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Conserved domains on  [gi|1927644809|emb|CAA0298329|]
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Autoinducer 2-binding protein LsrB [Klebsiella oxytoca]

Protein Classification

autoinducer 2 ABC transporter substrate-binding protein( domain architecture ID 11487778)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
1-337 0e+00

autoinducer 2 ABC transporter substrate-binding protein LsrB;


:

Pssm-ID: 237961  Cd Length: 336  Bit Score: 646.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809   1 MKTKRILqtSALALALSVATAQAADRIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQ 80
Cdd:PRK15408    2 KKKIALV--SALGIALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  81 GYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQVTKPTAKVAFFYSSPT 160
Cdd:PRK15408   80 GYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMAAKQVGKDKAKVAFFYSSPT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 161 VTDQNQWVKEAKAKIEKAHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQGVAIV 240
Cdd:PRK15408  160 VTDQNQWVKEAKAKIAKEHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRDKVAIV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 241 GFSTPNVMRPYVERGTVKAFGLWDVVQQGKIAVNVADRLLKKGDLNVGDSVDVKDLGTLKVEPNSVQGYQYEAKGNGIVL 320
Cdd:PRK15408  240 GFSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLKKGKLNVGDSLDVPGIGKVEVSPNSVQGYDYEAKGNGIVL 319

                         330
                  ....*....|....*..
gi 1927644809 321 LPERVVFTKENINNYDF 337
Cdd:PRK15408  320 LPERVVFTKENIDKYDF 336
 
Name Accession Description Interval E-value
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
1-337 0e+00

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 646.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809   1 MKTKRILqtSALALALSVATAQAADRIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQ 80
Cdd:PRK15408    2 KKKIALV--SALGIALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  81 GYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQVTKPTAKVAFFYSSPT 160
Cdd:PRK15408   80 GYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMAAKQVGKDKAKVAFFYSSPT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 161 VTDQNQWVKEAKAKIEKAHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQGVAIV 240
Cdd:PRK15408  160 VTDQNQWVKEAKAKIAKEHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRDKVAIV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 241 GFSTPNVMRPYVERGTVKAFGLWDVVQQGKIAVNVADRLLKKGDLNVGDSVDVKDLGTLKVEPNSVQGYQYEAKGNGIVL 320
Cdd:PRK15408  240 GFSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLKKGKLNVGDSLDVPGIGKVEVSPNSVQGYDYEAKGNGIVL 319

                         330
                  ....*....|....*..
gi 1927644809 321 LPERVVFTKENINNYDF 337
Cdd:PRK15408  320 LPERVVFTKENIDKYDF 336
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
 26-333 1.12e-157

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: 443.26  E-value: 1.12e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:cd20003     1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVDVTYDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQvTKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQWEVV 185
Cdd:cd20003    81 GIKVVTWDSDVNPDARDFFVNQATPEGIGKTLVDMVAEQ-TGEKGKVAIVTSSPTATNQNAWIKAMKAYIAEKYPDMKIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 186 TTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFGLWD 264
Cdd:cd20003   160 TTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTGkVAVTGLSTPNVMRPYVKDGTVKSVVLWD 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927644809 265 VVQQGKIAVNVADRLLKKGDLNVGDSVDVKDLGTLKVEPnsvqgyqyeaKGNGIVLLPERVVFTKENIN 333
Cdd:cd20003   240 VVDLGYLAVYVARALADGTLLKVGDFFVAGRLGTFTVVP----------KGNGIILLGEPLIFTKENID 298
RhaS TIGR02637
rhamnose ABC transporter, rhamnose-binding protein; This sugar-binding component of ABC ...
 27-337 2.82e-72

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: 226.28  E-value: 2.82e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  27 IAFIPKLVGVGFFTSGGNGAKEAGKALG-VDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:TIGR02637   1 IGLVVKSLGNPFFEAANKGAEEAAKELGsVYIIYTGPTGTTAEGQIEVVNSLIAQKVDAIAISANDPDALVPALKKAMKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQVTKpTAKVAFFYSSPTVTDQNQWVKEAKAKI-EKAHPQWEV 184
Cdd:TIGR02637  81 GIKVVTWDSGVAPEGRNLFLNQASADLIGRTQVQLAAEQIGN-GGEIAILSAASTATNQNAWIEIMKKELkDPKYPKVKL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 185 VTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFGLW 263
Cdd:TIGR02637 160 VATVYGDDDAQKSYQEAQGLLKSYPNLKGIIAPTTVGIKAAAQAVSDAKLIGkVKLTGLGLPSEMAKYVKNGTVKAFALW 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927644809 264 DVVQQGKIAVNVADRLL-KKGDLNVGDSVDVKDLGTLKVEPNsvqgyqyeakGNGIVLLPerVVFTKENINNYDF 337
Cdd:TIGR02637 240 NPIDLGYSAAYTAYRLSsGEITGKPGETFKAGRMGEYTIGDN----------GVAALGPP--FVFDADNIDQFSK 302
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 27-281 2.40e-57

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


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 186.36  E-value: 2.40e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  27 IAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRG 106
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 107 VKVLTWDSDTKPECRSIYINQgTPQQLGGLLVEMAEKQVtKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQWEVVT 186
Cdd:pfam13407  81 IPVVTFDSDAPSSPRLAYVGF-DNEAAGEAAGELLAEAL-GGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 187 TQFGYN-DATKSLQTAEGILKAYPD-LDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFGLW 263
Cdd:pfam13407 159 EVEGTNwDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGkVVVTGFDATPEALEAIKDGTIDATVLQ 238

                         250
                  ....*....|....*...
gi 1927644809 264 DVVQQGKIAVNVADRLLK 281
Cdd:pfam13407 239 DPYGQGYAAVELAAALLK 256
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 4-285 2.69e-56

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: 185.13  E-value: 2.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809   4 KRILQTSALALALSVA-----------TAQAADRIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDgPTEPSVSGQVQ 72
Cdd:COG1879     2 RLALLAAVLALALALAacgsaaaeaaaAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVV-DAEGDAAKQIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  73 LINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIYINQgTPQQLGGLLVEMAEKQvTKPTAKV 152
Cdd:COG1879    81 QIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGS-DNYAAGRLAAEYLAKA-LGGKGKV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 153 AFFYSSPTVTDQNQWVKEAKAKIeKAHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENL 232
Cdd:COG1879   159 AILTGSPGAPAANERTDGFKEAL-KEYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAA 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1927644809 233 KRQG-VAIVGFSTPNVMRPYVERGTVKAFGLWDVVQQGKIAVNVADRLLKKGDL 285
Cdd:COG1879   238 GRKGdVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEV 291
 
Name Accession Description Interval E-value
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
1-337 0e+00

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 646.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809   1 MKTKRILqtSALALALSVATAQAADRIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQ 80
Cdd:PRK15408    2 KKKIALV--SALGIALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  81 GYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQVTKPTAKVAFFYSSPT 160
Cdd:PRK15408   80 GYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMAAKQVGKDKAKVAFFYSSPT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 161 VTDQNQWVKEAKAKIEKAHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQGVAIV 240
Cdd:PRK15408  160 VTDQNQWVKEAKAKIAKEHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRDKVAIV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 241 GFSTPNVMRPYVERGTVKAFGLWDVVQQGKIAVNVADRLLKKGDLNVGDSVDVKDLGTLKVEPNSVQGYQYEAKGNGIVL 320
Cdd:PRK15408  240 GFSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLKKGKLNVGDSLDVPGIGKVEVSPNSVQGYDYEAKGNGIVL 319

                         330
                  ....*....|....*..
gi 1927644809 321 LPERVVFTKENINNYDF 337
Cdd:PRK15408  320 LPERVVFTKENIDKYDF 336
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
 26-333 1.12e-157

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: 443.26  E-value: 1.12e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:cd20003     1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVDVTYDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQvTKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQWEVV 185
Cdd:cd20003    81 GIKVVTWDSDVNPDARDFFVNQATPEGIGKTLVDMVAEQ-TGEKGKVAIVTSSPTATNQNAWIKAMKAYIAEKYPDMKIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 186 TTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFGLWD 264
Cdd:cd20003   160 TTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTGkVAVTGLSTPNVMRPYVKDGTVKSVVLWD 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927644809 265 VVQQGKIAVNVADRLLKKGDLNVGDSVDVKDLGTLKVEPnsvqgyqyeaKGNGIVLLPERVVFTKENIN 333
Cdd:cd20003   240 VVDLGYLAVYVARALADGTLLKVGDFFVAGRLGTFTVVP----------KGNGIILLGEPLIFTKENID 298
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
 26-332 2.80e-104

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: 307.63  E-value: 2.80e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:cd06302     1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQVTKPtAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQWEVV 185
Cdd:cd06302    81 GIKVITWDSDAPPSARDYFVNQADDEGLGEALVDSLAKEIGGK-GKVAILSGSLTATNLNAWIKAMKEYLKSKYPDIELV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 186 TTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFGLWD 264
Cdd:cd06302   160 DTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGkVAVTGIGLPNTARPYLKDGSVKEGVLWD 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927644809 265 VVQQGKIAVNVADRLLkKGDLNVGDSVDVKDLGTLKVEPNsvqgyqyeakgNGIVLLPERVVFTKENI 332
Cdd:cd06302   240 PAKLGYLTVYAAYQLL-KGKGFTEDSDDVGTGGKVKVDVA-----------GGEILLGPPLVFTKDNV 295
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
 26-333 3.01e-81

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: 249.10  E-value: 3.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:cd20000     1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQVTkPTAKVAFFYSSPTVTDQNQWVKEAKAKIEK-AHPQWEV 184
Cdd:cd20000    81 GIKVVTFDSDVAPEARDLFVNQADADGIGRAQVDMMAELIG-GEGEFAILSATPTATNQNAWIDAMKKELASpEYAGMKL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 185 VTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFGLW 263
Cdd:cd20000   160 VKVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGkVKVTGLGLPSEMAKYVKDGTVPAFALW 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927644809 264 DVVQQGKIAVNVADRLLKKG-DLNVGDSVDVKDLGTLKVEPnsvqgyqyeakgNGIVLLPERVVFTKENIN 333
Cdd:cd20000   240 NPIDLGYLAAYAAAALAQGEiTGKEGETFTAGRLGEYTVGE------------GGEVVLGPPFVFTADNID 298
RhaS TIGR02637
rhamnose ABC transporter, rhamnose-binding protein; This sugar-binding component of ABC ...
 27-337 2.82e-72

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: 226.28  E-value: 2.82e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  27 IAFIPKLVGVGFFTSGGNGAKEAGKALG-VDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:TIGR02637   1 IGLVVKSLGNPFFEAANKGAEEAAKELGsVYIIYTGPTGTTAEGQIEVVNSLIAQKVDAIAISANDPDALVPALKKAMKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQVTKpTAKVAFFYSSPTVTDQNQWVKEAKAKI-EKAHPQWEV 184
Cdd:TIGR02637  81 GIKVVTWDSGVAPEGRNLFLNQASADLIGRTQVQLAAEQIGN-GGEIAILSAASTATNQNAWIEIMKKELkDPKYPKVKL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 185 VTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFGLW 263
Cdd:TIGR02637 160 VATVYGDDDAQKSYQEAQGLLKSYPNLKGIIAPTTVGIKAAAQAVSDAKLIGkVKLTGLGLPSEMAKYVKNGTVKAFALW 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927644809 264 DVVQQGKIAVNVADRLL-KKGDLNVGDSVDVKDLGTLKVEPNsvqgyqyeakGNGIVLLPerVVFTKENINNYDF 337
Cdd:TIGR02637 240 NPIDLGYSAAYTAYRLSsGEITGKPGETFKAGRMGEYTIGDN----------GVAALGPP--FVFDADNIDQFSK 302
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 27-281 2.40e-57

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


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 186.36  E-value: 2.40e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  27 IAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRG 106
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 107 VKVLTWDSDTKPECRSIYINQgTPQQLGGLLVEMAEKQVtKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQWEVVT 186
Cdd:pfam13407  81 IPVVTFDSDAPSSPRLAYVGF-DNEAAGEAAGELLAEAL-GGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 187 TQFGYN-DATKSLQTAEGILKAYPD-LDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFGLW 263
Cdd:pfam13407 159 EVEGTNwDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGkVVVTGFDATPEALEAIKDGTIDATVLQ 238

                         250
                  ....*....|....*...
gi 1927644809 264 DVVQQGKIAVNVADRLLK 281
Cdd:pfam13407 239 DPYGQGYAAVELAAALLK 256
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 4-285 2.69e-56

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: 185.13  E-value: 2.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809   4 KRILQTSALALALSVA-----------TAQAADRIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDgPTEPSVSGQVQ 72
Cdd:COG1879     2 RLALLAAVLALALALAacgsaaaeaaaAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVV-DAEGDAAKQIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  73 LINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIYINQgTPQQLGGLLVEMAEKQvTKPTAKV 152
Cdd:COG1879    81 QIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGS-DNYAAGRLAAEYLAKA-LGGKGKV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 153 AFFYSSPTVTDQNQWVKEAKAKIeKAHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENL 232
Cdd:COG1879   159 AILTGSPGAPAANERTDGFKEAL-KEYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAA 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1927644809 233 KRQG-VAIVGFSTPNVMRPYVERGTVKAFGLWDVVQQGKIAVNVADRLLKKGDL 285
Cdd:COG1879   238 GRKGdVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEV 291
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 26-285 1.49e-44

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: 153.49  E-value: 1.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPtEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:cd01536     1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDA-QGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTWDSD-TKPECRSIYInqGTPQQLGGLLV-EMAEKQVtKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKaHPQWE 183
Cdd:cd01536    80 GIPVVAVDTDiDGGGDVVAFV--GTDNYEAGKLAgEYLAEAL-GGKGKVAILEGPPGSSTAIDRTKGFKEALKK-YPDIE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 184 VVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFGL 262
Cdd:cd01536   156 IVAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGdIKIVGVDGTPEALKAIKDGELDATVA 235

                         250       260
                  ....*....|....*....|...
gi 1927644809 263 WDVVQQGKIAVNVADRLLKKGDL 285
Cdd:cd01536   236 QDPYLQGYLAVEAAVKLLNGEKV 258
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 26-283 2.20e-43

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: 150.42  E-value: 2.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:cd06314     1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTWDSDTKPECRSIYInqGTPQQLGGLLVEMAEKQVTKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKaHPQWEVV 185
Cdd:cd06314    81 GIPVITFDSDAPDSKRLAYI--GTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKG-SPGIEIV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 186 TTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFglwd 264
Cdd:cd06314   158 DPLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGkVKIVGFDTLPETLQGIKDGVIAAT---- 233

                         250       260
                  ....*....|....*....|...
gi 1927644809 265 VVQQ----GKIAVNVADRLLKKG 283
Cdd:cd06314   234 VGQRpyemGYLSVKLLYKLLKGG 256
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 26-333 6.47e-38

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


Pssm-ID: 380656  Cd Length: 296  Bit Score: 137.02  E-value: 6.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:cd20001     1 TIAVVVKVTGIAWFDRMETGVEQFAKDTGVNVYQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTW--------DSDTKPecrsiYINQGTPQQLGGLLVE-MAEKqvtkptAKVAFFYSSPTVTDQNQWVKEAKAKIE 176
Cdd:cd20001    81 GIVVITHeasnlknvDYDVEA-----FDNAAYGAFIMDKLAEaMGGK------GKYVTFVGSLTSTSHMEWANAAVAYQK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 177 KAHPQWEVVT-TQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVER 254
Cdd:cd20001   150 ANYPDMLLVTdRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGkIAVVGTGLPSVAGEYLED 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 255 GTVKAFGLWDVVQQGKIAVNVADRLLKKGDLNVGdsvdvKDLGtlkvepnsVQGYQYEAKGNGIVLLPER-VVFTKENIN 333
Cdd:cd20001   230 GTIDYIQFWDPADAGYAMNALAVMVLEGEKITDG-----TDLG--------VPGYEKVTVGKGKVLYGNAwLIVTKDNVD 296
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 27-307 1.71e-36

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: 133.21  E-value: 1.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  27 IAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRG 106
Cdd:cd20002     2 IVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 107 VKVLTWDSDTKPECR---SIYINQGTPQQLGGLLV-EMAEKqvtkptAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQW 182
Cdd:cd20002    82 IVVITHESPGQKGADwdvELIDNEKFGEAQMELLAkEMGGK------GEYAIFVGSLTVPLHNLWADAAVEYQKEKYPNM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 183 EVVTTQF-GYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAF 260
Cdd:cd20002   156 KQVTDRIpGGEDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGLKGkVAVVGTVIPSQAAAYLKEGSITEG 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1927644809 261 GLWDVVQQGKIAVNVADRLLKKGDLNVGDSVDVKDLGTLKVEPNSVQ 307
Cdd:cd20002   236 YLWDPADAGYAMVYIAKMLLDGKRKEIGDGFEIPGKGTPDIDGNVII 282
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 26-285 3.39e-28

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: 110.41  E-value: 3.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:cd20007     1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQGPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTWDSD-TKPECRSIYInqGTPQQLGGLLV--EMAEkqVTKPTAKVAFFYSSPTVTDQNQWVKEAKAKIeKAHPQW 182
Cdd:cd20007    81 GIKVVTVDTTlGDPSFVLSQI--ASDNVAGGALAaeALAE--LIGGKGKVLVINSTPGVSTTDARVKGFAEEM-KKYPGI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 183 EVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFG 261
Cdd:cd20007   156 KVLGVQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGkVKVVGFDASPAQVEQLKAGTIDALI 235

                         250       260
                  ....*....|....*....|....
gi 1927644809 262 LWDVVQQGKIAVNVADRLLKKGDL 285
Cdd:cd20007   236 AQKPAEIGYLAVEQAVAALTGKPV 259
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 26-282 2.62e-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: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 108.07  E-value: 2.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVG--FFTSGGNGAKEAGKALGVDVTYDGPT-EPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRA 102
Cdd:cd20006     1 KIALILKSSDPNsdFWQTVKSGAEAAAKEYGVDLEFLGPEsEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 103 MQRGVKVLTWDSDTKPECRSIYInqGTPQQLGGllVEMAEKQV--TKPTAKVAFFYSSPTVTDQNQWVKEAKAKIeKAHP 180
Cdd:cd20006    81 KKAGIPVITIDSPVNSKKADSFV--ATDNYEAG--KKAGEKLAslLGEKGKVAIVSFVKGSSTAIEREEGFKQAL-AEYP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 181 QWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKA 259
Cdd:cd20006   156 NIKIVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLGGkVKVVGFDSSVEEIQLLEEGIIDA 235

                         250       260
                  ....*....|....*....|....*..
gi 1927644809 260 FglwdVVQQ----GKIAVNVADRLLKK 282
Cdd:cd20006   236 L----VVQNpfnmGYLSVQAAVDLLNG 258
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 26-292 9.23e-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: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 106.54  E-value: 9.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGP-TEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQ 104
Cdd:cd20008     1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPaTEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 105 rGVKVLTWDSDTKPECRSIYI---NQGTPQQLGGLLVEMAEKQVTKPtAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQ 181
Cdd:cd20008    81 -GIPVVLVDSGANTDDYDAFLatdNVAAGALAADELAELLKASGGGK-GKVAIISFQAGSQTLVDREEGFRDYIKEKYPD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 182 WEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAF 260
Cdd:cd20008   159 IEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAGkIVLVGFDSSPDEVALLKSGVIKAL 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1927644809 261 GLWDVVQQGKIAVNVADRLLKKGDLnVGDSVD 292
Cdd:cd20008   239 VVQDPYQMGYEGVKTAVKALKGEEI-VEKNVD 269
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 26-284 1.54e-25

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


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 103.09  E-value: 1.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGP-TEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQ 104
Cdd:cd20005     1 YIAVISKGFQHQFWKAVKKGAEQAAKELGVKITFEGPdTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 105 RGVKVLTWDSDTkpECRSIYINQGTPQQLGGLLV--EMAEkqVTKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQW 182
Cdd:cd20005    81 KGIPVVTFDSGV--PSDLPLATVATDNYAAGALAadHLAE--LIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 183 EVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFG 261
Cdd:cd20005   157 KVVNVQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLGkIKVVGFDSGEAQIDAIKNGVIAGSV 236

                         250       260
                  ....*....|....*....|...
gi 1927644809 262 LWDVVQQGKIAVNVADRLLKKGD 284
Cdd:cd20005   237 TQNPYGMGYKTVKAAVKALKGEE 259
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 26-268 1.69e-25

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


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 103.08  E-value: 1.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGP-TEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQ 104
Cdd:cd20004     1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPsREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 105 RGVKVLTWDSDTKPECRSIYInqGTPQQLGGLLV--EMAEKQVTKPtaKVAFF-YS--SPTVTDQNQWVKEAkakIEKAH 179
Cdd:cd20004    81 QGIPVVIIDSDLGGDAVISFV--ATDNYAAGRLAakRMAKLLNGKG--KVALLrLAkgSASTTDRERGFLEA---LKKLA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 180 PQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVK 258
Cdd:cd20004   154 PGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLAGkVKFIGFDASDLLLDALRAGEIS 233

                         250
                  ....*....|
gi 1927644809 259 AFglwdVVQQ 268
Cdd:cd20004   234 AL----VVQD 239
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
 29-259 4.30e-24

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: 99.33  E-value: 4.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  29 FIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVK 108
Cdd:cd19969     4 MVTFKSGHPYWDDVKEGFEDAGAELGVKTEYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 109 VLTWDSDTKPECRSIYINQGTPQQLGGLLVEMAEKQVTKptAKVAFFYSSPTvTDQNQWVKEAKAKIEKaHPQWEVVTTQ 188
Cdd:cd19969    84 VVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELLGGK--GKVAVLTGPGQ-PNHEERVEGFKEAFAE-YPGIEVVAVG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927644809 189 FGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKA 259
Cdd:cd19969   160 DDNDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTGkVKIVAFDDDPETLDLIKDGVIDA 231
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 26-286 7.22e-23

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: 95.87  E-value: 7.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGP-TEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQ 104
Cdd:cd06310     1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPeSEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 105 RGVKVLTWDSDTKPECRSIYInqGTPQQLGGLLVEMAEKQVTKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQWEV 184
Cdd:cd06310    81 KGIPVIVIDSGIKGDAYLSYI--ATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIKV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 185 VTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFglw 263
Cdd:cd06310   159 LASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGqIKIVGFDSQEELLDALKNGKIDAL--- 235

                         250       260
                  ....*....|....*....|....*..
gi 1927644809 264 dVVQQ----GKIAVNVADRLLKKGDLN 286
Cdd:cd06310   236 -VVQNpyeiGYEGIKLALKLLKGEEVP 261
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 38-281 7.83e-23

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: 95.81  E-value: 7.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  38 FFTSGGNGAKEAGKALGVDVTYDGPtEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTK 117
Cdd:cd06322    13 FFVDIKDAMKKEAAELGVKVVVADA-NGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFTVDVKAD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 118 PECRSIYInqGTPQQLGGLLV-EMAEKQVTKPTAKVAFFySSPTVTDQNQWVKEAKAKIEKaHPQWEVVTTQFGYNDATK 196
Cdd:cd06322    92 GAKVVTHV--GTDNYAGGKLAgEYALKALLGGGGKIAII-DYPEVESVVLRVNGFKEAIKK-YPNIEIVAEQPGDGRREE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 197 SLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGF-STPNVMRPYVERGTVKAfglwDVVQQ----GK 270
Cdd:cd06322   168 ALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDkIKVIGFdGNPEAIKAIAKGGKIKA----DIAQQpdkiGQ 243

                         250
                  ....*....|.
gi 1927644809 271 IAVNVADRLLK 281
Cdd:cd06322   244 ETVEAIVKYLA 254
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
 45-285 7.17e-22

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: 93.03  E-value: 7.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  45 GAKEAGKALGVDVT-YDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDtkPECRSI 123
Cdd:cd06306    20 GIVDEAKRLGVKLTvYEAGGYTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNG--IDSPKV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 124 YINQGTPQ-QLGGLLVE-MAEKQVTKPTaKVAFFySSPtvtdQNQ-WVKEAKAKIEKA--HPQWEVVTTQFGYNDATKSL 198
Cdd:cd06306    98 AARVLVDFyDMGYLAGEyLVEHHPGKPV-KVAWF-PGP----AGAgWAEDREKGFKEAlaGSNVEIVATKYGDTGKAVQL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 199 QTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQGVAIVGFS-TPNVMRpYVERGTVKAFGLWDVVQQGKIAVNVAD 277
Cdd:cd06306   172 NLVEDALQAHPDIDYIVGNAVAAEAAVGALREAGLTGKVKVVSTYlTPGVYR-GIKRGKILAAPSDQPVLQGRIAVDQAV 250


                  ....*...
gi 1927644809 278 RLLKKGDL 285
Cdd:cd06306   251 RALEGKPV 258
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 26-284 8.19e-22

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: 93.21  E-value: 8.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSvSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:cd06317     1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDP-SKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTWDSDTKPECRSIYI---NQGTPQQLGGLLVEMAEKQVTKPtAKVAFFYSSPTVTdQNQWVKEAKAKIeKAHPQW 182
Cdd:cd06317    80 GIPVIAYDAVIPSDFQAAQVgvdNLEGGKEIGKYAADYIKAELGGQ-AKIGVVGALSSLI-QNQRQKGFEEAL-KANPGV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 183 EVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFS-TPNVMRPYVERGTVKAF 260
Cdd:cd06317   157 EIVATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQGkIKVFGWDlTKQAIFLGIDEGVLQAV 236

                         250       260
                  ....*....|....*....|....
gi 1927644809 261 GLWDVVQQGKIAVNVADRLLKKGD 284
Cdd:cd06317   237 VQQDPEKMGYEAVKAAVKAIKGED 260
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 26-216 9.35e-22

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: 93.10  E-value: 9.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYD-GPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQ 104
Cdd:cd06320     1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQaAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 105 RGVKVLTWDSDTKPECRSIYINQGTPQ------QLGGLLVE-MAEKQVTKptAKVAFFYSSPTVTDQNQWVKEAKAKIEK 177
Cdd:cd06320    81 KGIPVINLDDAVDADALKKAGGKVTSFigtdnvAAGALAAEyIAEKLPGG--GKVAIIEGLPGNAAAEARTKGFKETFKK 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1927644809 178 AhPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIA 216
Cdd:cd06320   159 A-PGLKLVASQPADWDRTKALDAATAILQAHPDLKGIYA 196
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 38-216 1.18e-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: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 84.21  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  38 FFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDS-DT 116
Cdd:cd06312    14 FWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAINSgDD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 117 KPECRSIYINQ-GTPQQLGGllVEMAEKQVTKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQWEVVTTQFgynDAT 195
Cdd:cd06312    94 RSKERLGALTYvGQDEYLAG--QAAGERALEAGPKNALCVNHEPGNPGLEARCKGFADAFKGAGILVELLDVGG---DPT 168

                         170       180
                  ....*....|....*....|.
gi 1927644809 196 KSLQTAEGILKAYPDLDAIIA 216
Cdd:cd06312   169 EAQEAIKAYLQADPDTDAVLT 189
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 38-284 7.80e-18

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: 81.96  E-value: 7.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  38 FFTSGGNGAKEAGKALGVDVT-YDGPTEPSVsgQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 116
Cdd:cd06323    13 FFVSLKDGAQAEAKELGVELVvLDAQNDPAK--QLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 117 KPECRSIYInqGTPQQLGGllvEMAEK---QVTKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKaHPQWEVVTTQFGYND 193
Cdd:cd06323    91 TGGKVVSHI--ASDNVAGG---EMAAEyiaKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAK-YPKINVVASQTADFD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 194 ATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQGVAIVGF-STPNVMRPyVERGTVKAfglwDVVQQ---- 268
Cdd:cd06323   165 RTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFdGTPDAVKA-VKDGKLAA----TVAQQpeem 239

                         250
                  ....*....|....*.
gi 1927644809 269 GKIAVNVADRLLKKGD 284
Cdd:cd06323   240 GAKAVETADKYLKGEK 255
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 26-294 4.33e-17

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: 79.99  E-value: 4.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGK-ALGVD-VTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAM 103
Cdd:cd19970     1 KVALVMKSLANEFFIEMEKGARKHAKeANGYElLVKGIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 104 QRGVKVLTWDS---DTKPECRSIYIN-QGTPQQLGGLLVEMA-EKQVTKPTaKVAFFYSSPTVTDQNQWVKEAKAKIEKA 178
Cdd:cd19970    81 DAGIAVINIDNrldADALKEGGINVPfVGPDNRQGAYLAGDYlAKKLGKGG-KVAIIEGIPGADNAQQRKAGFLKAFEEA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 179 hpQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTV 257
Cdd:cd19970   160 --GMKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKM 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1927644809 258 KA----FGlwdvVQQGKIAVNVADRLLKKGDLNVGDSVDVK 294
Cdd:cd19970   238 LAtidqHP----AKQAVYGIEYALKMLNGEEVPGWVKTPVE 274
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 37-216 1.16e-16

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: 78.80  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  37 GFFTSGGNGAKEAGKALGVDVTYDgPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 116
Cdd:cd06309    12 PWRVANTKSIKEAAKKRGYELVYT-DANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVDRTI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 117 KPECRSIYINQ-GTPQ-QLGGLLVEMAEKQVTKPTAKVAFF---YSSPTVTDQNQWVKEAkakIEKaHPQWEVVTTQFGY 191
Cdd:cd06309    91 DGEDGSLYVTFiGSDFvEEGRRAAEWLVKNYKGGKGNVVELqgtAGSSVAIDRSKGFREV---IKK-HPNIKIVASQSGN 166

                         170       180
                  ....*....|....*....|....*.
gi 1927644809 192 NDATKSLQTAEGILKAYP-DLDAIIA 216
Cdd:cd06309   167 FTREKGQKVMENLLQAGPgDIDVIYA 192
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 26-242 4.78e-15

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: 73.85  E-value: 4.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 105
Cdd:cd19965     1 KFVFVTHVTTNPFFQPVKKGMDDACELLGAECQFTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 106 GVKVLTW--DSDTKPECRSIYINQGTPQ---QLGgllVEMAEKQVTKPtAKVAFFYSSPtvtdQNQWVKEAKAKIEKA-- 178
Cdd:cd19965    81 GIPVVAFnvDAPGGENARLAFVGQDLYPagyVLG---KRIAEKFKPGG-GHVLLGISTP----GQSALEQRLDGIKQAlk 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927644809 179 ----HPQWEVVTTQfgyNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGF 242
Cdd:cd19965   153 eygrGITYDVIDTG---TDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGkVLVGGF 218
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 38-287 5.66e-15

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


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 73.90  E-value: 5.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  38 FFTSGGNGAKEAGKALGVDVT-YDgpTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 116
Cdd:cd19967    13 FFVVEAEGAKEKAKELGYEVTvFD--HQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLIDREI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 117 KPEcrSIYINQGTPQQLGGLlVEMAEKQVTKPTAKVAFFYSSPTVTDQNQWVKeAKAKIE--KAHPQWEVVTTQFGYNDA 194
Cdd:cd19967    91 NAE--GVAVAQIVSDNYQGA-VLLAQYFVKLMGEKGLYVELLGKESDTNAQLR-SQGFHSviDQYPELKMVAQQSADWDR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 195 TKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENL-KRQGVAIVGFSTPNVMRPYVERGTVKAFGLWDVVQQGKIAV 273
Cdd:cd19967   167 TEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAgRAGDVIIVGFDGSNDVRDAIKEGKISATVLQPAKLIARLAV 246

                         250
                  ....*....|....
gi 1927644809 274 NVADRLLKKGDLNV 287
Cdd:cd19967   247 EQADQYLKGGSTGK 260
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 26-217 6.06e-15

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: 73.87  E-value: 6.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIpKLVGVGFFTS-GGNGAKEAGKALGVDV-TYDGptEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAM 103
Cdd:cd06305     1 TIAVV-RNGTSGDWDQqALQGAVAEAEKLGGTViVFDA--NGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 104 QRGVKVLTWDSDTkPECRSIYINQGtpQQLGGLLVEMAEKQVTKPTAKVA---FFYSSPTVTDQNQWvkeakAKIEKAHP 180
Cdd:cd06305    78 DAGIPVVTFDTDS-QVPGVNNITQD--DYALGTLSLGQLVKDLNGEGNIAvfnVFGVPPLDKRYDIY-----KAVLKANP 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1927644809 181 QWEVVTTQFGYNDATKSLQTA---EGILKAYPD--LDAIIAP 217
Cdd:cd06305   150 GIKKIVAELGDVTPNTAADAQtqvEALLKKYPEggIDAIWAA 191
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 66-214 1.26e-14

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


Pssm-ID: 380651 [Multi-domain]  Cd Length: 302  Bit Score: 73.04  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  66 SVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIYINQGtpQQLGGLLveMAE--- 142
Cdd:cd19996    43 DTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSGVGSDKYTAFVGVD--DAAFGRV--GAEwlv 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927644809 143 KQVtKPTAKVAFFYSSPTVTDQNQWVKEAKaKIEKAHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAI 214
Cdd:cd19996   119 KQL-GGKGNIIALRGIAGVSVSEDRWAGAK-EVFKEYPGIKIVGEVYADWDYAKAKQAVESLLAAYPDIDGV 188
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
 67-216 2.07e-14

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: 72.74  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  67 VSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSD-TKPECRSIYINQGTPQQLGG--LLVEMAEK 143
Cdd:cd06300    46 ATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGAvTSPDAYNVSNDQVEWGRLGAkwLFEALGGK 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927644809 144 qvtkptAKVAFFY---SSPTVTDQNQWVKEAKAKiekaHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIA 216
Cdd:cd06300   126 ------GNVLVVRgiaGAPASADRHAGVKEALAE----YPGIKVVGEVFGGWDEATAQTAMLDFLATHPQVDGVWT 191
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 26-286 2.74e-14

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: 71.92  E-value: 2.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVT-YDGptEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQ 104
Cdd:cd06313     1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVvLDG--NGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 105 RGVKVLTWDSDTKPECRSIYInqGTPQQLGGLLV--EMAEKQVTKptAKVAFFY----SSPTVTDqnqwvKEAKAKIEKA 178
Cdd:cd06313    79 AGIPLVGVNALIENEDLTAYV--GSDDVVAGELEgqAVADRLGGK--GNVVILEgpigQSAQIDR-----GKGIENVLKK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 179 HPQWEVVTTQFGYNDATKSLQTAEGILKAYPD-LDAIIAPDANALPAAAQAAENLKRQGVAIVGFSTPNVMRPYVERGTV 257
Cdd:cd06313   150 YPDIKVLAEQTANWSRDEAMSLMENWLQAYGDeIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDALQAVKSGEL 229

                         250       260
                  ....*....|....*....|....*....
gi 1927644809 258 KAFGLWDVVQQGKIAVNVADRLLKKGDLN 286
Cdd:cd06313   230 IATVLQDAEAQGKGAVEVAVDAVKGEGVE 258
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 63-216 1.08e-13

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: 70.40  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  63 TEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPEC-RSIYINQGT-PQQLGGLLVEM 140
Cdd:cd19998    41 SGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVVDEPCaYNVNTDQAKaGEQTAQWLVDK 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927644809 141 AEKQvtkptAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQWEVVTTQFGYNDATKSLQTAEgILKAYPDLDAIIA 216
Cdd:cd19998   121 LGGK-----GNILMVRGVPGTSVDRDRYEGAKEVFKKYPDIKVVAEYYGNWDDGTAQKAVAD-ALAAHPDVDGVWT 190
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 38-282 1.12e-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: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 69.92  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  38 FFTSGGNGAKEAGKALGVD-VTYDGptEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 116
Cdd:cd19971    13 FFIAINDGIKKAVEANGDElITRDP--QLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 117 K-PECRSIYInqGTPQQLGGLLVEMAEKQVTKPTAKVAFFYsSPTVTDQNQWVKEAKAKIeKAHPQWEVVTTQFGYNDAT 195
Cdd:cd19971    91 KdTDLVDSTI--ASDNYNAGKLCGEDMVKKLPEGAKIAVLD-HPTAESCVDRIDGFLDAI-KKNPKFEVVAQQDGKGQLE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 196 KSLQTAEGILKAYPDLDAIIA-PDANALPAAAQAAENLKRQGVAIVGFSTPNVMRPYVERGTVKAFGLWDVVQQGKIAVN 274
Cdd:cd19971   167 VAMPIMEDILQAHPDLDAVFAlNDPSALGALAALKAAGKLGDILVYGVDGSPDAKAAIKDGKMTATAAQSPIEIGKKAVE 246


                  ....*...
gi 1927644809 275 VADRLLKK 282
Cdd:cd19971   247 TAYKILNG 254
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 67-218 1.53e-13

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: 70.03  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  67 VSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSD-TKPECRSIYINQGTPQQLGgllvemAEKQV 145
Cdd:cd19999    46 ATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPvSSPDAINVVIDQYKWAAIQ------AQWLA 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927644809 146 TK--PTAKVAFFYSSPTVTDQNQWVKEAKAKIEKaHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPD 218
Cdd:cd19999   120 EQlgGKGNIVAINGVAGNPANEARVKAADDVFAK-YPGIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLTQD 193
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 38-281 1.61e-13

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: 69.75  E-value: 1.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  38 FFTSGGNGAKEAGKALGVDVTY-DGptEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 116
Cdd:cd06318    13 YYAALVAAAKAEAKKLGVELVVtDA--QNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGIPVITVDSAL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 117 KPECRSIYINQGTPQQLGGLLVEMAEKQVTKPTAKVAFFYSSP--TVTDQNQW------VKEAKAKIEKAhpQWEVVTTQ 188
Cdd:cd06318    91 DPSANVATQVGRDNKQNGVLVGKEAAKALGGDPGKIIELSGDKgnEVSRDRRDgflagvNEYQLRKYGKS--NIKVVAQP 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 189 FGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQGVAIVgFSTPNVMRPY--VERGTVKAFGLWDVV 266
Cdd:cd06318   169 YGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVKV-AGADGQKEALklIKDGKYVATGLNDPD 247

                         250
                  ....*....|....*
gi 1927644809 267 QQGKIAVNVADRLLK 281
Cdd:cd06318   248 LLGKTAVDTAAKVVK 262
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
2-259 2.60e-13

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 69.52  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809   2 KTKRILQTSALALALSVATAQAADrIAFIPKLVGVGFFTSGGNGAKEAGKALGVDV-TYDGPTEPSVSGQVQLINNFVNQ 80
Cdd:PRK09701    3 KYLKYFSGTLVGLMLSTSAFAAAE-YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPSEGDFQSQLQLFEDLSNK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  81 GYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDtkpecrsiyINQGTPQQLGGLLVEMAEKQVTKPTAKVAFFYSSPT 160
Cdd:PRK09701   82 NYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEK---------IDMDNLKKAGGNVEAFVTTDNVAVGAKGASFIIDKL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 161 VTDQNQ-WVKEAKA-------------KIEKAHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAA 226
Cdd:PRK09701  153 GAEGGEvAIIEGKAgnasgearrngatEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVA 232

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1927644809 227 QAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKA 259
Cdd:PRK09701  233 QAVANAGKTGkVLVVGTDGIPEARKMVEAGQMTA 266
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 39-215 5.58e-13

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: 68.47  E-value: 5.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  39 FTSGGNGAKEAGKALGVDVTyDGPTepSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKP 118
Cdd:cd19997    21 FEEAAKKAKADGLIADYIVV-NADG--SATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGVTE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 119 ECrsIYINQGTPQQLGGLLVEMAEKQVTKpTAKVAFFY----SSPtvtdqNQWVKEAKAKIEKAHPQWEVVTTQFGYNDA 194
Cdd:cd19997    98 PC--AYILNNDFEDYGAASVEYVADRLGG-KGNVLEVRgvagTSP-----DEEIYAGQVEALKKYPDLKVVAEVYGNWTQ 169

                         170       180
                  ....*....|....*....|.
gi 1927644809 195 TKSLQTAEGILKAYPDLDAII 215
Cdd:cd19997   170 SVAQKAVTGILPSLPEVDAVI 190
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
 47-282 7.98e-13

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: 67.57  E-value: 7.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  47 KEAGKALGVDVTY-DGptEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIYI 125
Cdd:cd06308    23 AEAAKYPNVELIVtDA--QGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVLDRKVSGDDYTAFI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 126 ---NQGTPQQLGGLLVEMAekqvtKPTAKVAFFY----SSPTVtDQNQWVKEAKAKiekaHPQWEVVTTQFGYNDATKSL 198
Cdd:cd06308   101 gadNVEIGRQAGEYIAELL-----NGKGNVVEIQglpgSSPAI-DRHKGFLEAIAK----YPGIKIVASQDGDWLRDKAI 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 199 QTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQ-GVAIVGF-STPNVMRPYVERGTVKAFGLWDVVqqGKIAVNVA 276
Cdd:cd06308   171 KVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREkEIKIIGVdGLPEAGEKAVKDGILAATFLYPTG--GKEAIEAA 248


                  ....*.
gi 1927644809 277 DRLLKK 282
Cdd:cd06308   249 LKILNG 254
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 26-249 9.88e-12

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: 64.33  E-value: 9.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVD-VTYDGptEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQ 104
Cdd:cd19968     1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKlVVLDA--QNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 105 RGVKVLTWDSdtKPECRSIYINQGTPQQLGGLLVEMAEKQVTKPTAKVAFFYSSP---TVTDQNQWVKEAKAKIEKahpq 181
Cdd:cd19968    79 AGIPVVTVDR--RAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPgssPAIDRTKGFHEELAAGPK---- 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927644809 182 WEVVTTQFGYNDATKSLQTAEGILKAYP-DLDAIIAP--DANALPAAAQAAENLKRQGVAIVGF-STPNVMR 249
Cdd:cd19968   153 IKVVFEQTGNFERDEGLTVMENILTSLPgPPDAIICAndDMALGAIEAMRAAGLDLKKVKVIGFdAVPDALQ 224
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
 47-282 2.93e-11

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: 63.02  E-value: 2.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  47 KEAGKALGVDVTY-DGptEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVltwdsdtkpecrsIYI 125
Cdd:cd06301    24 AYAKEYPGVKLVIvDA--QSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPL-------------VYV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 126 NQGTPQQLGGLLV---------EMAEKQVTK---PTAKVAFFYSSPTVTDQNQWVKEAKAKIEKaHPQWEVVTTQFGYND 193
Cdd:cd06301    89 NREPDSKPKGVAFvgsddiesgELQMEYLAKllgGKGNIAILDGVLGHEAQILRTEGNKDVLAK-YPGMKIVAEQTANWS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 194 ATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGF-STPNVMRpYVERGTVKAFGLWDVVQQGKI 271
Cdd:cd06301   168 REKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDdILVAGIdATPDALK-AMKAGRLDATVFQDAAGQGET 246

                         250
                  ....*....|.
gi 1927644809 272 AVNVADRLLKK 282
Cdd:cd06301   247 AVDVAVKAAKG 257
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 38-242 1.33e-10

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: 61.15  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  38 FFTSGGNGAKEAGKALGVDVTYDG-PTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 116
Cdd:cd06321    13 FFVAMVRGAEEAAAEINPGAKVTVvDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVVAVDVAA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 117 KPecrsIYINQGTPQQLGGLLV--EMAEKQVTKptAKVAFFySSPTVTDQNQWVKEAKAKIEKAhPQWEVVTTQFGYNDA 194
Cdd:cd06321    93 EG----ADATVTTDNVQAGYLAceYLVEQLGGK--GKVAII-DGPPVSAVIDRVNGCKEALAEY-PGIKLVDDQNGKGSR 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1927644809 195 TKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQGVAIVGF 242
Cdd:cd06321   165 AGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSV 212
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 38-119 1.31e-09

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: 58.25  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  38 FFTSGGNGAKEAGKALGVDV-TYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 116
Cdd:cd19973    13 FFVKMKEGAQKAAKALGIKLmTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVLVIALDTPT 92


                  ...
gi 1927644809 117 KPE 119
Cdd:cd19973    93 DPI 95
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
 8-300 1.34e-09

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 58.42  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809   8 QTSALaLALSVATAQAADRI-AFIPKL-----VGVGFftsggnGAKEAGKALGVDVT------YDGPTEpsvsgQVQLIN 75
Cdd:PRK10936   31 QRTSL-QYSPLLKAKKAWKLcALYPHLkdsywLSVNY------GMVEEAKRLGVDLKvleaggYYNLAK-----QQQQLE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  76 NFVNQGYNAIIVSAVSPDGLCPALKRaMQRGVKVLTW----DSDtKPECRSiyinqGTP-----QQLGGLLVEMAEKqvT 146
Cdd:PRK10936   99 QCVAWGADAILLGAVTPDGLNPDLEL-QAANIPVIALvngiDSP-QVTTRV-----GVSwyqmgYQAGRYLAQWHPK--G 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 147 KPTAKVAFFysspTVTDQNQWVKEAKAKIEKA--HPQWEVVTTQFGYNDatKSLQT--AEGILKAYPDLDAIIAPDANAL 222
Cdd:PRK10936  170 SKPLNVALL----PGPEGAGGSKAVEQGFRAAiaGSDVRIVDIAYGDND--KELQRnlLQELLERHPDIDYIAGSAVAAE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 223 PAAAQAAENLKRQGVAIVGF-STPNVMRPyVERGTVKAFGLWDVVQQGKIAVNVADRLLKKGDL--NVGDSVDVKDLGTL 299
Cdd:PRK10936  244 AAIGELRGRNLTDKIKLVSFyLSHQVYRG-LKRGKVLAAPSDQMVLQGRLAIDQAVRQLEGAPVpgDVGPKILVLTPKNL 322


                  .
gi 1927644809 300 K 300
Cdd:PRK10936  323 D 323
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 38-332 6.32e-09

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


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 56.21  E-value: 6.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  38 FFTSGGNGAKEAGKALGVD-VTYDGPTepSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 116
Cdd:cd06319    13 FWQIMERGVQAAAEELGYEfVTYDQKN--SANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIPVVIADIGT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 117 KPECRSIYI---NQGTPQQLGGLLVE-MAEKQVTKptAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQwEVVTTQFGYN 192
Cdd:cd06319    91 GGGDYVSYIisdNYDGGYQAGEYLAEaLKENGWGG--GSVGIIAIPQSRVNGQARTAGFEDALEEAGVE-EVALRQTPNS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 193 DATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGFSTPNVMRPYVERGTVKAFGLWDVVQQGKI 271
Cdd:cd06319   168 TVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGdILVVGFDGDPEALDLIKDGKLDGTVAQQPFGMGAR 247

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927644809 272 AVNVADRLLKkgdlnvGDSVDVKDlgtlkvepnsvqgyqyeakgngiVLLPERVVfTKENI 332
Cdd:cd06319   248 AVELAIQALN------GDNTVEKE-----------------------IYLPVLLV-TSENV 278
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 46-218 6.77e-07

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: 50.06  E-value: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  46 AKEAGKALGvDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIYI 125
Cdd:cd06311    21 AEKQAKELA-DLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYDLYV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 126 NQGTPqqlgGLLVEMAEKQVTK--PTAKVAFFYSSPTVTDQNQWVKEAKAKIeKAHPQWEVVTTQFGYNDATKSLQTAEG 203
Cdd:cd06311   100 AGDNP----GMGVVSAEYIGKKlgGKGNVVVLEVPSSGSVNEERVAGFKEVI-KGNPGIKILAMQAGDWTREDGLKVAQD 174

                         170
                  ....*....|....*
gi 1927644809 204 ILKAYPDLDAIIAPD 218
Cdd:cd06311   175 ILTKNKKIDAVWAAD 189
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 44-217 6.80e-06

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: 46.85  E-value: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  44 NGAKEAGKALGVDV--TYDGPTEPSVsgQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVK-VLTwdsDTKP-- 118
Cdd:cd06316    19 AGIKDTFEELGIEVvaVTDANFDPAK--QITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKlVFM---DNVPdg 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 119 -ECRSIYINQGTPQQLG-GLLV--EMAEKQVTKPTAKVAFFYSSPTVTdqNQWVKEAKAKIEKAHPQWEVVTTQfGYNDA 194
Cdd:cd06316    94 lEAGKDYVSVVSSDNRGnGQIAaeLLAEAIGGKGKVGIIYHDADFYAT--NQRDKAFKDTLKEKYPDIKIVAEQ-GFADP 170

                         170       180
                  ....*....|....*....|...
gi 1927644809 195 TKSLQTAEGILKAYPDLDAIIAP 217
Cdd:cd06316   171 NDAEEVASAMLTANPDIDGIYVS 193
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
1-301 1.44e-05

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 45.85  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809   1 MKTKRILQ-TSALALALSV-ATAQAADRIAFIPKLVGVGFFTSGGNGAKEAGKALGVD-VTYDGPTEPSvsGQVQLINNF 77
Cdd:PRK10653    1 MNMKKLATlVSAVALSATVsANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNlVVLDSQNNPA--KELANVQDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  78 VNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWD-SDTKPECRSiyiNQGTPQQLGGllvEMAEKQVTKPTAKVAFFY 156
Cdd:PRK10653   79 TVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDrGATKGEVVS---HIASDNVAGG---KMAGDFIAKKLGEGAKVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 157 SSPTV--TDQNQWVKEAKAKIEKAHpQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKR 234
Cdd:PRK10653  153 QLEGIagTSAARERGEGFKQAVAAH-KFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927644809 235 QGVAIVGFS-TPNVMRPyVERGTVKAfglwDVVQQ----GKIAVNVADRLLKkgdlnvGDSVDVKDLGTLKV 301
Cdd:PRK10653  232 SDVMVVGFDgTPDGIKA-VNRGKLAA----TIAQQpdqiGAIGVETADKVLK------GEKVEAKIPVDLKL 292
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
 47-216 1.34e-04

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


Pssm-ID: 380646 [Multi-domain]  Cd Length: 284  Bit Score: 42.99  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  47 KEAGKALGVDVTYDGPTEpSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDsdtkpecRSI--- 123
Cdd:cd19991    22 VKKAKELGAEVIVQSANG-DDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYD-------RLIlna 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 124 ----YINqGTPQQLGGLLVEMAEKQvtKPTAKVAFFYSSPtvTDQNQ------WVKEAKAKIEKAhpQWEVVTTQFGYN- 192
Cdd:cd19991    94 dvdlYVS-FDNEKVGELQAEALVKA--KPKGNYVLLGGSP--TDNNAklfregQMKVLQPLIDSG--DIKVVGDQWVDDw 166

                         170       180
                  ....*....|....*....|....*
gi 1927644809 193 DATKSLQTAEGILKAY-PDLDAIIA 216
Cdd:cd19991   167 DPEEALKIMENALTANnNKIDAVIA 191
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 26-212 1.42e-04

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


Pssm-ID: 380482 [Multi-domain]  Cd Length: 294  Bit Score: 43.05  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDVTY-DGPTEPSVsgQVQLINNFVNQGYNAIIVsaVSPD-GLCPA-LKRA 102
Cdd:cd01540     1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKiDAKMDGEK--VLSAIDNLIAQGAQGIVI--CTPDqKLGPAiAAKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 103 MQRGVKVLTWD-----SDTKPECRSIYINqGTP--QQLGGLLVEMAEKQVTKPTAKVAF----FYSSPTVTDQnqwVKEA 171
Cdd:cd01540    77 KAAGIPVIAVDdqlvdADPMKIVPFVGID-AYKigEAVGEWLAKEMKKRGWDDVKEVGVlaitMDTLSVCVDR---TDGA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1927644809 172 KAKIEKA-HPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLD 212
Cdd:cd01540   153 KDALKAAgFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVK 194
PBP1_ABC_sugar_binding-like cd06315
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 26-178 1.43e-04

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


Pssm-ID: 380538  Cd Length: 278  Bit Score: 42.72  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKLVGVGFFTSGGNGAKEAGKALGVDV-TYDGptEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQ 104
Cdd:cd06315     2 TIAYVASDLRNGGVLGVGRGVKEAAAALGWKVdVLDG--GGTVTGRLAALNQALALKPDGIILGGDDAVELQEPLKKAVK 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927644809 105 RGVKVLTWDSDTKP---ECRSIYINQGT-PQQLGGLLVEMAEKQvTKPTAKVAFFyssptvTDQNQWVKEAKAKIEKA 178
Cdd:cd06315    80 AGIPVVGWHAAASPgpiPELGLFTNITTdPREVAETAAALVIAQ-SGGKAGVVIF------TDSRYAIATAKANAMKK 150
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 26-215 4.26e-04

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


Pssm-ID: 380621 [Multi-domain]  Cd Length: 278  Bit Score: 41.54  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  26 RIAFIPKL-VGVGFFTSGGNGAKEAGKALGVDVTYDGPTEpSVSGQVQLINNFVNQGYNAIIVSAVSPDG-LCPALKRAM 103
Cdd:cd19966     1 KIYFIPGGaPGDPFWTVVYNGAKDAAADLGVDLDYVFSSW-DPEKMVEQFKEAIAAKPDGIAIMGHPGDGaYTPLIEAAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 104 QRGVKVLTWDSD----TKPECRSIYInqGTPQQLGGLLV--EMAEKQVTKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEK 177
Cdd:cd19966    80 KAGIIVTSFNTDlpklEYGDCGLGYV--GADLYAAGYTLakELVKRGGLKTGDRVFVPGLLPGQPYRVLRTKGVIDALKE 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1927644809 178 AHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAII 215
Cdd:cd19966   158 AGIKVDYLEISLEPNKPAEGIPVMTGYLAANPDVKAIV 195
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 38-285 4.43e-04

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: 41.27  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  38 FFTSGGNGAKEAGKALGVDV-TYDGPTEPSVsgQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 116
Cdd:cd19972    13 FFNQIKQSVEAEAKKKGYKViTVDAKGDSAT--QVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 117 KPECRSIYINQGTPQQLGGLLVEMAEKqvTKPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKAhPQWEVVTTQFGYNDATK 196
Cdd:cd19972    91 EDAPGDTFIATDSVAAAKELGEWVIKQ--TGGKGEIAILHGQLGTTPEVDRTKGFQEALAEA-PGIKVVAEQTADWDQDE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 197 SLQTAEGILKAYPDLDAIIA-PDANALPAAAQAAENLKRQGVAIVGFSTPNVMRPYVERGTVKAFGLWDVVQQGKIAVNV 275
Cdd:cd19972   168 GFKVAQDMLQANPNITVFFGqSDAMALGAAQAVKVAGLDHKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKMGRLAVDS 247

                         250
                  ....*....|
gi 1927644809 276 ADRLLKKGDL 285
Cdd:cd19972   248 AIDLLNGKAV 257
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
 80-214 4.85e-04

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: 41.39  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  80 QGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIYInqGTPQ-QLG---GLLveMAeKQVTKPTAKVAFF 155
Cdd:cd06307    57 AGCDGVALVAPDHPLVRAAIDELAARGIPVVTLVSDLPGSRRLAYV--GIDNrAAGrtaAWL--MG-RFLGRRPGKVLVI 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927644809 156 YSSPTVTDQNQwvKEA--KAKIEKAHPQWEVVTTQFGYNDATKSLQTAEGILKAYPDLDAI 214
Cdd:cd06307   132 LGSHRFRGHEE--REAgfRSVLRERFPDLTVLEVLEGLDDDELAYELLRELLARHPDLVGI 190
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
 43-113 7.66e-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: 40.69  E-value: 7.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927644809  43 GNGAKEAGKALG--VDVTYdgpTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWD 113
Cdd:cd19994    18 GENLKSELEEAGytVDLQY---ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYD 87
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 47-303 1.70e-03

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


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 39.49  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  47 KEAGKALGVDVTYDGpTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDsdtkpecRSI--- 123
Cdd:cd19992    22 EEEAKELGVELIFQV-ADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYD-------RLIlna 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 124 ----YINQGTPqQLGGLLVEMAEKQVtkPTAKVAFFY----SSPTVTDQNQWVKEAKAKIEKAhpQWEVVTTQFGYN-DA 194
Cdd:cd19992    94 dvdlYVGRDNY-KVGQLQAEYALEAV--PKGNYVILSgdpgDNNAQLITAGAMDVLQPAIDSG--DIKIVLDQYVKGwSP 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 195 TKSLQTAEGILKAY-PDLDAIIAPDANALPAAAQAAENLKRQG-VAIVGF-STPNVMRpYVERGTVKAFGLWDVVQQGKI 271
Cdd:cd19992   169 DEAMKLVENALTANnNNIDAVLAPNDGMAGGAIQALKAQGLAGkVFVTGQdAELAALK-RIVEGTQTMTVWKDLKELARA 247

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1927644809 272 AVNVADRLLKKGDLNVGDSVD---VKDLGTLKVEP 303
Cdd:cd19992   248 AADAAVKLAKGEKPQTTDETInngGKDVPAILIPG 282
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
 48-217 3.20e-03

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: 38.56  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809  48 EAGKALGVDVTY---DGptepSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSIY 124
Cdd:cd01538    23 EQLEEKGAKVLVqsaDG----DKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYDRLILNADVDYY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927644809 125 INQGTpQQLGgllvEMAEKQVT--KPTAKVAFFYSSPTVTDQNQWVKEAKAKIEKAHPQWEVVTTQFGYND---ATKSLQ 199
Cdd:cd01538    99 ISFDN-EKVG----ELQAQALLdaKPEGNYVLIGGSPTDNNAKLFRDGQMKVLQPAIDSGKIKVVGDQWVDdwlPANAQQ 173

                         170
                  ....*....|....*....
gi 1927644809 200 TAEGILKAY-PDLDAIIAP 217
Cdd:cd01538   174 IMENALTANgNNVDAVVAS 192
PBP1_BmpA_Med_PnrA-like cd06304
periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and ...
 37-86 7.60e-03

periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and various putative lipoproteins from other bacteria; Periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and various putative lipoproteins from other bacteria. These outer membrane proteins include Med, a cell-surface localized protein regulating the competence transcription factor gene comK in Bacillus subtilis, and PnrA, a periplasmic purine nucleoside binding protein of an ATP-binding cassette (ABC) transport system in Treponema pallidum. All contain the type 1 periplasmic sugar-binding protein-like fold.


Pssm-ID: 380527  Cd Length: 262  Bit Score: 37.52  E-value: 7.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1927644809  37 GFFTSGGNGAKEAGKALGVDVTYdgpTE-PSVSGQVQLINNFVNQGYNAII 86
Cdd:cd06304    14 GWNQAAYEGLKKAAKELGIEVAY---SEnVPPADAERVLRDYASQGYDLII 61
 
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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