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Conserved domains on  [gi|1582227628|gb|TBA09511|]
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ABC transporter substrate-binding protein [Rhizobium ruizarguesonis]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 14448385)

ABC transporter substrate-binding protein may function in transport of sugar substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 30-335 2.52e-142

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: 404.75  E-value: 2.52e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMLTSWGKVTGEAVKAGTVAAAdPFTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVK 109
Cdd:cd19997     1 VIALSNSYAGNTWRQQMVDAFEEAAKKAKADGLIADY-IVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 110 EACDAGITVVSFDGIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKI 189
Cdd:cd19997    80 QACDAGIKVVVFDSGVTEPCAYILNNDFEDYGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKKYPDLKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 190 VGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDGYGAAQAIAATDRKMPIIIMGNREDELKWWKEQKDAKSYETMSV 269
Cdd:cd19997   160 VAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGDGYGAAQAFEAAGRPLPIIIGGNRGEFLKWWQEEYAKNGYETVSV 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582227628 270 SIAPGVSTLAFWVAQQILDGKEVKKDLVVPFLRIDQDNLETNLANTQAGGVANVEYTQADAIKVIE 335
Cdd:cd19997   240 STDPGQGSAAFWVALDILNGKDVPKEMILPVVTITEDDLDAWLAVTPDGIVAPTYYTEWVVSNLID 305
 
Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 30-335 2.52e-142

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: 404.75  E-value: 2.52e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMLTSWGKVTGEAVKAGTVAAAdPFTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVK 109
Cdd:cd19997     1 VIALSNSYAGNTWRQQMVDAFEEAAKKAKADGLIADY-IVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 110 EACDAGITVVSFDGIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKI 189
Cdd:cd19997    80 QACDAGIKVVVFDSGVTEPCAYILNNDFEDYGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKKYPDLKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 190 VGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDGYGAAQAIAATDRKMPIIIMGNREDELKWWKEQKDAKSYETMSV 269
Cdd:cd19997   160 VAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGDGYGAAQAFEAAGRPLPIIIGGNRGEFLKWWQEEYAKNGYETVSV 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582227628 270 SIAPGVSTLAFWVAQQILDGKEVKKDLVVPFLRIDQDNLETNLANTQAGGVANVEYTQADAIKVIE 335
Cdd:cd19997   240 STDPGQGSAAFWVALDILNGKDVPKEMILPVVTITEDDLDAWLAVTPDGIVAPTYYTEWVVSNLID 305
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 21-308 1.47e-51

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: 172.80  E-value: 1.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  21 SAFAETSAKKIALSNNYAGNSWRQAMltswgkvtGEAVKAgtvAAADP-----FTTAENQATEQAAQIQNMILQGYDAIV 95
Cdd:COG1879    26 AAAAAAKGKTIGFVVKTLGNPFFVAV--------RKGAEA---AAKELgveliVVDAEGDAAKQISQIEDLIAQGVDAII 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  96 LNAASPTALNGAVKEACDAGITVVSFD-GIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEIS 174
Cdd:COG1879    95 VSPVDPDALAPALKKAKAAGIPVVTVDsDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANERT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 175 AGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDG-YGAAQAIAATDRKMPIIIMGN--REDE 251
Cdd:COG1879   175 DGFKEALKEYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMaLGAAQALKAAGRKGDVKVVGFdgSPEA 254

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 252 LKWWKEQkdaksyeTMSVSIA---PGVSTLAFWVAQQILDGKEVKKDLVVPFLRIDQDNL 308
Cdd:COG1879   255 LQAIKDG-------TIDATVAqdpYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 31-291 4.38e-44

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: 152.08  E-value: 4.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  31 IALSNNYAGNSWRQAMLTSWGKVTGEAVKAGTVAAadpftTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKE 110
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVG-----PAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 111 ACDAGITVVSFD-GIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQ-FPQFK 188
Cdd:pfam13407  76 AKDAGIPVVTFDsDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEkYPGIK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 189 IVGSV-HGDWAQDVAQKAVAGILPSLPD-IAGVVTQGGDG-YGAAQAIAATDRKMPIIIMG--NREDELKWWKEQKdaks 263
Cdd:pfam13407 156 VVAEVeGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMaGGAAQALEAAGLAGKVVVTGfdATPEALEAIKDGT---- 231

                         250       260
                  ....*....|....*....|....*...
gi 1582227628 264 YETMSVSIAPGVSTLAFWVAQQILDGKE 291
Cdd:pfam13407 232 IDATVLQDPYGQGYAAVELAAALLKGKK 259
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
 74-235 8.22e-08

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 53.03  E-value: 8.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  74 NQATeQAAQIQNMILQGYDAIVLNAASPTALNGAVKEAcDAGITVVSF-DGIVTEPCAWRIAVNFKEMGRSEVEYLSKKL 152
Cdd:PRK10936   89 NLAK-QQQQLEQCVAWGADAILLGAVTPDGLNPDLELQ-AANIPVIALvNGIDSPQVTTRVGVSWYQMGYQAGRYLAQWH 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 153 PDGGNLLEI------RGLAGVfvdDEISAGIHEGVKQfPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVtqggdg 226
Cdd:PRK10936  167 PKGSKPLNVallpgpEGAGGS---KAVEQGFRAAIAG-SDVRIVDIAYGDNDKELQRNLLQELLERHPDIDYIA------ 236


                  ....*....
gi 1582227628 227 yGAAQAIAA 235
Cdd:PRK10936  237 -GSAVAAEA 244
 
Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 30-335 2.52e-142

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: 404.75  E-value: 2.52e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMLTSWGKVTGEAVKAGTVAAAdPFTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVK 109
Cdd:cd19997     1 VIALSNSYAGNTWRQQMVDAFEEAAKKAKADGLIADY-IVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 110 EACDAGITVVSFDGIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKI 189
Cdd:cd19997    80 QACDAGIKVVVFDSGVTEPCAYILNNDFEDYGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKKYPDLKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 190 VGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDGYGAAQAIAATDRKMPIIIMGNREDELKWWKEQKDAKSYETMSV 269
Cdd:cd19997   160 VAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGDGYGAAQAFEAAGRPLPIIIGGNRGEFLKWWQEEYAKNGYETVSV 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582227628 270 SIAPGVSTLAFWVAQQILDGKEVKKDLVVPFLRIDQDNLETNLANTQAGGVANVEYTQADAIKVIE 335
Cdd:cd19997   240 STDPGQGSAAFWVALDILNGKDVPKEMILPVVTITEDDLDAWLAVTPDGIVAPTYYTEWVVSNLID 305
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
 30-310 4.09e-73

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: 228.36  E-value: 4.09e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMLTSWGKVTGEAVKAGTVAAADpFTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVK 109
Cdd:cd06300     1 TIGLSNTYAGNSWREQMIASLKADAAQSGQKGLVKELI-VANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 110 EACDAGITVVSFDGIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKI 189
Cdd:cd06300    80 QAADAGIPVVAFDGAVTSPDAYNVSNDQVEWGRLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEALAEYPGIKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 190 VGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDGYGAAQAIAATDRKM-PIIIMGNREDELKWWKEQKDAksYETMS 268
Cdd:cd06300   160 VGEVFGGWDEATAQTAMLDFLATHPQVDGVWTQGGEDTGVLQAFQQAGRPPvPIVGGDENGFAKQWWKHPKKG--LTGAA 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1582227628 269 VSIAPGVSTLAFWVAQQILDGKEVK-KDLVVPFLRIDQDNLET 310
Cdd:cd06300   238 VWPPPAIGAAGLEVALRLLEGQGPKpQSVLLPPPLITNDDAKA 280
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 30-309 2.69e-72

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: 226.40  E-value: 2.69e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQamltswgkvtgEAVKAGTVAAADP-------FTT--AENQATEQAAQIQNMILQGYDAIVLNAAS 100
Cdd:cd19998     1 KIALSNSYSGNDWRQ-----------EMINIAKAAAKQPpyadkveLKVvsSGTDVQAQISAIDNMIAAGYDAILIYAIS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 101 PTALNGAVKEACDAGITVVSFDGIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEG 180
Cdd:cd19998    70 PTALNPVIKRACDAGIVVVAFDNVVDEPCAYNVNTDQAKAGEQTAQWLVDKLGGKGNILMVRGVPGTSVDRDRYEGAKEV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 181 VKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGdGYGAAQAIAATDRKMPIIIM----GNREDELKwwk 256
Cdd:cd19998   150 FKKYPDIKVVAEYYGNWDDGTAQKAVADALAAHPDVDGVWTQGG-ETGVIKALQAAGHPLVPVGGeaenGFRKAMLE--- 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582227628 257 eqKDAKSYETMSVSIAPGVSTLAFWVAQQILDGKEVKKDLVVPFLRIDQDNLE 309
Cdd:cd19998   226 --PLANGLPGISAGSPPALSAVALKLAVAVLEGEKEPKTIELPLPWVTTDDVK 276
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 30-310 6.56e-59

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: 191.69  E-value: 6.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMltsWGKVTGEAVKAGTVAAADPFTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVK 109
Cdd:cd19996     1 TIGFSNAGLGNSWRVQM---IAEFEAEAAKLKKLIKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 110 EACDAGITVVSFDGIV-TEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFK 188
Cdd:cd19996    78 KAAAAGIPVVLFDSGVgSDKYTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYPGIK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 189 IVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDG-YGAAQAIAATDRKMPIIIMGNREDELKWWKEQKDAKSYETM 267
Cdd:cd19996   158 IVGEVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMtLGAIEAFEEAGRPLVPMTGEDNNGFLKAWKELPGFKSIAPS 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1582227628 268 SvsiAPGVSTLAFWVAQQILDGKEVKKDLVVPFLRIDQDNLET 310
Cdd:cd19996   238 Y---PPWLGATALDAALAALEGEPVPKYVYIPLPVITDENLDQ 277
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 30-299 1.06e-55

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: 183.66  E-value: 1.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMLTSWGKVTGEAVKAG-----TVAAADpfttaeNQATEQAAQIQNMILQGYDAIVLNAASPTAL 104
Cdd:cd19999     1 VIGVSNGYVGNEWRAQMIADFEEVAAEYKEEGvisdlIVQNAD------ADATGQISQIRNMINEGVDAILIDPVSATAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 105 NGAVKEACDAGITVVSFDGIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQF 184
Cdd:cd19999    75 NPVIEKAQAAGILVVSFDQPVSSPDAINVVIDQYKWAAIQAQWLAEQLGGKGNIVAINGVAGNPANEARVKAADDVFAKY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 185 PQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDGYGAAQAIAATDRKMPIIIMGNREDELKWWKEQkDAKSY 264
Cdd:cd19999   155 PGIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLTQDGMAEGVLRAFQAAGKDPPVMTGDYRKGFLRKWKEL-DLPDF 233

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1582227628 265 ETMSVSIAPGVSTLAFWVAQQILDGKEVKKDLVVP 299
Cdd:cd19999   234 ESIGVVNPPGIGATALRIAVRLLQGKELKEDALNP 268
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 21-308 1.47e-51

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: 172.80  E-value: 1.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  21 SAFAETSAKKIALSNNYAGNSWRQAMltswgkvtGEAVKAgtvAAADP-----FTTAENQATEQAAQIQNMILQGYDAIV 95
Cdd:COG1879    26 AAAAAAKGKTIGFVVKTLGNPFFVAV--------RKGAEA---AAKELgveliVVDAEGDAAKQISQIEDLIAQGVDAII 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  96 LNAASPTALNGAVKEACDAGITVVSFD-GIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEIS 174
Cdd:COG1879    95 VSPVDPDALAPALKKAKAAGIPVVTVDsDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANERT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 175 AGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDG-YGAAQAIAATDRKMPIIIMGN--REDE 251
Cdd:COG1879   175 DGFKEALKEYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMaLGAAQALKAAGRKGDVKVVGFdgSPEA 254

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 252 LKWWKEQkdaksyeTMSVSIA---PGVSTLAFWVAQQILDGKEVKKDLVVPFLRIDQDNL 308
Cdd:COG1879   255 LQAIKDG-------TIDATVAqdpYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 31-291 4.38e-44

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: 152.08  E-value: 4.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  31 IALSNNYAGNSWRQAMLTSWGKVTGEAVKAGTVAAadpftTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKE 110
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVG-----PAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 111 ACDAGITVVSFD-GIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQ-FPQFK 188
Cdd:pfam13407  76 AKDAGIPVVTFDsDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEkYPGIK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 189 IVGSV-HGDWAQDVAQKAVAGILPSLPD-IAGVVTQGGDG-YGAAQAIAATDRKMPIIIMG--NREDELKWWKEQKdaks 263
Cdd:pfam13407 156 VVAEVeGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMaGGAAQALEAAGLAGKVVVTGfdATPEALEAIKDGT---- 231

                         250       260
                  ....*....|....*....|....*...
gi 1582227628 264 YETMSVSIAPGVSTLAFWVAQQILDGKE 291
Cdd:pfam13407 232 IDATVLQDPYGQGYAAVELAAALLKGKK 259
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
 30-299 1.35e-40

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: 143.07  E-value: 1.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMLtswgkvtgEAVKAgtVAAADP-----FTTAENQATEQAAQIQNMILQGYDAIVLNAASPTAL 104
Cdd:cd06308     1 VIGFSQCSLNDPWRAAMN--------EEIKA--EAAKYPnveliVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADAL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 105 NGAVKEACDAGITVVSFD-GIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQ 183
Cdd:cd06308    71 TPVVKKAYDAGIPVIVLDrKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 184 FPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGD-GYGAAQAIAATDRKMPIIIMGnrEDELKwwKEQKDAK 262
Cdd:cd06308   151 YPGIKIVASQDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEmALGAYQALKKAGREKEIKIIG--VDGLP--EAGEKAV 226

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1582227628 263 SYETMSVSIA-PGVSTLAFWVAQQILDGKEVKKDLVVP 299
Cdd:cd06308   227 KDGILAATFLyPTGGKEAIEAALKILNGEKVPKEIVLP 264
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 30-300 8.47e-40

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: 141.16  E-value: 8.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMLtswgkvtgEAVKAgtvAAADP-----FTTAENQATEQAAQIQNMILQGYDAIVLNAASPTAL 104
Cdd:cd01536     1 KIGVVVKDLTNPFWVAVK--------KGAEA---AAKELgvelvVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEAL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 105 NGAVKEACDAGITVVSFDGIVT--EPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVK 182
Cdd:cd01536    70 VPAVKKANAAGIPVVAVDTDIDggGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 183 QFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDG-YGAAQAIAATDRKMPIIIMGN--REDELKWWKEQK 259
Cdd:cd01536   150 KYPDIEIVAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMaLGAAEALKAAGRTGDIKIVGVdgTPEALKAIKDGE 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1582227628 260 daksyETMSVSIAPGV-STLAFWVAQQILDGKEVKKDLVVPF 300
Cdd:cd01536   230 -----LDATVAQDPYLqGYLAVEAAVKLLNGEKVPKEILTPV 266
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 30-314 7.96e-29

periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 112.31  E-value: 7.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMLTSwgkVTGEAVKAGTVAAadpFTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVK 109
Cdd:cd06309     1 TVGFSQAGSESPWRVANTKS---IKEAAKKRGYELV---YTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 110 EACDAGITVVSFD-GIVTEPC---AWRIAVNFKEMGRSEVEYLSKKL-PDGGNLLEIRGLAGVFVDDEISAGIHEGVKQF 184
Cdd:cd06309    75 EAKDAGIPVILVDrTIDGEDGslyVTFIGSDFVEEGRRAAEWLVKNYkGGKGNVVELQGTAGSSVAIDRSKGFREVIKKH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 185 PQFKIVGSVHGDWAQDVAQKAVAGILPSLP-DIAGVVTQGGD-GYGAAQAIAATDRKMP--IIIMGnrEDELKW-WKEQK 259
Cdd:cd06309   155 PNIKIVASQSGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDmALGAIQALKEAGLKPGkdVLVVG--IDGQKDaLEAIK 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582227628 260 DAKSyeTMSVSIAPGVSTLAFWVAQQILDGKEVKKDLVVPFLRIDQDNLETNLAN 314
Cdd:cd06309   233 AGEL--NATVECNPLFGPTAFDTIAKLLAGEKVPKLIIVEERLFDKDNAAEELEP 285
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 56-309 1.71e-27

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: 108.89  E-value: 1.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  56 EAVKAG---TVAAADpfttAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEPCAWR 132
Cdd:cd06320    24 EAKKLGvkvDVQAAP----SETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKKGIPVINLDDAVDADALKK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 133 --------IAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQK 204
Cdd:cd06320   100 aggkvtsfIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKKAPGLKLVASQPADWDRTKALD 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 205 AVAGILPSLPDIAGVVTQG-GDGYGAAQAIAATDRKMPIIIMGnredeLKWWKEQKDAKSYETMSVSIA---PGVSTLAF 280
Cdd:cd06320   180 AATAILQAHPDLKGIYAANdTMALGAVEAVKAAGKTGKVLVVG-----TDGIPEAKKSIKAGELTATVAqypYLEGAMAV 254

                         250       260
                  ....*....|....*....|....*....
gi 1582227628 281 WVAQQILDGKEVKKDLVVPFLRIDQDNLE 309
Cdd:cd06320   255 EAALRLLQGQKVPAVVATPQALITKDNVD 283
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 71-299 2.09e-26

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: 105.52  E-value: 2.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  71 TAENqATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEPCA-WRIAVNFKEMGRSEVEYLS 149
Cdd:cd06311    37 TSSN-ANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYdLYVAGDNPGMGVVSAEYIG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 150 KKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGD-GYG 228
Cdd:cd06311   116 KKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNPGIKILAMQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDmAIG 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582227628 229 AAQAIAATDRKMPIIIMGNREDElKWWKEQKDAKSYETMSVSIAPGVSTLAFWVAQQILDG-KEVKKDLVVP 299
Cdd:cd06311   196 VLQAIKEAGRTDIKVMTGGGGSQ-EYFKRIMDGDPIWPASATYSPAMIADAIKLAVLILKGgKTVEKEVIIP 266
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 68-299 3.17e-24

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: 99.68  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  68 PFTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEPC-AWRIAVNFKEMGRSEVE 146
Cdd:cd06323    33 VVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSVTGGKvVSHIASDNVAGGEMAAE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 147 YLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGD- 225
Cdd:cd06323   113 YIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAKYPKINVVASQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEm 192

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582227628 226 GYGAAQAIAATDRKMPIII-MGNREDELKWWKEQKdaksyetMSVSIA--PG-VSTLAFWVAQQILDGKEVKKDLVVP 299
Cdd:cd06323   193 ALGAIQALKAAGRKDVIVVgFDGTPDAVKAVKDGK-------LAATVAqqPEeMGAKAVETADKYLKGEKVPKKIPVP 263
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 72-307 6.90e-23

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: 96.19  E-value: 6.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDG-IVTEPCAWRIAVNFKEMGRSEVEYLSK 150
Cdd:cd06313    37 GNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAGIPLVGVNAlIENEDLTAYVGSDDVVAGELEGQAVAD 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 151 KLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPD-IAGVVTQGGD-GYG 228
Cdd:cd06313   117 RLGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYPDIKVLAEQTANWSRDEAMSLMENWLQAYGDeIDGIIAQNDDmALG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 229 AAQAIAATDR-KMPIIIMGNREDELKWWKEQKDAKSyetmSVSIAPGVSTLAFWVAQQILDGKEVKKDLVVPFLRIDQDN 307
Cdd:cd06313   197 ALQAVKAAGRdDIPVVGIDGIEDALQAVKSGELIAT----VLQDAEAQGKGAVEVAVDAVKGEGVEKKYYIPFVLVTKDN 272
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 72-301 2.90e-22

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: 94.38  E-value: 2.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFD--GIVTEPCAWRIAVNFkEMGRSEVEYLS 149
Cdd:cd19968    37 AQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAGIPVVTVDrrAEGAAPVPHVGADNV-AGGREVAKFVV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 150 KKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLP-DIAGVVTQGGD-GY 227
Cdd:cd19968   116 DKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAAGPKIKVVFEQTGNFERDEGLTVMENILTSLPgPPDAIICANDDmAL 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582227628 228 GAAQAIAAT---DRKMPIIIMGNREDELkwwKEQKDAKSYETMSVSIAPGVSTLAFWVAQQILDGKEVKKDLVVPFL 301
Cdd:cd19968   196 GAIEAMRAAgldLKKVKVIGFDAVPDAL---QAIKDGELYATVEQPPGGQARTALRILVDYLKDKKAPKKVNLKPKL 269
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 72-299 4.98e-19

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


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 85.33  E-value: 4.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEP--CAWRIAVNFKEMGRSEVEYLS 149
Cdd:cd19971    37 PQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPVKDTdlVDSTIASDNYNAGKLCGEDMV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 150 KKLPDGGNLLEIRGLAGVFVDDEISaGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTqGGD--GY 227
Cdd:cd19971   117 KKLPEGAKIAVLDHPTAESCVDRID-GFLDAIKKNPKFEVVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFA-LNDpsAL 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582227628 228 GAAQAIAATDRKMPIIIMG-NREDELKwwKEQKDAKSYET---MSVSIApgvsTLAFWVAQQILDGKEVKKDLVVP 299
Cdd:cd19971   195 GALAALKAAGKLGDILVYGvDGSPDAK--AAIKDGKMTATaaqSPIEIG----KKAVETAYKILNGEKVEKEIVVP 264
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 30-307 1.57e-18

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: 84.00  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMLTSwgkVTGEAVKAG-TVAAADpfttAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAV 108
Cdd:cd06318     1 KIGFSQRTLASPYYAALVAA---AKAEAKKLGvELVVTD----AQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 109 KEACDAGITVVSFD-GIVTEP-CAWRIAVNFKEMGRSEVEYLSKKL-PDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFP 185
Cdd:cd06318    74 KAAKAAGIPVITVDsALDPSAnVATQVGRDNKQNGVLVGKEAAKALgGDPGKIIELSGDKGNEVSRDRRDGFLAGVNEYQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 186 -------QFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDG-YGAAQAIAATDR--KMPIIIMGNREDELKWW 255
Cdd:cd06318   154 lrkygksNIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMaLGAMKALKAAGMldKVKVAGADGQKEALKLI 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582227628 256 KEQKdaksYETMSVSIAPGVSTLAFWVAQQILDGKE-VKKDLVVPFLRIDQDN 307
Cdd:cd06318   234 KDGK----YVATGLNDPDLLGKTAVDTAAKVVKGEEsFPEFTYTPTALITKDN 282
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 73-246 3.76e-17

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


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 80.06  E-value: 3.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  73 ENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITV------VSFDGIVTEpcawRIAVNFKEMGRSEVE 146
Cdd:cd19967    38 QNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVflidreINAEGVAVA----QIVSDNYQGAVLLAQ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 147 YLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTqGGD- 225
Cdd:cd19967   114 YFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQYPELKMVAQQSADWDRTEAFEKMESILQANPDIKGVIC-GNDe 192

                         170       180
                  ....*....|....*....|..
gi 1582227628 226 -GYGAAQAIAATDRKMPIIIMG 246
Cdd:cd19967   193 mALGAIAALKAAGRAGDVIIVG 214
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 56-297 2.30e-16

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: 77.71  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  56 EAVKAGTVAAADPFTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVtEPCAWRIAV 135
Cdd:cd06321    23 EAAAEINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVVAVDVAA-EGADATVTT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 136 NFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEIsAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPD 215
Cdd:cd06321   102 DNVQAGYLACEYLVEQLGGKGKVAIIDGPPVSAVIDRV-NGCKEALAEYPGIKLVDDQNGKGSRAGGLSVMTRMLTAHPD 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 216 IAGVVT-QGGDGYGAAQAIAATDRKmPIIIMG-----NREDELKWWKEQKDAKSYETMSVSIAPGVStlafwVAQQILDG 289
Cdd:cd06321   181 VDGVFAiNDPGAIGALLAAQQAGRD-DIVITSvdgspEAVAALKREGSPFIATAAQDPYDMARKAVE-----LALKILNG 254


                  ....*...
gi 1582227628 290 KEVKKDLV 297
Cdd:cd06321   255 QEPAPELV 262
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
 69-300 3.50e-16

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: 77.27  E-value: 3.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  69 FTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVV----SFDGiVTEPCAWrIAVNFKEMGRSE 144
Cdd:cd06301    36 IVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPLVyvnrEPDS-KPKGVAF-VGSDDIESGELQ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 145 VEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGG 224
Cdd:cd06301   114 MEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYPGMKIVAEQTANWSREKAMDIVENWLQSGDKIDAIVANND 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 225 D-GYGAAQAIAATDRKMPIIIMG--NREDELKWWKEQKdaksyetMSVSI---APGVSTLAFWVAQQILDGKEVKKDLVV 298
Cdd:cd06301   194 EmAIGAILALEAAGKKDDILVAGidATPDALKAMKAGR-------LDATVfqdAAGQGETAVDVAVKAAKGEEVESDIWI 266


                  ..
gi 1582227628 299 PF 300
Cdd:cd06301   267 PF 268
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 73-246 1.02e-15

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


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 76.13  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  73 ENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFD----------GIVTEPCawrIAVNFKEMGR 142
Cdd:cd19970    41 ETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDnrldadalkeGGINVPF---VGPDNRQGAY 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 143 SEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPqFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTq 222
Cdd:cd19970   118 LAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAG-MKIVASQSANWEIDEANTVAANLLTAHPDIRGILC- 195

                         170       180
                  ....*....|....*....|....*.
gi 1582227628 223 GGD--GYGAAQAIAATDRKMPIIIMG 246
Cdd:cd19970   196 ANDnmALGAIKAVDAAGKAGKVLVVG 221
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 53-295 2.02e-15

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


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 75.17  E-value: 2.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  53 VTGEAVKAG-TVAAADpfttAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTE-PCA 130
Cdd:cd19972    21 VEAEAKKKGyKVITVD----AKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNPEDaPGD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 131 WRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGIL 210
Cdd:cd19972    97 TFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAEAPGIKVVAEQTADWDQDEGFKVAQDML 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 211 PSLPDIAGVVTQG-GDGYGAAQAIAATDRKMPIIIMGNREDeLKWWKEQKDAKSYETMsVSIAPGVSTLAFWVAQQILDG 289
Cdd:cd19972   177 QANPNITVFFGQSdAMALGAAQAVKVAGLDHKIWVVGFDGD-VAGLKAVKDGVLDATM-TQQTQKMGRLAVDSAIDLLNG 254


                  ....*.
gi 1582227628 290 KEVKKD 295
Cdd:cd19972   255 KAVPKE 260
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
 74-245 2.99e-15

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: 74.54  E-value: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  74 NQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSF-DGIVTEPCAWRIAVNFKEMGRSEVEYLSKKL 152
Cdd:cd06306    41 TNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLvNGIDSPKVAARVLVDFYDMGYLAGEYLVEHH 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 153 P-DGGNLLEIRGLAGVFVDDEISAGIHEGVKQfPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDGYGAAQ 231
Cdd:cd06306   121 PgKPVKVAWFPGPAGAGWAEDREKGFKEALAG-SNVEIVATKYGDTGKAVQLNLVEDALQAHPDIDYIVGNAVAAEAAVG 199

                         170
                  ....*....|....
gi 1582227628 232 AIAATDRKMPIIIM 245
Cdd:cd06306   200 ALREAGLTGKVKVV 213
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
 52-246 1.29e-14

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: 73.05  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  52 KVTG----EAVKAGTVAAADPF-------TTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVS 120
Cdd:cd06302     7 KVVGipyfDAAEEGAKKAAKELgvevvytGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVIT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 121 FDGIVTEPCA-WRIA-VNFKEMGRSEVEYLSKKLPDGGNLLEirgLAGVFVDDEISAGIHEGVKQF----PQFKIVGSVH 194
Cdd:cd06302    87 WDSDAPPSARdYFVNqADDEGLGEALVDSLAKEIGGKGKVAI---LSGSLTATNLNAWIKAMKEYLkskyPDIELVDTYY 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582227628 195 GDWAQDVAQKAVAGILPSLPDIAGVVTQGGDGY-GAAQAIAATDRKMPIIIMG 246
Cdd:cd06302   164 TDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPpAAAQAVEEAGKTGKVAVTG 216
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 30-238 1.96e-14

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: 72.33  E-value: 1.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  30 KIALSNNYAGNSWRQAMLTSwgkVTGEAVKAG-TVAAADpfttAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAV 108
Cdd:cd06305     1 TIAVVRNGTSGDWDQQALQG---AVAEAEKLGgTVIVFD----ANGDDARMADQIQQAITQKVDAIIISHGDADALDPKL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 109 KEACDAGITVVSFDGIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGlAGVFVDDEISAGIHEGVKQFPQFK 188
Cdd:cd06305    74 KKALDAGIPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKDLNGEGNIAVFNV-FGVPPLDKRYDIYKAVLKANPGIK 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582227628 189 IV----GSVHGDWAQDvAQKAVAGILPSLPDIagvvtqGGDGY---------GAAQAIAATDR 238
Cdd:cd06305   153 KIvaelGDVTPNTAAD-AQTQVEALLKKYPEG------GIDAIwaawdepakGAVQALEEAGR 208
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 69-235 2.36e-13

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


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 69.15  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  69 FTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFD-GIVTEPCAWRIAVNFKEMGRSEVEY 147
Cdd:cd19992    34 FQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDrLILNADVDLYVGRDNYKVGQLQAEY 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 148 LSKKLPDgGNLLEIRGLAGVFVDDEISAGIHEGVKQFP---QFKIVG-SVHGDWAQDVAQKAVAGILPSL-PDIAGVVTq 222
Cdd:cd19992   114 ALEAVPK-GNYVILSGDPGDNNAQLITAGAMDVLQPAIdsgDIKIVLdQYVKGWSPDEAMKLVENALTANnNNIDAVLA- 191

                         170
                  ....*....|....*
gi 1582227628 223 GGDG--YGAAQAIAA 235
Cdd:cd19992   192 PNDGmaGGAIQALKA 206
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 72-309 5.70e-13

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: 68.17  E-value: 5.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIV-TEPCAWRIAVN----FKEMGRSEVE 146
Cdd:cd06317    37 ANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAVIpSDFQAAQVGVDnlegGKEIGKYAAD 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 147 YLSKKLpDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDG 226
Cdd:cd06317   117 YIKAEL-GGQAKIGVVGALSSLIQNQRQKGFEEALKANPGVEIVATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPA 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 227 -YGAAQAIAATDRKMPIIIMGNreDELKWWKEQKDAKSYETMSVSIAP-GVSTLAFWVAQQILDGKEVKKDLVVPFLRID 304
Cdd:cd06317   196 lLGAVAAVRSQGRQGKIKVFGW--DLTKQAIFLGIDEGVLQAVVQQDPeKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVT 273


                  ....*
gi 1582227628 305 QDNLE 309
Cdd:cd06317   274 KENVD 278
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 56-257 8.59e-13

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: 67.61  E-value: 8.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  56 EAVKAGTVAAADPF-------TTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVteP 128
Cdd:cd06314    15 DLAEAGAEKAAKELgvnvefvGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFDSDA--P 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 129 CAWRIA---VNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVG--SVHGDWAQdvAQ 203
Cdd:cd06314    93 DSKRLAyigTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKGSPGIEIVDplSDNDDIAK--AV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582227628 204 KAVAGILPSLPDIAGVVTQGG-DGYGAAQAIAATDR--KMPIIIMGNREDELKWWKE 257
Cdd:cd06314   171 QNVEDILKANPDLDAIFGVGAyNGPAIAAALKDAGKvgKVKIVGFDTLPETLQGIKD 227
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
 52-247 1.13e-12

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: 67.30  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  52 KVTG----EAVKAGTVAAADP----FTT---AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVS 120
Cdd:cd20003     7 KLVGvpyfTAAGQGAQEAAKElgvdVTYdgpTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 121 FDGIVtEPCAWRIAVN---FKEMGRSEVEYLSKKLPDGGnllEIRGLAGVFVD-------DEISAGIHEgvkQFPQFKIV 190
Cdd:cd20003    87 WDSDV-NPDARDFFVNqatPEGIGKTLVDMVAEQTGEKG---KVAIVTSSPTAtnqnawiKAMKAYIAE---KYPDMKIV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582227628 191 GSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDGY-GAAQAIAATDRKMPIIIMGN 247
Cdd:cd20003   160 TTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALpGAAEAVEQLGRTGKVAVTGL 217
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 76-304 1.43e-12

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: 66.88  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  76 ATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEPC--AWRIAVNFKEMGRSEVEYLSKKLP 153
Cdd:cd20007    42 PTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVDTTLGDPSfvLSQIASDNVAGGALAAEALAELIG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 154 DGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSvhgDWAQDVAQKA---VAGILPSLPDIAGV-VTQGGDGYGA 229
Cdd:cd20007   122 GKGKVLVINSTPGVSTTDARVKGFAEEMKKYPGIKVLGV---QYSENDPAKAasiVAAALQANPDLAGIfGTNTFSAEGA 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 230 AQAIAATDRKMPIIIMG-----NREDELKwwkeqkdAKSYETMSVSIAPGVSTLAFWVAQQILDGKEVKKDLVVPFLRID 304
Cdd:cd20007   199 AAALRNAGKTGKVKVVGfdaspAQVEQLK-------AGTIDALIAQKPAEIGYLAVEQAVAALTGKPVPKDILTPFVVIT 271
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 56-239 2.28e-12

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: 66.47  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  56 EAVKAGTVAAADPFT--------TAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFD-GIVT 126
Cdd:cd20006    17 QTVKSGAEAAAKEYGvdleflgpESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDsPVNS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 127 EPCAWRIAVNFKEMGRSEVEYLSKKLPDGGNlleirglAGVFVDDEISA-------GIHEGVKQFPQFKIVGSVHGDWAQ 199
Cdd:cd20006    97 KKADSFVATDNYEAGKKAGEKLASLLGEKGK-------VAIVSFVKGSStaiereeGFKQALAEYPNIKIVETEYCDSDE 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1582227628 200 DVAQKAVAGILPSLPDIAGVVT---QGGDgyGAAQAIAATDRK 239
Cdd:cd20006   170 EKAYEITKELLSKYPDINGIVAlneQSTL--GAARALKELGLG 210
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 72-235 2.74e-12

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


Pssm-ID: 380650 [Multi-domain]  Cd Length: 294  Bit Score: 66.16  E-value: 2.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDG-IVTEPCAWRIAVNFKEMGRSEVEYLSK 150
Cdd:cd19995    40 ANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRlILGGPADYYVSFDNVAVGEAQAQSLVD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 151 KL----PDGGNLLEIRGLAGVFVDDEISAGIHEGVK---QFPQFKIVGSVHG-DWAQDVAQKAVAGILPSLPDIAGVVTQ 222
Cdd:cd19995   120 HLkaigKKGVNIVMINGSPTDNNAGLFKKGAHEVLDplgDSGELKLVCEYDTpDWDPANAQTAMEQALTKLGNNIDGVLS 199

                         170
                  ....*....|...
gi 1582227628 223 GGDGYGAAqAIAA 235
Cdd:cd19995   200 ANDGLAGG-AIAA 211
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 58-221 6.06e-12

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: 64.95  E-value: 6.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  58 VKAGTVAAADPFTTA--------ENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFD-GIVTEP 128
Cdd:cd20004    17 VKAGAEKAAQELGVEiywrgpsrEDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDsDLGGDA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 129 CAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQ-FPQFKIVGSVHGDWAQDVAQKAVA 207
Cdd:cd20004    97 VISFVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAKGSASTTDRERGFLEALKKlAPGLKVVDDQYAGGTVGEARSSAE 176

                         170
                  ....*....|....
gi 1582227628 208 GILPSLPDIAGVVT 221
Cdd:cd20004   177 NLLNQYPDVDGIFT 190
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 58-246 6.98e-12

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: 64.67  E-value: 6.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  58 VKAGTVAAAD------PFTTAENQATE--QAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFD-GIVTEP 128
Cdd:cd06310    17 VREGAEAAAKdlgvkiIFVGPESEEDVagQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPVIVIDsGIKGDA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 129 CAWRIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQ-FKIVGSVHGDWAQDVAQKAVA 207
Cdd:cd06310    97 YLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGgIKVLASQYAGSDYAKAANETE 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1582227628 208 GILPSLPDIAGVV-TQGGDGYGAAQAIAATDRKMPIIIMG 246
Cdd:cd06310   177 DLLGKYPDIDGIFaTNEITALGAAVAIKSRKLSGQIKIVG 216
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 69-246 1.20e-11

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


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 64.22  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  69 FTTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFD-GIVTEPCAWRIAVNFKEMGRSEVEY 147
Cdd:cd06322    34 VADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFTVDvKADGAKVVTHVGTDNYAGGKLAGEY 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 148 LSKklpdggNLLEIRGLAGVFVDDEISA------GIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVT 221
Cdd:cd06322   114 ALK------ALLGGGGKIAIIDYPEVESvvlrvnGFKEAIKKYPNIEIVAEQPGDGRREEALAATEDMLQANPDLDGIFA 187

                         170       180
                  ....*....|....*....|....*.
gi 1582227628 222 QGGDG-YGAAQAIAATDRKMPIIIMG 246
Cdd:cd06322   188 IGDPAaLGALTAIESAGKEDKIKVIG 213
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
 71-284 2.29e-11

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: 63.51  E-value: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  71 TAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGivTEPCAWRIAV---NFKEMGRSEVEY 147
Cdd:cd19969    37 PATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDS--DAPESKRISYvgtDNYEAGYAAAEK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 148 LSKKLPDGGNLLEIRGLaGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVV-TQGGDG 226
Cdd:cd19969   115 LAELLGGKGKVAVLTGP-GQPNHEERVEGFKEAFAEYPGIEVVAVGDDNDDPEKAAQNTSALLQAHPDLVGIFgVDASGG 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 227 YGAAQAIAATDR--KMPIIIMGNREDELKWWKEqkdaksyETMSVSIAPGVSTLAFWVAQ 284
Cdd:cd19969   194 VGAAQAVREAGKtgKVKIVAFDDDPETLDLIKD-------GVIDASIAQRPWMMGYWSLQ 246
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 39-251 4.61e-11

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


Pssm-ID: 380648 [Multi-domain]  Cd Length: 287  Bit Score: 62.49  E-value: 4.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  39 GNSWRQAMLTSWgKVTGEAVKAGTVAAADPFTTAENQ--ATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGI 116
Cdd:cd19993     3 GVSWSNFQEERW-KTDEAAMKKALEKAGAKYISADAQssAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 117 TVVSFDGIVTEPCAWRIAVNFKEMGRSEVEYLSKKLPDgGNLLEIRG-----LAGVFV---DDEISAGIHEGvkqfpQFK 188
Cdd:cd19993    82 PVIAYDRLIENPIAFYISFDNVEVGRMQARGVLKAKPE-GNYVFIKGsptdpNADFLRagqMEVLQPAIDSG-----KIK 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582227628 189 IVGSVHGD-WAQDVAQKAVAGILPSLPDIAGVVTQGGDGY--GAAQAIAATDRKMPIIIMGNREDE 251
Cdd:cd19993   156 IVGEQYTDgWKPANAQKNMEQILTANNNKVDAVVASNDGTagGAVAALAAQGLAGKVPVSGQDADK 221
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
 71-237 2.67e-10

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: 60.35  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  71 TAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVtEPCAWRIAVN---FKEMGRSEVEY 147
Cdd:cd20000    37 PTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAAGIKVVTFDSDV-APEARDLFVNqadADGIGRAQVDM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 148 LSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVK--QFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGD 225
Cdd:cd20000   116 MAELIGGEGEFAILSATPTATNQNAWIDAMKKELAspEYAGMKLVKVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTV 195

                         170
                  ....*....|...
gi 1582227628 226 GY-GAAQAIAATD 237
Cdd:cd20000   196 GIaAAARALEDSG 208
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 70-244 2.86e-10

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


Pssm-ID: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 60.33  E-value: 2.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  70 TTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVT-----EPCAWRIAVNFKEMGRSE 144
Cdd:cd06316    36 TDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKLVFMDNVPDgleagKDYVSVVSSDNRGNGQIA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 145 VEYLSKKLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQ-FPQFKIVGSVHGDWAQDVAQKAVAgILPSLPDIAGV-VTQ 222
Cdd:cd06316   116 AELLAEAIGGKGKVGIIYHDADFYATNQRDKAFKDTLKEkYPDIKIVAEQGFADPNDAEEVASA-MLTANPDIDGIyVSW 194

                         170       180
                  ....*....|....*....|..
gi 1582227628 223 GGDGYGAAQAIAATDRKMPIII 244
Cdd:cd06316   195 DTPALGVISALRAAGRSDIKIT 216
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
 70-235 5.04e-10

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


Pssm-ID: 380646 [Multi-domain]  Cd Length: 284  Bit Score: 59.56  E-value: 5.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  70 TTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTE-PCAWRIAVNFKEMGRSEVEYL 148
Cdd:cd19991    35 QSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNaDVDLYVSFDNEKVGELQAEAL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 149 SKKLPDgGNLLEIRGLagvfVDDEISAGIHEGVKQFPQ-------FKIVGS-VHGDWAQDVAQKAVAGILPSLPDIAGVV 220
Cdd:cd19991   115 VKAKPK-GNYVLLGGS----PTDNNAKLFREGQMKVLQplidsgdIKVVGDqWVDDWDPEEALKIMENALTANNNKIDAV 189

                         170
                  ....*....|....*..
gi 1582227628 221 TQGGDGY--GAAQAIAA 235
Cdd:cd19991   190 IASNDGTagGAIQALAE 206
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 71-246 6.06e-10

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


Pssm-ID: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 59.17  E-value: 6.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  71 TAENQATEQAAQIQNMILQGYDAIVLnAASPTALNGAVKEACDAGITVVSFD-GIVTEPCAWRIAVNFKEMGRSEVEYLS 149
Cdd:cd20008    38 ATEADIAGQVNLVENAISRKPDAIVL-APNDTAALVPAVEAADAGIPVVLVDsGANTDDYDAFLATDNVAAGALAADELA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 150 KKL----PDGGNLLEIRGLAGVFVDDEISAGIHEGVKQ-FPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVV-TQG 223
Cdd:cd20008   117 ELLkasgGGKGKVAIISFQAGSQTLVDREEGFRDYIKEkYPDIEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFgANN 196

                         170       180
                  ....*....|....*....|...
gi 1582227628 224 GDGYGAAQAIAATDRKMPIIIMG 246
Cdd:cd20008   197 PSAVGVAQALAEAGKAGKIVLVG 219
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
 72-163 1.23e-09

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 58.61  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTE-PCAWRIAVNFKEMGRSEVEYLSK 150
Cdd:COG4213    40 ANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVIAYDRLILNsDVDYYVSFDNVKVGELQGQYLVD 119

                          90
                  ....*....|....*
gi 1582227628 151 KLPD--GGNLLEIRG 163
Cdd:COG4213   120 GLPLkgKGNIELFGG 134
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 72-308 1.16e-08

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


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 55.44  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFD-GIVTEPCAWRIAVNFKEMGRSEVEYLSK 150
Cdd:cd06319    37 QKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIPVVIADiGTGGGDYVSYIISDNYDGGYQAGEYLAE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 151 KL----PDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGDG 226
Cdd:cd06319   117 ALkengWGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEVALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQM 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 227 Y-GAAQAIAATDRKMPIIIMG-NREDE-LKWWKEQKdaksyetMSVSIAP---GVSTLAFWVAQQILDGK-EVKKDLVVP 299
Cdd:cd06319   197 AqGALQAIEEAGRTGDILVVGfDGDPEaLDLIKDGK-------LDGTVAQqpfGMGARAVELAIQALNGDnTVEKEIYLP 269


                  ....*....
gi 1582227628 300 FLRIDQDNL 308
Cdd:cd06319   270 VLLVTSENV 278
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 71-241 1.46e-08

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: 54.97  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  71 TAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEPCAWR---IAVNFKEMGRSEVEY 147
Cdd:cd19965    37 PQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAFNVDAPGGENARlafVGQDLYPAGYVLGKR 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 148 LSKKL-PDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPqfKIVGSVHGDWAQDVAQkAVAGILPSL---PDIAGVV-TQ 222
Cdd:cd19965   117 IAEKFkPGGGHVLLGISTPGQSALEQRLDGIKQALKEYG--RGITYDVIDTGTDLAE-ALSRIEAYYtahPDIKAIFaTG 193

                         170
                  ....*....|....*....
gi 1582227628 223 GGDGYGAAQAIAatDRKMP 241
Cdd:cd19965   194 AFDTAGAGQAIK--DLGLK 210
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
 69-247 1.49e-08

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: 54.87  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  69 FTTAENQATEQAAQIQNmILQGYDAIVLNAASPTALNGAVKEACDAGITVVSfdgIVTE-PCAWRIA---VNFKEMGRSE 144
Cdd:cd06307    38 HFVDSLDPEALAAALRR-LAAGCDGVALVAPDHPLVRAAIDELAARGIPVVT---LVSDlPGSRRLAyvgIDNRAAGRTA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 145 VEYLSKKL-PDGGNLLEIRG----------LAGvFvddeiSAGIHEgvkQFPQFKIVGSV--HGDwaQDVAQKAVAGILP 211
Cdd:cd06307   114 AWLMGRFLgRRPGKVLVILGshrfrgheerEAG-F-----RSVLRE---RFPDLTVLEVLegLDD--DELAYELLRELLA 182

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1582227628 212 SLPDIAGVVTQGGDGYGAAQAIAATDRKMPIIIMGN 247
Cdd:cd06307   183 RHPDLVGIYNAGGGNEGIARALREAGRARRVVFIGH 218
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
 71-122 3.39e-08

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: 54.17  E-value: 3.39e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582227628  71 TAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFD 122
Cdd:cd19994    36 YADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYD 87
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 72-299 4.67e-08

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: 53.82  E-value: 4.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEPCAWRI-AVNFKEMGRSEVEYLSK 150
Cdd:cd20001    38 ATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDAGIVVITHEASNLKNVDYDVeAFDNAAYGAFIMDKLAE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 151 KLPDGGNLLEIRG-LAGVFVDDEISAGIHEGVKQFPQFKIVGS-VHGDWAQDVAQKAVAGILPSLPDIAGVV-TQGGDGY 227
Cdd:cd20001   118 AMGGKGKYVTFVGsLTSTSHMEWANAAVAYQKANYPDMLLVTDrVETNDDSETAYEKAKELLKTYPDLKGIVgCSSSDVP 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 228 GAAQAIAATDRKMPIIIMGNredelkwwkeqkdaksyETMSVS---IAPG-VSTLAFW-----------VAQQILDGKEV 292
Cdd:cd20001   198 GAARAVEELGLQGKIAVVGT-----------------GLPSVAgeyLEDGtIDYIQFWdpadagyamnaLAVMVLEGEKI 260


                  ....*....
gi 1582227628 293 K--KDLVVP 299
Cdd:cd20001   261 TdgTDLGVP 269
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
 74-235 8.22e-08

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 53.03  E-value: 8.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  74 NQATeQAAQIQNMILQGYDAIVLNAASPTALNGAVKEAcDAGITVVSF-DGIVTEPCAWRIAVNFKEMGRSEVEYLSKKL 152
Cdd:PRK10936   89 NLAK-QQQQLEQCVAWGADAILLGAVTPDGLNPDLELQ-AANIPVIALvNGIDSPQVTTRVGVSWYQMGYQAGRYLAQWH 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 153 PDGGNLLEI------RGLAGVfvdDEISAGIHEGVKQfPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVtqggdg 226
Cdd:PRK10936  167 PKGSKPLNVallpgpEGAGGS---KAVEQGFRAAIAG-SDVRIVDIAYGDNDKELQRNLLQELLERHPDIDYIA------ 236


                  ....*....
gi 1582227628 227 yGAAQAIAA 235
Cdd:PRK10936  237 -GSAVAAEA 244
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 57-246 3.59e-07

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: 50.70  E-value: 3.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  57 AVKAGTVAAADPF--------TTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEP 128
Cdd:cd20005    16 AVKKGAEQAAKELgvkitfegPDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGVPSD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 129 CAW-RIAVNFKEMGRSEVEYLSKKLPDGGNLLEIRGLAGVF-VDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAV 206
Cdd:cd20005    96 LPLaTVATDNYAAGALAADHLAELIGGKGKVAIVAHDATSEtGIDRRDGFKDEIKEKYPDIKVVNVQYGVGDHAKAADIA 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1582227628 207 AGILPSLPDIAGV-VTQGGDGYGAAQAIAATDRKMPIIIMG 246
Cdd:cd20005   176 KAILQANPDLKGIyATNEGAAIGVANALKEMGKLGKIKVVG 216
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 58-293 1.72e-06

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: 48.85  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  58 VKAGTVAAADPfttaenQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEPCAWRI---- 133
Cdd:cd20002    30 VNAYQVGPADA------DPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVITHESPGQKGADWDVelid 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 134 AVNFkemGRSEVEYLSKKLPDGGNLLEIRG-----LAGVFVDdeisAGIHEGVKQFPQFKIVGS-VHGDWAQDVAQKAVA 207
Cdd:cd20002   104 NEKF---GEAQMELLAKEMGGKGEYAIFVGsltvpLHNLWAD----AAVEYQKEKYPNMKQVTDrIPGGEDVDVSRQTTL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 208 GILPSLPDIAGVVTQGGDG-YGAAQAIAATDRKMPIIIMGNREDElkwwkeqkDAKSY-----ETMSVSIAPGVSTLAF- 280
Cdd:cd20002   177 ELLKAYPDLKGIISFGSLGpIGAGQALREKGLKGKVAVVGTVIPS--------QAAAYlkegsITEGYLWDPADAGYAMv 248

                         250
                  ....*....|...
gi 1582227628 281 WVAQQILDGKEVK 293
Cdd:cd20002   249 YIAKMLLDGKRKE 261
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
70-246 2.14e-06

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 48.72  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  70 TTAENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEPCAWR--------IAVNFKEMG 141
Cdd:PRK09701   62 SPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKKaggnveafVTTDNVAVG 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 142 RSEVEYLSKKL-PDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGV- 219
Cdd:PRK09701  142 AKGASFIIDKLgAEGGEVAIIEGKAGNASGEARRNGATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIy 221

                         170       180
                  ....*....|....*....|....*..
gi 1582227628 220 VTQGGDGYGAAQAIAATDRKMPIIIMG 246
Cdd:PRK09701  222 CANDTMAMGVAQAVANAGKTGKVLVVG 248
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
 72-235 2.21e-06

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: 48.57  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEP-CAWRIAVNFKEMGRSEVEYLSK 150
Cdd:cd01538    37 ADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYDRLILNAdVDYYISFDNEKVGELQAQALLD 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 151 KLPdGGNLLEIRGL-----AGVFVDDEISAgiHEGVKQFPQFKIVGSVHGD-WAQDVAQKAVAGILPSL-PDIAGVVTqG 223
Cdd:cd01538   117 AKP-EGNYVLIGGSptdnnAKLFRDGQMKV--LQPAIDSGKIKVVGDQWVDdWLPANAQQIMENALTANgNNVDAVVA-S 192

                         170
                  ....*....|....
gi 1582227628 224 GDGY--GAAQAIAA 235
Cdd:cd01538   193 NDGTagGAIAALKA 206
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 74-246 2.21e-05

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


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 45.30  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  74 NQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIVTEPcAWRI-AVNF-----KEMGRSEVEY 147
Cdd:cd06312    41 NDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAINSGDDRS-KERLgALTYvgqdeYLAGQAAGER 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 148 LSKKLPdgGNLLEIRGLAGVFVDDEISAGIHEGVKQFPQFKIVGSVHGDWAQdvAQKAVAGILPSLPDIAGVVTQGGDG- 226
Cdd:cd06312   120 ALEAGP--KNALCVNHEPGNPGLEARCKGFADAFKGAGILVELLDVGGDPTE--AQEAIKAYLQADPDTDAVLTLGPVGa 195

                         170       180
                  ....*....|....*....|
gi 1582227628 227 YGAAQAIAATDRKMPIIIMG 246
Cdd:cd06312   196 DPALKAVKEAGLKGKVKIGT 215
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
22-129 3.38e-05

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 45.17  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  22 AFAETSAKKIALSNNYAGNSWrqamLTSWGKvtgEAVKAGTVAAAD-----PfttAENQATEQAAQIQNMILQGYDAIVL 96
Cdd:PRK15408   17 SMTVQAAERIAFIPKLVGVGF----FTSGGN---GAKEAGKELGVDvtydgP---TEPSVSGQVQLINNFVNQGYNAIIV 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1582227628  97 NAASPTALNGAVKEACDAGITVVSFDGIVTEPC 129
Cdd:PRK15408   87 SAVSPDGLCPALKRAMQRGVKVLTWDSDTKPEC 119
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
 72-121 5.21e-05

periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 44.50  E-value: 5.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSF 121
Cdd:cd01539    39 AQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVIFF 88
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 79-128 6.68e-05

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: 44.00  E-value: 6.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582227628  79 QAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGiVTEP 128
Cdd:cd19973    46 QVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVLVIALDT-PTDP 94
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 175-327 3.53e-03

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


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 38.74  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 175 AGIHEGVKQFPQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGD-GYGAAQAIAATDRKM--PIIIMGnrede 251
Cdd:cd06324   161 QGLRDALAEHPDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAmALGAIDALEEAGLKPgkDVLVGG----- 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 252 LKWWKEQKDA-KSYEtMSVSIApGVSTLAFWVAQQILD---GKEVKKDLVV---PFLRIDQDNLETNLANTQAGGVANVE 324
Cdd:cd06324   236 IDWSPEALQAvKDGE-LTASVG-GHFLEGAWALVLLYDyhhGIDFAAGTSVqlkPMLAITRDNVAQYLKLFGDDNWPKID 313


                  ...
gi 1582227628 325 YTQ 327
Cdd:cd06324   314 FRQ 316
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
72-299 4.46e-03

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 38.53  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  72 AENQATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFD-GIVTEPCAWRIAVNFKEMGRSEVEYLSK 150
Cdd:PRK10653   64 SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDrGATKGEVVSHIASDNVAGGKMAGDFIAK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628 151 KLPDGGNLLEIRGLAGVFVDDEISAGIHEGVKQFpQFKIVGSVHGDWAQDVAQKAVAGILPSLPDIAGVVTQGGD-GYGA 229
Cdd:PRK10653  144 KLGEGAKVIQLEGIAGTSAARERGEGFKQAVAAH-KFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEmALGA 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582227628 230 AQAIAATDrKMPIIIMG--NREDELKWWKEQKDAKSYETMSVSI-APGVSTlafwvAQQILDGKEVKKDLVVP 299
Cdd:PRK10653  223 LRALQTAG-KSDVMVVGfdGTPDGIKAVNRGKLAATIAQQPDQIgAIGVET-----ADKVLKGEKVEAKIPVD 289
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
47-159 5.18e-03

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 38.18  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582227628  47 LTSWGKVTGEAVKAGTVAAADPFTTAEN-QATEQAAQIQNMILQGYDAIVLNAASPTALNGAVKEACDAGITVVSFDGIV 125
Cdd:PRK10355   37 LERWQKDRDIFVKKAESLGAKVFVQSANgNEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMI 116

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1582227628 126 TEP-CAWRIAVNFKEMGRSEVEYLSKKLPDGGNLL 159
Cdd:PRK10355  117 NNAdIDFYISFDNEKVGELQAKALVDKVPQGNYFL 151
 
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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