPSEMAKYVKNGTVKAFALWN 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1177747929 274 PNQLGYLAGYAAASLASGAITGKEGESFDAGKLGKRTIGPQGEIILGPPTTFDSSNIDNFNF 335
Cdd:TIGR02637 241 PIDLGYSAAYTAYRLSSGEITGKPGETFKAGRMGEYTIGDNGVAALGPPFVFDADNIDQFSK 302
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
34-331 5.99e-110

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: 321.92  E-value: 5.99e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd20003     1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVDVTYDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpEYSKIKLV 193
Cdd:cd20003    81 GIKVVTWDSDVNPDARDFFVNQATPEGIGKTLVDMVAEQTGEKGKVAIVTSSPTATNQNAWIKAMKAYIAE-KYPDMKIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWD 273
Cdd:cd20003   160 TTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTGKVAVTGLSTPNVMRPYVKDGTVKSVVLWD 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 274 PNQLGYLAGYAAASLASGAITgKEGESFDAGKLGKRTIGPQ--GEIILGPPTTFDSSNID 331
Cdd:cd20003   240 VVDLGYLAVYVARALADGTLL-KVGDFFVAGRLGTFTVVPKgnGIILLGEPLIFTKENID 298
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
34-331 6.24e-108

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: 316.88  E-value: 6.24e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd06302     1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpEYSKIKLV 193
Cdd:cd06302    81 GIKVITWDSDAPPSARDYFVNQADDEGLGEALVDSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKS-KYPDIELV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWD 273
Cdd:cd06302   160 DTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGKVAVTGIGLPNTARPYLKDGSVKEGVLWD 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1177747929 274 PNQLGYLAGYAAASLASGAITGKEGESFDAGKLGKRTIGPqGEIILGPPTTFDSSNID 331
Cdd:cd06302   240 PAKLGYLTVYAAYQLLKGKGFTEDSDDVGTGGKVKVDVAG-GEILLGPPLVFTKDNVD 296
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
12-335 2.67e-64

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 206.57  E-value: 2.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  12 ALCVALVAISCAASAaglknglKIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQD 91
Cdd:PRK15408   10 ALGIALISMTVQAAE-------RIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  92 AIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGE-GEFAVLSATPNATN 170
Cdd:PRK15408   83 AIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMAAKQVGKDkAKVAFFYSSPTVTD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 171 QNTWIKWMQEELKKpEYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARyISSSSSKGKVAVTG 250
Cdd:PRK15408  163 QNQWVKEAKAKIAK-EHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQ-AAENLKRDKVAIVG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 251 LGTPNQMRAFVKNGTVKAFQLWDPNQLGYLAGYAAASLASGAITgKEGESFDAGKLGKRTIGP---QGE--------IIL 319
Cdd:PRK15408  241 FSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLKKGKL-NVGDSLDVPGIGKVEVSPnsvQGYdyeakgngIVL 319
                         330
                  ....*....|....*..
gi 1177747929 320 GPP-TTFDSSNIDNFNF 335
Cdd:PRK15408  320 LPErVVFTKENIDKYDF 336
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
35-291 6.52e-64

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: 203.31  E-value: 6.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  35 IAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQG 114
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 115 IKVVTFDSDtAPEGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpEYSKIKLVK 194
Cdd:pfam13407  81 IPVVTFDSD-APSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKE-KYPGIKVVA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 195 IAYGNDDDQ-KSFVETQGLLQAYPN-LKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLW 272
Cdd:pfam13407 159 EVEGTNWDPeKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVLQ 238
                         250
                  ....*....|....*....
gi 1177747929 273 DPNQLGYLAGYAAASLASG 291
Cdd:pfam13407 239 DPYGQGYAAVELAAALLKG 257
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
6-291 1.17e-62

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: 201.69  E-value: 1.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929   6 RHTGTAALCVALVAISC----AASAAGLKNGLKIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVgPSDAGASSQVQY 81
Cdd:COG1879     3 LALLAAVLALALALAACgsaaAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVV-DAEGDAAKQISQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  82 INTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQLFVNQaNAEGIGRGQIQLVSKLIGGEGEFAV 161
Cdd:COG1879    82 IEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGS-DNYAAGRLAAEYLAKALGGKGKVAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 162 LSATPNATNQNTWIKWMQEELKkpEYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSS 241
Cdd:COG1879   161 LTGSPGAPAANERTDGFKEALK--EYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAG 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1177747929 242 SKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWDPNQLGYLAGYAAASLASG 291
Cdd:COG1879   239 RKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKG 288
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
34-331 2.90e-48

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: 164.03  E-value: 2.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd20002     1 TIVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPeGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpEYSKIKLV 193
Cdd:cd20002    81 GIVVITHESPGQK-GADWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKE-KYPNMKQV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAY-GNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLW 272
Cdd:cd20002   159 TDRIpGGEDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGLKGKVAVVGTVIPSQAAAYLKEGSITEGYLW 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1177747929 273 DPNQlgylAGYAAASLASGAITGKEGESFDAGK-LGKRTIGPQGEII-LGPPTTFDSSNID 331
Cdd:cd20002   239 DPAD----AGYAMVYIAKMLLDGKRKEIGDGFEiPGKGTPDIDGNVIiFDAPLEITKENAD 295
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
34-300 3.75e-48

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: 163.60  E-value: 3.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd20001     1 TIAVVVKVTGIAWFDRMETGVEQFAKDTGVNVYQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFdsdtapEGRQL---------FVNqanaEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKK 184
Cdd:cd20001    81 GIVVITH------EASNLknvdydveaFDN----AAYGAFIMDKLAEAMGGKGKYVTFVGSLTSTSHMEWANAAVAYQKA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 185 pEYSKIKLV-KIAYGNDDDQKSFVETQGLLQAYPNLKAIV---APTTVGIAAAaryISSSSSKGKVAVTGLGTPNQMRAF 260
Cdd:cd20001   151 -NYPDMLLVtDRVETNDDSETAYEKAKELLKTYPDLKGIVgcsSSDVPGAARA---VEELGLQGKIAVVGTGLPSVAGEY 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1177747929 261 VKNGTVKAFQLWDPNqlgyLAGYAAASLASGAITGKEGES 300
Cdd:cd20001   227 LEDGTIDYIQFWDPA----DAGYAMNALAVMVLEGEKITD 262
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
34-281 7.06e-47

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: 159.67  E-value: 7.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd06314     1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLV 193
Cdd:cd06314    81 GIPVITFDSDAPDSKRLAYIGTDNYEA-GREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKG--SPGIEIV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWD 273
Cdd:cd06314   158 DPLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVIAATVGQR 237

                  ....*...
gi 1177747929 274 PNQLGYLA 281
Cdd:cd06314   238 PYEMGYLS 245
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
34-291 1.47e-41

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: 145.79  E-value: 1.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAgASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd01536     1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGD-VAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSD-TAPEGRQLFVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKL 192
Cdd:cd01536    80 GIPVVAVDTDiDGGGDVVAFVGTDNYEA-GKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKK--YPDIEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 193 VKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLW 272
Cdd:cd01536   157 VAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGDIKIVGVDGTPEALKAIKDGELDATVAQ 236
                         250
                  ....*....|....*....
gi 1177747929 273 DPNQLGYLAGYAAASLASG 291
Cdd:cd01536   237 DPYLQGYLAVEAAVKLLNG 255
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
34-281 2.76e-35

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: 129.38  E-value: 2.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGP-SDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMS 112
Cdd:cd06310     1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPeSEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 113 QGIKVVTFDSDTAPEGRQLFVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpEYSKIKL 192
Cdd:cd06310    81 KGIPVIVIDSGIKGDAYLSYIATDNYAA-GRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKK-HPGGIKV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 193 VKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLW 272
Cdd:cd06310   159 LASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIVGFDSQEELLDALKNGKIDALVVQ 238

                  ....*....
gi 1177747929 273 DPNQLGYLA 281
Cdd:cd06310   239 NPYEIGYEG 247
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
34-291 1.35e-34

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: 127.33  E-value: 1.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEV--IADDGGMAAIKEFGGVGKVVGP-SDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKA 110
Cdd:cd20006     1 KIALILKSSDPNSDFwqTVKSGAEAAAKEYGVDLEFLGPeSEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 111 MSQGIKVVTFDSDTAPEGRQLFVNQANAEgIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKkpEYSKI 190
Cdd:cd20006    81 KKAGIPVITIDSPVNSKKADSFVATDNYE-AGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQALA--EYPNI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 191 KLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVA---PTTVGiaaAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVK 267
Cdd:cd20006   158 KIVETEYCDSDEEKAYEITKELLSKYPDINGIVAlneQSTLG---AARALKELGLGGKVKVVGFDSSVEEIQLLEEGIID 234
                         250       260
                  ....*....|....*....|....
gi 1177747929 268 AFQLWDPNQLGYLAGYAAASLASG 291
Cdd:cd20006   235 ALVVQNPFNMGYLSVQAAVDLLNG 258
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
34-301 5.12e-34

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: 125.81  E-value: 5.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd20007     1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQGPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSD-TAPEGRQLFVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKL 192
Cdd:cd20007    81 GIKVVTVDTTlGDPSFVLSQIASDNVAG-GALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMKK--YPGIKV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 193 VKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLW 272
Cdd:cd20007   158 LGVQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGKVKVVGFDASPAQVEQLKAGTIDALIAQ 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 1177747929 273 DPNQLGYLAG-YAAASLASGAITGKEGESF 301
Cdd:cd20007   238 KPAEIGYLAVeQAVAALTGKPVPKDILTPF 267
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
52-291 8.06e-34

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: 125.43  E-value: 8.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  52 DGGMAAIKEFGGVGKVVGPSDAGA-SSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQ 130
Cdd:cd20005    19 KGAEQAAKELGVKITFEGPDTESDvDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGVPSDLPL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 131 LFV--NQANAEGIGRGQIQlvsKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpEYSKIKLVKIAYGNDDDQKSFVE 208
Cdd:cd20005    99 ATVatDNYAAGALAADHLA---ELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKE-KYPDIKVVNVQYGVGDHAKAADI 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 209 TQGLLQAYPNLKAIVA---PTTVGIAAAaryISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQLWDPNQLGYLAGYAA 285
Cdd:cd20005   175 AKAILQANPDLKGIYAtneGAAIGVANA---LKEMGKLGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAA 251

                  ....*.
gi 1177747929 286 ASLASG 291
Cdd:cd20005   252 VKALKG 257
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
56-268 2.08e-33

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: 124.37  E-value: 2.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  56 AAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQLFVNQ 135
Cdd:cd19969    23 DAGAELGVKTEYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSDAPESKRISYVGT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 136 ANaEGIGRGQIQLVSKLIGGEGEFAVLSaTPNATNQNTWIKWMQEELKkpEYSKIKLVKIAYGNDDDQKSFVETQGLLQA 215
Cdd:cd19969   103 DN-YEAGYAAAEKLAELLGGKGKVAVLT-GPGQPNHEERVEGFKEAFA--EYPGIEVVAVGDDNDDPEKAAQNTSALLQA 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1177747929 216 YPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKA 268
Cdd:cd19969   179 HPDLVGIFGVDASGGVGAAQAVREAGKTGKVKIVAFDDDPETLDLIKDGVIDA 231
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
34-304 1.39e-32

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: 122.34  E-value: 1.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSD-AGASSQVQYINTLITQRQDAIVIAANDANAVVPyLKKAMS 112
Cdd:cd20008     1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPATeADIAGQVNLVENAISRKPDAIVLAPNDTAALVP-AVEAAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 113 QGIKVVTFDSDTAPEGRQLFV---NQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpEYSK 189
Cdd:cd20008    80 AGIPVVLVDSGANTDDYDAFLatdNVAAGALAADELAELLKASGGGKGKVAIISFQAGSQTLVDREEGFRDYIKE-KYPD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 190 IKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVA---PTTVGIAAAaryISSSSSKGKVAVTGLGTPNQMRAFVKNGTV 266
Cdd:cd20008   159 IEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGannPSAVGVAQA---LAEAGKAGKIVLVGFDSSPDEVALLKSGVI 235
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1177747929 267 KAFQLWDPNQLGYLAGYAAASLASGaiTGKEGESFDAG 304
Cdd:cd20008   236 KALVVQDPYQMGYEGVKTAVKALKG--EEIVEKNVDTG 271
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
34-291 2.07e-27

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: 108.09  E-value: 2.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSD-AGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMS 112
Cdd:cd20004     1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPSReDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 113 QGIKVVTFDSDTAPEGRQLFVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNatNQNTwikwMQ------EELKKpE 186
Cdd:cd20004    81 QGIPVVIIDSDLGGDAVISFVATDNYAA-GRLAAKRMAKLLNGKGKVALLRLAKG--SAST----TDrergflEALKK-L 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 187 YSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAP---TTVGIAAAARyisSSSSKGKVAVTGLGTPNQMRAFVKN 263
Cdd:cd20004   153 APGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPnesTTIGALRALR---RLGLAGKVKFIGFDASDLLLDALRA 229
                         250       260
                  ....*....|....*....|....*...
gi 1177747929 264 GTVKAFQLWDPNQLGYLAGYAAASLASG 291
Cdd:cd20004   230 GEISALVVQDPYRMGYLGVKTAVAALRG 257
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
34-291 1.12e-23

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: 98.14  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGgVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd06323     1 TIGLSVSTLNNPFFVSLKDGAQAEAKELG-VELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLV 193
Cdd:cd06323    80 GIPVITVDRSVTGGKVVSHIASDNVAG-GEMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAK--YPKINVV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKgKVAVTGL-GTPNQMRAfVKNGTVKAFQLW 272
Cdd:cd06323   157 ASQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRK-DVIVVGFdGTPDAVKA-VKDGKLAATVAQ 234
                         250
                  ....*....|....*....
gi 1177747929 273 DPNQLGYLAGYAAASLASG 291
Cdd:cd06323   235 QPEEMGAKAVETADKYLKG 253
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
43-268 5.95e-21

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: 90.68  E-value: 5.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  43 NNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDS 122
Cdd:cd06308    10 NDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVLDR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 123 DTAPEGRQLFVNQANAEgIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLVKIAYGNDDD 202
Cdd:cd06308    90 KVSGDDYTAFIGADNVE-IGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAK--YPGIKIVASQDGDWLR 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1177747929 203 QKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGL-GTPNQMRAFVKNGTVKA 268
Cdd:cd06308   167 DKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKEIKIIGVdGLPEAGEKAVKDGILAA 233
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
34-297 9.48e-19

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: 84.61  E-value: 9.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVV--GPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAM 111
Cdd:cd19970     1 KVALVMKSLANEFFIEMEKGARKHAKEANGYELLVkgIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 112 SQGIKVVTFDS---DTAPEGRQL---FVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNATN----QNTWIKWMQEe 181
Cdd:cd19970    81 DAGIAVINIDNrldADALKEGGInvpFVGPDNRQG-AYLAGDYLAKKLGKGGKVAIIEGIPGADNaqqrKAGFLKAFEE- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 182 lkkpeySKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFV 261
Cdd:cd19970   159 ------AGMKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGKVLVVGFDNIPAVRPLL 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1177747929 262 KNGTVKAfqlwDPNQLGYLAGYAAASLASGAITGKE 297
Cdd:cd19970   233 KDGKMLA----TIDQHPAKQAVYGIEYALKMLNGEE 264
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
44-291 3.58e-18

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


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 82.71  E-value: 3.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  44 NPYEVIADDGGMAAIKEFGGVGKVVGPsDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSD 123
Cdd:cd06322    11 HPFFVDIKDAMKKEAAELGVKVVVADA-NGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFTVDVK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 124 TAPEGRQLFVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLVKIAYGNDDDQ 203
Cdd:cd06322    90 ADGAKVVTHVGTDNYAG-GKLAGEYALKALLGGGGKIAIIDYPEVESVVLRVNGFKEAIKK--YPNIEIVAEQPGDGRRE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 204 KSFVETQGLLQAYPNLKAIVA---PTTVGIAAAaryISSSSSKGKVAVTGL-GTPNQMRAFVKNGTVKAFQLWDPNQLGY 279
Cdd:cd06322   167 EALAATEDMLQANPDLDGIFAigdPAALGALTA---IESAGKEDKIKVIGFdGNPEAIKAIAKGGKIKADIAQQPDKIGQ 243
                         250
                  ....*....|..
gi 1177747929 280 LAGYAAASLASG 291
Cdd:cd06322   244 ETVEAIVKYLAG 255
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
34-283 5.07e-18

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: 82.32  E-value: 5.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd19965     1 KFVFVTHVTTNPFFQPVKKGMDDACELLGAECQFTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTF--DSDTAPEGRQLFVNQaNAEGIGR--GQiQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKPEYsK 189
Cdd:cd19965    81 GIPVVAFnvDAPGGENARLAFVGQ-DLYPAGYvlGK-RIAEKFKPGGGHVLLGISTPGQSALEQRLDGIKQALKEYGR-G 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 190 IKLVKIAYGNDDDQ-----KSFvetqglLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNG 264
Cdd:cd19965   158 ITYDVIDTGTDLAEalsriEAY------YTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGKVLVGGFDLVPEVLQGIKAG 231
                         250
                  ....*....|....*....
gi 1177747929 265 TVKaFQLwdpNQLGYLAGY 283
Cdd:cd19965   232 YID-FTI---DQQPYLQGF 246
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
52-292 8.86e-18

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: 82.04  E-value: 8.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  52 DGGMAAIKEFGGVGKVVGPSDAgASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQL 131
Cdd:cd06317    19 QGAQAAAKDLGVDLVVFNANDD-PSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAVIPSDFQAA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 132 FVNQANAEG---IGRGQIQLVSKLIGGEGEFAVLSATpNATNQNTWIKWMQEELKkpEYSKIKLVKIAYGNDDDQKSFVE 208
Cdd:cd06317    98 QVGVDNLEGgkeIGKYAADYIKAELGGQAKIGVVGAL-SSLIQNQRQKGFEEALK--ANPGVEIVATVDGQNVQEKALSA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 209 TQGLLQAYPNLKAIVA---PTTVGIAAAARyisSSSSKGKVAVTGL-GTPNQMRAFVKNGTVKAFQLWDPNQLGYLAGYA 284
Cdd:cd06317   175 AENLLTANPDLDAIYAtgePALLGAVAAVR---SQGRQGKIKVFGWdLTKQAIFLGIDEGVLQAVVQQDPEKMGYEAVKA 251

                  ....*...
gi 1177747929 285 AASLASGA 292
Cdd:cd06317   252 AVKAIKGE 259
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
75-291 6.18e-17

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


Pssm-ID: 380651 [Multi-domain]  Cd Length: 302  Bit Score: 79.98  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  75 ASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSdtAPEGRQL--FVNQANAEgIGRGQIQLVSKL 152
Cdd:cd19996    44 TQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDS--GVGSDKYtaFVGVDDAA-FGRVGAEWLVKQ 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 153 IGGEGEFAVLSATPNATNQNTWIKWMQEELKkpEYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVA---PTTVG 229
Cdd:cd19996   121 LGGKGNIIALRGIAGVSVSEDRWAGAKEVFK--EYPGIKIVGEVYADWDYAKAKQAVESLLAAYPDIDGVWSdggAMTLG 198
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1177747929 230 IA----AAARYIssssskgkVAVTGLGTPNQMRAFVKNGTVKAFQLWDPNQLGYLAGYAAASLASG 291
Cdd:cd19996   199 AIeafeEAGRPL--------VPMTGEDNNGFLKAWKELPGFKSIAPSYPPWLGATALDAALAALEG 256
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
34-291 9.52e-17

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: 78.99  E-value: 9.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIAddggMAAIKEFG---GVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKA 110
Cdd:cd06318     1 KIGFSQRTLASPYYAAL----VAAAKAEAkklGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 111 MSQGIKVVTFDSDTAPEGRQLFVNQANAEGIGRGQIQLVSKLIGG-EGEFAVLSATPNAT----NQNTWIKWMQEE-LKK 184
Cdd:cd06318    77 KAAGIPVITVDSALDPSANVATQVGRDNKQNGVLVGKEAAKALGGdPGKIIELSGDKGNEvsrdRRDGFLAGVNEYqLRK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 185 PEYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNG 264
Cdd:cd06318   157 YGKSNIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVKVAGADGQKEALKLIKDG 236
                         250       260
                  ....*....|....*....|....*..
gi 1177747929 265 TVKAFQLWDPNQLGYLAGYAAASLASG 291
Cdd:cd06318   237 KYVATGLNDPDLLGKTAVDTAAKVVKG 263
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
55-239 2.74e-16

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: 78.13  E-value: 2.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  55 MAAIKEFGGVGKV----VGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSD-TAPEGR 129
Cdd:cd06300    22 KADAAQSGQKGLVkeliVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGAvTSPDAY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 130 QLFVNQANAegiGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKkpEYSKIKLVKIAYGNDDDQKSFVET 209
Cdd:cd06300   102 NVSNDQVEW---GRLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEALA--EYPGIKVVGEVFGGWDEATAQTAM 176
                         170       180       190
                  ....*....|....*....|....*....|
gi 1177747929 210 QGLLQAYPNLKAIVAPTTVGIAAAARYISS 239
Cdd:cd06300   177 LDFLATHPQVDGVWTQGGEDTGVLQAFQQA 206
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
67-222 3.20e-15

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


Pssm-ID: 380654 [Multi-domain]  Cd Length: 313  Bit Score: 75.04  E-value: 3.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  67 VVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGrQLFVNQANAEgIGRGQI 146
Cdd:cd19999    38 IVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPVSSPD-AINVVIDQYK-WAAIQA 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1177747929 147 QLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAI 222
Cdd:cd19999   116 QWLAEQLGGKGNIVAINGVAGNPANEARVKAADDVFAK--YPGIKVLASVPGGWDQATAQQVMATLLATYPDIDGV 189
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
34-264 3.81e-15

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


Pssm-ID: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 74.35  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGgVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd19968     1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLG-VKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLV 193
Cdd:cd19968    80 GIPVVTVDRRAEGAAPVPHVGADNVAG-GREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAA--GPKIKVV 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYPN-LKAIVAPTTVGIAAAARYISSSS-SKGKVAVTGL-GTPNQMRAfVKNG 264
Cdd:cd19968   157 FEQTGNFERDEGLTVMENILTSLPGpPDAIICANDDMALGAIEAMRAAGlDLKKVKVIGFdAVPDALQA-IKDG 229
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
34-291 4.71e-15

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


Pssm-ID: 380543 [Multi-domain]  Cd Length: 283  Bit Score: 74.22  E-value: 4.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFG-GVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMS 112
Cdd:cd06320     1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGvKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 113 QGIKVVTFDSDTAPEGRQLFVNQA------NAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpe 186
Cdd:cd06320    81 KGIPVINLDDAVDADALKKAGGKVtsfigtDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKK-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 187 YSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGL-GTPnQMRAFVKNGT 265
Cdd:cd06320   159 APGLKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTGKVLVVGTdGIP-EAKKSIKAGE 237
                         250       260
                  ....*....|....*....|....*.
gi 1177747929 266 VKAFQLWDPNQLGYLAGYAAASLASG 291
Cdd:cd06320   238 LTATVAQYPYLEGAMAVEAALRLLQG 263
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
55-331 5.41e-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: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 74.20  E-value: 5.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  55 MAAIK-EFGGVG-KVVGPSDAG--ASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFdsDTAPEGrq 130
Cdd:cd06316    18 VAGIKdTFEELGiEVVAVTDANfdPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKLVFM--DNVPDG-- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 131 lFVNQ--------ANAEGIGRGQIQLVSKLIGGEGEFAVLSATPN--ATNQ--NTWIKWMqeelkKPEYSKIKLVKIAyG 198
Cdd:cd06316    94 -LEAGkdyvsvvsSDNRGNGQIAAELLAEAIGGKGKVGIIYHDADfyATNQrdKAFKDTL-----KEKYPDIKIVAEQ-G 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 199 NDDDQKSFVETQGLLQAYPNLKAIVAPTTV---GIAAAARyiSSSSSKGKVAVTGLGTPNQMrAFVKNGTVKAFQlwdpN 275
Cdd:cd06316   167 FADPNDAEEVASAMLTANPDIDGIYVSWDTpalGVISALR--AAGRSDIKITTVDLGTEIAL-DMAKGGNVKGIG----A 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1177747929 276 QLGYLAGYAAASLASGAITGKEGESFdagklgkrtigpqgeiILGPPTTFDSSNID 331
Cdd:cd06316   240 QRPYDQGVAEALAAALALLGKEVPPF----------------IGVPPLAVTKDNLL 279
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
34-291 1.59e-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: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 72.23  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVgpsDAGASS--QVQYINTLITQRQDAIVIAANDANAVVPYLKKAM 111
Cdd:cd19971     1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITR---DPQLDQnkQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 112 SQGIKVVTFDSDTA-PEGRQLFV--NQANAegigrGQI---QLVSKLIGGeGEFAVLSaTPNATNQNTWIKWMQEELKKp 185
Cdd:cd19971    78 EAGIPVINVDTPVKdTDLVDSTIasDNYNA-----GKLcgeDMVKKLPEG-AKIAVLD-HPTAESCVDRIDGFLDAIKK- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 186 eYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVA---PTTVGIAAAaryISSSSSKGKVAVTGL-GTPnQMRAFV 261
Cdd:cd19971   150 -NPKFEVVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFAlndPSALGALAA---LKAAGKLGDILVYGVdGSP-DAKAAI 224
                         250       260       270
                  ....*....|....*....|....*....|
gi 1177747929 262 KNGTVKAFQLWDPNQLGYLAGYAAASLASG 291
Cdd:cd19971   225 KDGKMTATAAQSPIEIGKKAVETAYKILNG 254
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
75-305 7.07e-14

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: 70.69  E-value: 7.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  75 ASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSdtAPEGRQ--LFVNQANAEgIGRGQIQLVSKL 152
Cdd:cd19992    41 AKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDR--LILNADvdLYVGRDNYK-VGQLQAEYALEA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 153 IgGEGEFAVLSATPNATN----QNTWIKWMQeelKKPEYSKIKLVKIAYGND---DDQKSFVETqGLLQAYPNLKAIVAP 225
Cdd:cd19992   118 V-PKGNYVILSGDPGDNNaqliTAGAMDVLQ---PAIDSGDIKIVLDQYVKGwspDEAMKLVEN-ALTANNNNIDAVLAP 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 226 TTvGIA-AAARYISSSSSKGKVAVTGL-GTPNQMRAFVkNGTVKAFQLWDPNQLGYLAGYAAASLASGAITGKEGESFDA 303
Cdd:cd19992   193 ND-GMAgGAIQALKAQGLAGKVFVTGQdAELAALKRIV-EGTQTMTVWKDLKELARAAADAAVKLAKGEKPQTTDETINN 270

                  ..
gi 1177747929 304 GK 305
Cdd:cd19992   271 GG 272
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
43-297 1.03e-13

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: 70.01  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  43 NNPYEVIADDGGMAAIKEFGGVGKVVgPSDAGASS--QVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTF 120
Cdd:cd06321    10 GNPFFVAMVRGAEEAAAEINPGAKVT-VVDARYDLakQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVVAV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 121 dsDTAPEGRQLFVNQANaegIGRGQI---QLVSKLiGGEGEFAVLSATPNATNQNTwIKWMQEELKkpEYSKIKLVKIAY 197
Cdd:cd06321    89 --DVAAEGADATVTTDN---VQAGYLaceYLVEQL-GGKGKVAIIDGPPVSAVIDR-VNGCKEALA--EYPGIKLVDDQN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 198 GNDDDQKSFVETQGLLQAYPNLKAIVA---PTTVGIAAAARyissSSSKGKVAVTGL-GTPNQMRAF-VKNGTVKAFQLW 272
Cdd:cd06321   160 GKGSRAGGLSVMTRMLTAHPDVDGVFAindPGAIGALLAAQ----QAGRDDIVITSVdGSPEAVAALkREGSPFIATAAQ 235
                         250       260
                  ....*....|....*....|....*
gi 1177747929 273 DPnqlgYLAGYAAASLASGAITGKE 297
Cdd:cd06321   236 DP----YDMARKAVELALKILNGQE 256
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
33-291 1.13e-13

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: 69.95  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  33 LKIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMS 112
Cdd:cd06301     1 IKIGVSMQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 113 QGIKVVTFDSDT--APEGrQLFVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKI 190
Cdd:cd06301    81 AGIPLVYVNREPdsKPKG-VAFVGSDDIES-GELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAK--YPGM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 191 KLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGL-GTPNQMRAfVKNGTVKAF 269
Cdd:cd06301   157 KIVAEQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDDILVAGIdATPDALKA-MKAGRLDAT 235
                         250       260
                  ....*....|....*....|..
gi 1177747929 270 QLWDPNQLGYLAGYAAASLASG 291
Cdd:cd06301   236 VFQDAAGQGETAVDVAVKAAKG 257
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
34-297 1.33e-13

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: 69.66  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVGpSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd19967     1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFD-HQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSdtapegrqlfvnQANAEGIGRGQI------------QLVSKLIGGEGEFAVLSATPNATNqnTWIKWMQEE 181
Cdd:cd19967    80 GIPVFLIDR------------EINAEGVAVAQIvsdnyqgavllaQYFVKLMGEKGLYVELLGKESDTN--AQLRSQGFH 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 182 LKKPEYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVA---PTTVGIAAAaryISSSSSKGKVAVTGLGTPNQMR 258
Cdd:cd19967   146 SVIDQYPELKMVAQQSADWDRTEAFEKMESILQANPDIKGVICgndEMALGAIAA---LKAAGRAGDVIIVGFDGSNDVR 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1177747929 259 AFVKNGTVKAFQLWDPNQLGYLAGYAAASLASGAITGKE 297
Cdd:cd19967   223 DAIKEGKISATVLQPAKLIARLAVEQADQYLKGGSTGKE 261
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
52-291 3.20e-13

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


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 68.62  E-value: 3.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  52 DGGMAAIKEFGGvgKVVGPSDAG-ASSQVQYINTLITQRQDAIV-IAANDANAVVPyLKKAMSQGIKVVTFDSDtaPEGR 129
Cdd:cd19972    19 QSVEAEAKKKGY--KVITVDAKGdSATQVNQIQDLITQNIDALIyIPAGATAAAVP-VKAARAAGIPVIAVDRN--PEDA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 130 QL--FV---NQANAEGIGRgqiqLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKkpEYSKIKLVKIAYGNDDDQK 204
Cdd:cd19972    94 PGdtFIatdSVAAAKELGE----WVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALA--EAPGIKVVAEQTADWDQDE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 205 SFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGL-GTPNQMRAfVKNGTVKAFQLWDPNQLGYLAGY 283
Cdd:cd19972   168 GFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDHKIWVVGFdGDVAGLKA-VKDGVLDATMTQQTQKMGRLAVD 246

                  ....*...
gi 1177747929 284 AAASLASG 291
Cdd:cd19972   247 SAIDLLNG 254
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
51-307 5.55e-13

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: 68.27  E-value: 5.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  51 DDGGMAAIKEFGGVgKVVGpSDAGASSQVQY--INTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSdTAPEG 128
Cdd:cd19993    17 DEAAMKKALEKAGA-KYIS-ADAQSSAEKQLddIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDR-LIENP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 129 RQLFVNQANAEgIGRGQIQLVSKLIgGEGEFAVLSATPNATNQNTWIKWMQEELKKP-EYSKIKLVKIAY--GNDDDQKS 205
Cdd:cd19993    94 IAFYISFDNVE-VGRMQARGVLKAK-PEGNYVFIKGSPTDPNADFLRAGQMEVLQPAiDSGKIKIVGEQYtdGWKPANAQ 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 206 FVETQGLLQAYPNLKAIVAPT--TVGIAAAAryISSSSSKGKVAVTGL-GTPNQMRAFVKnGTVKAFQLWDPNQLGYLAG 282
Cdd:cd19993   172 KNMEQILTANNNKVDAVVASNdgTAGGAVAA--LAAQGLAGKVPVSGQdADKAALNRIAL-GTQTVTVWKDARELGKEAA 248
                         250       260
                  ....*....|....*....|....*..
gi 1177747929 283 YAAASLASG-AITG-KEGESFDAGKLG 307
Cdd:cd19993   249 EIAVELAKGtKIEAiKGAALTNDGPKK 275
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
56-233 1.02e-12

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: 67.39  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  56 AAIKEFGGVG-KVVGPSDAGasSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQLFVN 134
Cdd:cd06311    23 KQAKELADLEyKLVTSSNAN--EQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYDLYVA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 135 QANAeGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLVKIAYGNDDDQKSFVETQGLLQ 214
Cdd:cd06311   101 GDNP-GMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKG--NPGIKILAMQAGDWTREDGLKVAQDILT 177
                         170       180
                  ....*....|....*....|..
gi 1177747929 215 AYPNLKAIVA---PTTVGIAAA 233
Cdd:cd06311   178 KNKKIDAVWAaddDMAIGVLQA 199
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
12-278 1.31e-12

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 67.59  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  12 ALCVALVAISCAASAAGlknglKIAFVPKQINNPYEVIADDGGMAAIKEFG-GVGKVVGPSDAGASSQVQYINTLITQRQ 90
Cdd:PRK09701    9 SGTLVGLMLSTSAFAAA-----EYAVVLKTLSNPFWVDMKKGIEDEAKTLGvSVDIFASPSEGDFQSQLQLFEDLSNKNY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  91 DAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDT-------APEGRQLFVNQANAEGIGRGQIQLVSKLIGGEGEFAVLS 163
Cdd:PRK09701   84 KGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIdmdnlkkAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 164 ATPNATNQNTWIKWMQEELKKPeySKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSK 243
Cdd:PRK09701  164 GKAGNASGEARRNGATEAFKKA--SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT 241
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1177747929 244 GKVAVTGLGTPNQMRAFVKNGTVKAFQLWDPNQLG 278
Cdd:PRK09701  242 GKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIG 276
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
34-297 1.86e-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: 66.52  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEfGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd06313     1 KIGFTVYGLSSEFITNLVEAMKAVAKE-LNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFVNQANAEGiGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLV 193
Cdd:cd06313    80 GIPLVGVNALIENEDLTAYVGSDDVVA-GELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIENVLKK--YPDIKVL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 194 KIAYGNDDDQKSFVETQGLLQAYP-NLKAIVAPTTvGIAAAARYISSSSSKGKVAVTGL-GTPNQMRAfVKNGTVKAFQL 271
Cdd:cd06313   157 AEQTANWSRDEAMSLMENWLQAYGdEIDGIIAQND-DMALGALQAVKAAGRDDIPVVGIdGIEDALQA-VKSGELIATVL 234
                         250       260
                  ....*....|....*....|....*.
gi 1177747929 272 WDPNqlgyLAGYAAASLASGAITGKE 297
Cdd:cd06313   235 QDAE----AQGKGAVEVAVDAVKGEG 256
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
75-297 2.00e-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: 380653 [Multi-domain]  Cd Length: 302  Bit Score: 66.93  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  75 ASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSD-TAPEGRQLFVNQANAegiGRGQIQLVSKLI 153
Cdd:cd19998    45 VQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVvDEPCAYNVNTDQAKA---GEQTAQWLVDKL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 154 GGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIV--APTTVGIA 231
Cdd:cd19998   122 GGKGNILMVRGVPGTSVDRDRYEGAKEVFKK--YPDIKVVAEYYGNWDDGTAQKAVADALAAHPDVDGVWtqGGETGVIK 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1177747929 232 A--AARyisssssKGKVAVTGLGTpnqmrafvkNGTVKAFQLWDPNQL-GYLAGYAAAS------LASGAITGKE 297
Cdd:cd19998   200 AlqAAG-------HPLVPVGGEAE---------NGFRKAMLEPLANGLpGISAGSPPALsavalkLAVAVLEGEK 258
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
72-233 5.77e-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: 380652 [Multi-domain]  Cd Length: 305  Bit Score: 65.39  E-value: 5.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  72 DAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSD-TAPEGRQLfvnQANAEGIGRGQIQLVS 150
Cdd:cd19997    43 DGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGvTEPCAYIL---NNDFEDYGAASVEYVA 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 151 KLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGI 230
Cdd:cd19997   120 DRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKK--YPDLKVVAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGDGY 197

                  ...
gi 1177747929 231 AAA 233
Cdd:cd19997   198 GAA 200
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
52-225 3.79e-11

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


Pssm-ID: 380528 [Multi-domain]  Cd Length: 273  Bit Score: 62.70  E-value: 3.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  52 DGGMAAIKEFGGVGKVVgpsDAGA--SSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGr 129
Cdd:cd06305    19 QGAVAEAEKLGGTVIVF---DANGddARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAGIPVVTFDTDSQVPG- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 130 qLFVNQANAEGIGR-GQIQLVsKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKPEYSKIKLVKIAYGNDDDQKSFVE 208
Cdd:cd06305    95 -VNNITQDDYALGTlSLGQLV-KDLNGEGNIAVFNVFGVPPLDKRYDIYKAVLKANPGIKKIVAELGDVTPNTAADAQTQ 172
                         170
                  ....*....|....*....
gi 1177747929 209 TQGLLQAYPN--LKAIVAP 225
Cdd:cd06305   173 VEALLKKYPEggIDAIWAA 191
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
78-291 1.30e-10

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: 61.08  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  78 QVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQLFV--NQANAEGIGRGQIQLVSK-LIG 154
Cdd:cd06309    44 QINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVDRTIDGEDGSLYVtfIGSDFVEEGRRAAEWLVKnYKG 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 155 GEGEFAVLSATPNATNQNTWIKWMQEELKKpeYSKIKLVKIAYGNDDDQKSFVETQGLLQAYP-NLKAIVAPT---TVGI 230
Cdd:cd06309   124 GKGNVVELQGTAGSSVAIDRSKGFREVIKK--HPNIKIVASQSGNFTREKGQKVMENLLQAGPgDIDVIYAHNddmALGA 201
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1177747929 231 AAAaryISSS--SSKGKVAVTGL-GTPNQMRAfVKNGTVKAFQLWDPNQlGYLAGYAAASLASG 291
Cdd:cd06309   202 IQA---LKEAglKPGKDVLVVGIdGQKDALEA-IKAGELNATVECNPLF-GPTAFDTIAKLLAG 260
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
34-297 3.01e-10

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: 60.07  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGgVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd06319     1 KIGYSVYDLDNPFWQIMERGVQAAAEELG-YEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 114 GIKVVTFDSDTAPEGRQLFV---NQANAEGIGRGQIQLVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKPEYSKI 190
Cdd:cd06319    80 KIPVVIADIGTGGGDYVSYIisdNYDGGYQAGEYLAEALKENGWGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 191 klVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAFQ 270
Cdd:cd06319   160 --ALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGDILVVGFDGDPEALDLIKDGKLDGTV 237
                         250       260
                  ....*....|....*....|....*..
gi 1177747929 271 LWDPnqlgYLAGYAAASLASGAITGKE 297
Cdd:cd06319   238 AQQP----FGMGARAVELAIQALNGDN 260
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
72-269 3.28e-10

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: 59.90  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  72 DAGA----SSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTF--DSDTAPEGRQLFVNQANaegIGRGQ 145
Cdd:cd06306    36 EAGGytnlSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLvnGIDSPKVAARVLVDFYD---MGYLA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 146 IQ-LVSKLIGGEGEFAVLSATPNATNQNTWIKWMQEELKKpeySKIKLVKIAYGNDD--DQKSFVETqgLLQAYPNLKAI 222
Cdd:cd06306   113 GEyLVEHHPGKPVKVAWFPGPAGAGWAEDREKGFKEALAG---SNVEIVATKYGDTGkaVQLNLVED--ALQAHPDIDYI 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1177747929 223 VApTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVKAF 269
Cdd:cd06306   188 VG-NAVAAEAAVGALREAGLTGKVKVVSTYLTPGVYRGIKRGKILAA 233
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
71-250 3.41e-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: 59.94  E-value: 3.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  71 SDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQLFVNqANAEGIGRGQIQLVS 150
Cdd:cd19991    37 ANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNADVDLYVS-FDNEKVGELQAEALV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 151 KLIgGEGEFAVLSATPNATN----QNTWIKWMQEELKKpeySKIKLVKIAYGNDDD-QKSFVETQGLLQAYPN-LKAIVA 224
Cdd:cd19991   116 KAK-PKGNYVLLGGSPTDNNaklfREGQMKVLQPLIDS---GDIKVVGDQWVDDWDpEEALKIMENALTANNNkIDAVIA 191
                         170       180
                  ....*....|....*....|....*.
gi 1177747929 225 PTTVGIAAAARYISSSSSKGKVAVTG 250
Cdd:cd19991   192 SNDGTAGGAIQALAEQGLAGKVAVSG 217
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
75-281 3.05e-09

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: 57.19  E-value: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  75 ASSQVQYINTLITQRqDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEGRQLFV--NQANAegiGR--GqiQLVS 150
Cdd:cd06307    45 PEALAAALRRLAAGC-DGVALVAPDHPLVRAAIDELAARGIPVVTLVSDLPGSRRLAYVgiDNRAA---GRtaA--WLMG 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 151 KLIGG-EGEFAVLSATPNATNQNTWIK----WMQEelkkpEYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAp 225
Cdd:cd06307   119 RFLGRrPGKVLVILGSHRFRGHEEREAgfrsVLRE-----RFPDLTVLEVLEGLDDDELAYELLRELLARHPDLVGIYN- 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 226 TTVGIAAAARYISSSSSKGKVAV--TGLGTPNqmRAFVKNGTVKAF--QlwDPNQLGYLA 281
Cdd:cd06307   193 AGGGNEGIARALREAGRARRVVFigHELTPET--RRLLRDGTIDAVidQ--DPELQARRA 248
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
53-289 1.06e-08

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: 55.32  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  53 GGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDS-DTAPEGR-- 129
Cdd:cd06312    21 GAKDAAKDLGVTVQYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAINSgDDRSKERlg 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 130 -QLFVNQANAE-GIGRGQIQLVskliGGEGEFAVLSATPNATNQNTWIKWMQEELKKPEYSKIKLvkiaYGNDDDQKSFV 207
Cdd:cd06312   101 aLTYVGQDEYLaGQAAGERALE----AGPKNALCVNHEPGNPGLEARCKGFADAFKGAGILVELL----DVGGDPTEAQE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 208 ETQGLLQAYPNLKAIVAPTTVGIAAAARYISSSSSKGKVAVTGLGTPNQMRAFVKNGTVkafqLWDPNQLGYLAGYAAAS 287
Cdd:cd06312   173 AIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKVKIGTFDLSPETLEAIKDGKI----LFAIDQQPYLQGYLAVV 248

                  ..
gi 1177747929 288 LA 289
Cdd:cd06312   249 FL 250
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
35-127 6.66e-08

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380628 [Multi-domain]  Cd Length: 285  Bit Score: 53.24  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  35 IAFVPKQINNPYEVIADDGGMAAIKEFG-GVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQ 113
Cdd:cd19973     2 IGLITKTDTNPFFVKMKEGAQKAAKALGiKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDA 81
                          90
                  ....*....|....
gi 1177747929 114 GIKVVTFDSDTAPE 127
Cdd:cd19973    82 GVLVIALDTPTDPI 95
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
49-250 2.80e-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: 51.27  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  49 IADDGGMAAIKEFGGVGKVVGPSDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDTAPEG 128
Cdd:cd01538    15 QTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYDRLILNAD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 129 RQLFVNQANaEGIGRGQIQLVSKlIGGEGEFAVLSATPNATNQNTWIKWMQEELKKP-EYSKIKLVKIAYGNDDDQKSFV 207
Cdd:cd01538    95 VDYYISFDN-EKVGELQAQALLD-AKPEGNYVLIGGSPTDNNAKLFRDGQMKVLQPAiDSGKIKVVGDQWVDDWLPANAQ 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1177747929 208 ET--QGLLQAYPNLKAIVAP---TTVGIAAAaryISSSSSKGKVAVTG 250
Cdd:cd01538   173 QImeNALTANGNNVDAVVASndgTAGGAIAA---LKAQGLSGGVPVSG 217
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
78-121 1.43e-05

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 45.90  E-value: 1.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1177747929  78 QVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFD 121
Cdd:COG4213    47 QLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVIAYD 90
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
75-157 1.24e-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: 380650 [Multi-domain]  Cd Length: 294  Bit Score: 43.05  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  75 ASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFDSDtAPEGRQLFVNQANAEGIGRGQIQLVSKLIG 154
Cdd:cd19995    44 ASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRL-ILGGPADYYVSFDNVAVGEAQAQSLVDHLK 122

                  ...
gi 1177747929 155 GEG 157
Cdd:cd19995   123 AIG 125
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
78-235 1.24e-04

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


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 43.36  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  78 QVQYINTLITQRQ--DAIVIAaNDANAVVPYLKKAMSQGIKVVTFDSDTAPE-------GRQLFVN-----QANAEGIGR 143
Cdd:cd06324    45 MLELAEELLARPPkpDYLILV-NEKGVAPELLELAEQAKIPVFLINNDLTDEerallgkPREKFKYwlgsiVPDNEQAGY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 144 gqiQLVSKLI--------GGEGEFAVLS---ATPNATNQNtwiKWMQEELKkpEYSKIKLVKIAYGNDDDQKSFVETQGL 212
Cdd:cd06324   124 ---LLAKALIkaarkksdDGKIRVLAISgdkSTPASILRE---QGLRDALA--EHPDVTLLQIVYANWSEDEAYQKTEKL 195
                         170       180
                  ....*....|....*....|....*.
gi 1177747929 213 LQAYPNLKAIVA---PTTVGIAAAAR 235
Cdd:cd06324   196 LQRYPDIDIVWAandAMALGAIDALE 221
PBP1_LuxPQ_Quorum_Sensing cd06303
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ...
149-252 2.71e-04

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


Pssm-ID: 380526 [Multi-domain]  Cd Length: 320  Bit Score: 42.36  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 149 VSKLIGGEGEFAVLSATPNATNQ---NTWIKWMQEelkkpeYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLKAIVAP 225
Cdd:cd06303   152 FIKIFPEEGKYAILYLTEGYVSDqrgDTFIDEVAR------HSNLELVSAYYTDFDRESAREAARALLARHPDLDFIYAC 225
                          90       100
                  ....*....|....*....|....*...
gi 1177747929 226 TTvGIA-AAARYISSSSSKGKVAVTGLG 252
Cdd:cd06303   226 ST-DIAlGAIDALQELGRETDIMINGWG 252
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
71-121 4.35e-04

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: 41.46  E-value: 4.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1177747929  71 SDAGASSQVQYINTLITQRQDAIVIAANDANAVVPYLKKAMSQGIKVVTFD 121
Cdd:cd19994    37 ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYD 87
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
34-252 1.13e-03

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: 40.35  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929  34 KIAFVPKQINNPYEVIADDGGMAAIKEFGGVGKVVgpsDAGASSQVQY--INTLITQRQDAIVIAAND---ANAVVpylK 108
Cdd:cd01540     1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKI---DAKMDGEKVLsaIDNLIAQGAQGIVICTPDqklGPAIA---A 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1177747929 109 KAMSQGIKVVTFD---SDTAPEGRQLFVNqANAEGIGRGQIQLVSKLIGGEG-----EFAVLSATPN---ATNQNTwiKW 177
Cdd:cd01540    75 KAKAAGIPVIAVDdqlVDADPMKIVPFVG-IDAYKIGEAVGEWLAKEMKKRGwddvkEVGVLAITMDtlsVCVDRT--DG 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1177747929 178 MQEELKKPEYSKIKLVKIAYGNDDDQKSFVETQGLLQAYPNLK--AIVAPTTVGIAAAARYISSSS-SKGKVAVTGLG 252
Cdd:cd01540   152 AKDALKAAGFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAGfDAEDIIGVGIG 229
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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