|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
32-298 |
1.55e-129 |
|
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: 369.61 E-value: 1.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQ 111
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDNPISDDDLVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPFNRASVLRADGFYAGLGENrSKFEVLSQQ 191
Cdd:cd19971 81 IPVINVDTPVKDTDLVDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLDHPTAESCVDRIDGFLDAIKKN-PKFEVVAQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 192 NGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQ 271
Cdd:cd19971 160 DGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKLGDILVYGVDGSPDAKAAIKDGKMTATAAQSPIE 239
|
250 260
....*....|....*....|....*..
gi 1046183786 272 LAKETYKVGKKVLAGESVAKEILVPTF 298
Cdd:cd19971 240 IGKKAVETAYKILNGEKVEKEIVVPTF 266
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
2-305 |
4.07e-77 |
|
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: 237.90 E-value: 4.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 2 KKFIASFLTITFFLFTSCFQLV---NADDKKPIKFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISM 78
Cdd:COG1879 2 RLALLAAVLALALALAACGSAAaeaAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 79 MEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDlVVSTVASDNFLAGKINGEQMAKDYPNGAKIAV 158
Cdd:COG1879 82 IEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSD-RVAYVGSDNYAAGRLAAEYLAKALGGKGKVAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 159 IDCPF-NRASVLRADGFYAGLGENrSKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNK 237
Cdd:COG1879 161 LTGSPgAPAANERTDGFKEALKEY-PGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046183786 238 LKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVLAGESVAKEILVPTFPITKEMI 305
Cdd:COG1879 240 KGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
32-298 |
1.73e-73 |
|
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: 227.06 E-value: 1.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQ 111
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDNPISDDDLVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVID-CPFNRASVLRADGFYAGLGENRsKFEVLSQ 190
Cdd:cd01536 81 IPVVAVDTDIDGGGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEgPPGSSTAIDRTKGFKEALKKYP-DIEIVAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 191 QNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPI 270
Cdd:cd01536 160 QPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGDIKIVGVDGTPEALKAIKDGELDATVAQDPY 239
|
250 260
....*....|....*....|....*...
gi 1046183786 271 QLAKETYKVGKKVLAGESVAKEILVPTF 298
Cdd:cd01536 240 LQGYLAVEAAVKLLNGEKVPKEILTPVT 267
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
34-301 |
6.51e-67 |
|
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: 210.60 E-value: 6.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIP 113
Cdd:cd06322 3 GVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 114 VVVIDNPISDDDlVVSTVASDNFLAGKINGEQMAKDY-PNGAKIAVIDCPFNRASVLRADGFYAGLGENRsKFEVLSQQN 192
Cdd:cd06322 83 VFTVDVKADGAK-VVTHVGTDNYAGGKLAGEYALKALlGGGGKIAIIDYPEVESVVLRVNGFKEAIKKYP-NIEIVAEQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 193 GKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLT-VAQAPIQ 271
Cdd:cd06322 161 GDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDKIKVIGFDGNPEAIKAIAKGGKIKAdIAQQPDK 240
|
250 260 270
....*....|....*....|....*....|
gi 1046183786 272 LAKETYKVGKKVLAGESVAKEILVPTFPIT 301
Cdd:cd06322 241 IGQETVEAIVKYLAGETVEKEILIPPKLYT 270
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
32-301 |
2.71e-54 |
|
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: 177.87 E-value: 2.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQ 111
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDNPISDDDlVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVID-CPFNRASVLRADGFYAGLGENrSKFEVLSQ 190
Cdd:cd06323 81 IPVITVDRSVTGGK-VVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQgIPGTSAARERGKGFHNAIAKY-PKINVVAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 191 QNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKlKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPI 270
Cdd:cd06323 159 QTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGR-KDVIVVGFDGTPDAVKAVKDGKLAATVAQQPE 237
|
250 260 270
....*....|....*....|....*....|.
gi 1046183786 271 QLAKETYKVGKKVLAGESVAKEILVPTFPIT 301
Cdd:cd06323 238 EMGAKAVETADKYLKGEKVPKKIPVPLKLVT 268
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
32-306 |
4.24e-54 |
|
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: 177.84 E-value: 4.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGdqyILVDPQY-----DQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLA 106
Cdd:cd06320 1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLG---VKVDVQAapsetDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 107 AKQKQIPVVVIDNPISDDDL------VVSTVASDNFLAGKINGEQMAKDYPNGAKIAVID-CPFNRASVLRADGFYAGLG 179
Cdd:cd06320 78 ANKKGIPVINLDDAVDADALkkaggkVTSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEgLPGNAAAEARTKGFKETFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 180 ENrSKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDG 259
Cdd:cd06320 158 KA-PGLKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTGKVLVVGTDGIPEAKKSIKAG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1046183786 260 DITLTVAQAPIQLAKETYKVGKKVLAGESVAKEILVPTFPITKEMID 306
Cdd:cd06320 237 ELTATVAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKDNVD 283
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
38-301 |
3.07e-50 |
|
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: 167.47 E-value: 3.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 38 STLNNSFFTAISDTFSEIAK--QNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVV 115
Cdd:cd06321 7 QDLGNPFFVAMVRGAEEAAAeiNPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 116 VIDNPIsddDLVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPFNRASVLRADGFYAGLGENrSKFEVLSQQNGKC 195
Cdd:cd06321 87 AVDVAA---EGADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPPVSAVIDRVNGCKEALAEY-PGIKLVDDQNGKG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 196 ALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKlKNVKVYTVDGSPDGKKAFSDGD--ITLTVAQAPIQLA 273
Cdd:cd06321 163 SRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGR-DDIVITSVDGSPEAVAALKREGspFIATAAQDPYDMA 241
|
250 260
....*....|....*....|....*....
gi 1046183786 274 KETYKVGKKVLAGESVA-KEILVPTFPIT 301
Cdd:cd06321 242 RKAVELALKILNGQEPApELVLIPSTLVT 270
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
32-303 |
9.55e-49 |
|
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: 164.12 E-value: 9.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQ 111
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDNPISDDDLVVSTVASDNFLAGKINGEQMAKDY-PNGAKIAVIDC-PFNRASVLRADGFYAGLGENR------S 183
Cdd:cd06318 81 IPVITVDSALDPSANVATQVGRDNKQNGVLVGKEAAKALgGDPGKIIELSGdKGNEVSRDRRDGFLAGVNEYQlrkygkS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 184 KFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITL 263
Cdd:cd06318 161 NIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVKVAGADGQKEALKLIKDGKYVA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1046183786 264 TVAQAPIQLAKETYKVGKKVLAGE-SVAKEILVPTFPITKE 303
Cdd:cd06318 241 TGLNDPDLLGKTAVDTAAKVVKGEeSFPEFTYTPTALITKD 281
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
32-308 |
3.93e-47 |
|
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: 160.08 E-value: 3.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQ 111
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDNPI--SDDDLVVSTVASDNFLAGKINGEQMAKDYPNG-AKIAVIDCPFNRASVL-RADGFYAGLGENrSKFEV 187
Cdd:cd06309 81 IPVILVDRTIdgEDGSLYVTFIGSDFVEEGRRAAEWLVKNYKGGkGNVVELQGTAGSSVAIdRSKGFREVIKKH-PNIKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 188 LSQQNGKCALEVTMPIAEDIIQAHP-DLQAFFAVNDPSALGVVVALKASNK--LKNVKVYTVDGSPDGKKAFSDGDITLT 264
Cdd:cd06309 160 VASQSGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLkpGKDVLVVGIDGQKDALEAIKAGELNAT 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1046183786 265 VAQAPIQlAKETYKVGKKVLAGESVAKEILVPTFPITKEMIDQY 308
Cdd:cd06309 240 VECNPLF-GPTAFDTIAKLLAGEKVPKLIIVEERLFDKDNAAEE 282
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
33-288 |
3.81e-46 |
|
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: 156.70 E-value: 3.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 33 FAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDP-QYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQ 111
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPaEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDNPISDDDlVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVI-DCPFNRASVLRADGFYAGLGENRSKFEVLS- 189
Cdd:pfam13407 81 IPVVTFDSDAPSSP-RLAYVGFDNEAAGEAAGELLAEALGGKGKVAILsGSPGDPNANERIDGFKKVLKEKYPGIKVVAe 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 190 QQNGKCALEVTMPIAEDIIQAHPD-LQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQA 268
Cdd:pfam13407 160 VEGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVLQD 239
|
250 260
....*....|....*....|
gi 1046183786 269 PIQLAKETYKVGKKVLAGES 288
Cdd:pfam13407 240 PYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
32-308 |
6.71e-44 |
|
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: 151.27 E-value: 6.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQ 111
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDNPISDDDLvVSTVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPF-NRASVLRADGFYAGLgENRSKFEVLSQ 190
Cdd:cd06313 81 IPLVGVNALIENEDL-TAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIgQSAQIDRGKGIENVL-KKYPDIKVLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 191 QNGKCALEVTMPIAEDIIQAHPD-LQAFFAVNDPSALGVVVALKASNKlKNVKVYTVDGSPDGKKAFSDGDITLTVAQAP 269
Cdd:cd06313 159 QTANWSRDEAMSLMENWLQAYGDeIDGIIAQNDDMALGALQAVKAAGR-DDIPVVGIDGIEDALQAVKSGELIATVLQDA 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 1046183786 270 IQLAKETYKVGKKVLAGESVAKEILVPTFPITKEMIDQY 308
Cdd:cd06313 238 EAQGKGAVEVAVDAVKGEGVEKKYYIPFVLVTKDNVDDY 276
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
34-302 |
3.14e-42 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 147.54 E-value: 3.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIP 113
Cdd:PRK10653 30 ALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 114 VVVIDNPISDDDlVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVID-CPFNRASVLRADGFYAGLGENrsKFEVLSQQN 192
Cdd:PRK10653 110 VITLDRGATKGE-VVSHIASDNVAGGKMAGDFIAKKLGEGAKVIQLEgIAGTSAARERGEGFKQAVAAH--KFNVLASQP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 193 GKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKnVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQL 272
Cdd:PRK10653 187 ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGIKAVNRGKLAATIAQQPDQI 265
|
250 260 270
....*....|....*....|....*....|
gi 1046183786 273 AKETYKVGKKVLAGESVAKEILVPTFPITK 302
Cdd:PRK10653 266 GAIGVETADKVLKGEKVEAKIPVDLKLVTK 295
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
34-308 |
4.81e-42 |
|
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: 146.75 E-value: 4.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIP 113
Cdd:cd06317 3 ALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 114 VVVIDNPISDDDlVVSTVASDNFLAGKINGEQMA---KDYPNG-AKIAVIDCPFNRASVLRADGFYAGLgENRSKFEVLS 189
Cdd:cd06317 83 VIAYDAVIPSDF-QAAQVGVDNLEGGKEIGKYAAdyiKAELGGqAKIGVVGALSSLIQNQRQKGFEEAL-KANPGVEIVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 190 QQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKA-FSDGDITLTVAQA 268
Cdd:cd06317 161 TVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQGKIKVFGWDLTKQAIFLgIDEGVLQAVVQQD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1046183786 269 PIQLAKETYKVGKKVLAGESVAKEILVPTFPITKEMIDQY 308
Cdd:cd06317 241 PEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTKENVDQF 280
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
34-298 |
1.11e-41 |
|
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: 145.54 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIP 113
Cdd:cd19967 3 AVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 114 VVVIDNPISDDDLVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPFNRA-SVLRADGFYAGLgENRSKFEVLSQQN 192
Cdd:cd19967 83 VFLIDREINAEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTnAQLRSQGFHSVI-DQYPELKMVAQQS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 193 GKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQL 272
Cdd:cd19967 162 ADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRAGDVIIVGFDGSNDVRDAIKEGKISATVLQPAKLI 241
|
250 260
....*....|....*....|....*.
gi 1046183786 273 AKETYKVGKKVLAGESVAKEILVPTF 298
Cdd:cd19967 242 ARLAVEQADQYLKGGSTGKEEKQLFD 267
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
32-300 |
1.13e-41 |
|
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: 145.38 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGD-QYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQK 110
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKYPNvELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 111 QIPVVVIDNPISDDDlVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVID-CPFNRASVLRADGFYAGLGENrSKFEVLS 189
Cdd:cd06308 81 GIPVIVLDRKVSGDD-YTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQgLPGSSPAIDRHKGFLEAIAKY-PGIKIVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 190 QQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPD-GKKAFSDGDITLTVaqA 268
Cdd:cd06308 159 SQDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKEIKIIGVDGLPEaGEKAVKDGILAATF--L 236
|
250 260 270
....*....|....*....|....*....|..
gi 1046183786 269 PIQLAKETYKVGKKVLAGESVAKEILVPTFPI 300
Cdd:cd06308 237 YPTGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
31-301 |
1.21e-40 |
|
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: 142.76 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 31 IKFAFITSTLNNSFFTAISDTFSEIAK-QNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQ 109
Cdd:cd06301 1 IKIGVSMQNFSDEFLTYLRDAIEAYAKeYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 110 KQIPVVVID-NPISDDDLVVStVASDNFLAGKINGEQMAKDYPNGAKIAVID-CPFNRASVLRADGFYAGLGENrSKFEV 187
Cdd:cd06301 81 AGIPLVYVNrEPDSKPKGVAF-VGSDDIESGELQMEYLAKLLGGKGNIAILDgVLGHEAQILRTEGNKDVLAKY-PGMKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 188 LSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQ 267
Cdd:cd06301 159 VAEQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDDILVAGIDATPDALKAMKAGRLDATVFQ 238
|
250 260 270
....*....|....*....|....*....|....
gi 1046183786 268 APIQLAKETYKVGKKVLAGESVAKEILVPTFPIT 301
Cdd:cd06301 239 DAAGQGETAVDVAVKAAKGEEVESDIWIPFELVT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
32-292 |
5.58e-40 |
|
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: 141.21 E-value: 5.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDP--QYDQAKQISMMEDVINQKVDIIYLIAVDSEGIrQGLLAAKQ 109
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPatEADIAGQVNLVENAISRKPDAIVLAPNDTAAL-VPAVEAAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 110 KQIPVVVIDNPISDDDlVVSTVASDNFLAGKINGEQMAK----DYPNGAKIAVID-CPFNRASVLRADGFYAGLGENRSK 184
Cdd:cd20008 80 AGIPVVLVDSGANTDD-YDAFLATDNVAAGALAADELAEllkaSGGGKGKVAIISfQAGSQTLVDREEGFRDYIKEKYPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 185 FEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLT 264
Cdd:cd20008 159 IEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAGKIVLVGFDSSPDEVALLKSGVIKAL 238
|
250 260
....*....|....*....|....*...
gi 1046183786 265 VAQAPIQLAKETYKVGKKVLAGESVAKE 292
Cdd:cd20008 239 VVQDPYQMGYEGVKTAVKALKGEEIVEK 266
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
32-305 |
5.90e-39 |
|
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: 138.65 E-value: 5.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQ 111
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDNPISDDDlVVSTVASDNFLAGKINGEQMAK----DYPNGAKIAVIDCPFNRA-SVLRADGFYAGLGENrSKFE 186
Cdd:cd06319 81 IPVVIADIGTGGGD-YVSYIISDNYDGGYQAGEYLAEalkeNGWGGGSVGIIAIPQSRVnGQARTAGFEDALEEA-GVEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 187 VLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVA 266
Cdd:cd06319 159 VALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGDILVVGFDGDPEALDLIKDGKLDGTVA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1046183786 267 QAPIQLAKETYKVGKKVLAGES-VAKEILVPTFPITKEMI 305
Cdd:cd06319 239 QQPFGMGARAVELAIQALNGDNtVEKEIYLPVLLVTSENV 278
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
56-303 |
4.66e-37 |
|
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: 133.52 E-value: 4.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 56 AKQNGDQYILVDPQY--DQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPIsDDDLVVSTVAS 133
Cdd:cd20005 25 AKELGVKITFEGPDTesDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGV-PSDLPLATVAT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 134 DNFLAGKINGEQMAKDYPNGAKIAVIDCPFN-RASVLRADGFYAGLGENRSKFEVLSQQNGKCALEVTMPIAEDIIQAHP 212
Cdd:cd20005 104 DNYAAGALAADHLAELIGGKGKVAIVAHDATsETGIDRRDGFKDEIKEKYPDIKVVNVQYGVGDHAKAADIAKAILQANP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 213 DLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVLAGESVAKE 292
Cdd:cd20005 184 DLKGIYATNEGAAIGVANALKEMGKLGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAAVKALKGEEVEKL 263
|
250
....*....|.
gi 1046183786 293 ILVPTFPITKE 303
Cdd:cd20005 264 IDTGAKWYDKD 274
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
32-301 |
5.78e-37 |
|
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: 133.13 E-value: 5.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILV-DPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQK 110
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQgPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 111 QIPVVVIDNPISDDDLVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPFNRASV-LRADGFYAGLGENrSKFEVLS 189
Cdd:cd20007 81 GIKVVTVDTTLGDPSFVLSQIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTdARVKGFAEEMKKY-PGIKVLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 190 QQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAP 269
Cdd:cd20007 160 VQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGKVKVVGFDASPAQVEQLKAGTIDALIAQKP 239
|
250 260 270
....*....|....*....|....*....|..
gi 1046183786 270 IQLAKETYKVGKKVLAGESVAKEILVPTFPIT 301
Cdd:cd20007 240 AEIGYLAVEQAVAALTGKPVPKDILTPFVVIT 271
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
32-301 |
6.93e-37 |
|
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: 132.90 E-value: 6.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQ 111
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDNPISDDDLVVStVASDNFLAGKINGEQMAKDYPNGAKIAVI-DCPFNRASVLRADGFYAGLgENRSKFEVLSQ 190
Cdd:cd19968 81 IPVVTVDRRAEGAAPVPH-VGADNVAGGREVAKFVVDKLPNGAKVIELtGTPGSSPAIDRTKGFHEEL-AAGPKIKVVFE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 191 QNGKCALEVTMPIAEDIIQAHP-DLQAFFAVNDPSALGVVVALKASN-KLKNVKVYTVDGSPDGKKAFSDGDITLTVAQA 268
Cdd:cd19968 159 QTGNFERDEGLTVMENILTSLPgPPDAIICANDDMALGAIEAMRAAGlDLKKVKVIGFDAVPDALQAIKDGELYATVEQP 238
|
250 260 270
....*....|....*....|....*....|...
gi 1046183786 269 PIQLAKETYKVGKKVLAGESVAKEILVPTFPIT 301
Cdd:cd19968 239 PGGQARTALRILVDYLKDKKAPKKVNLKPKLIT 271
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
32-301 |
3.57e-36 |
|
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: 130.78 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQ-YDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQK 110
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQkSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 111 QIPVVVIDNPiSDDDLVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVI-DCPFNRASVLRADGFYAGLGEnRSKFEVLS 189
Cdd:cd06314 81 GIPVITFDSD-APDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIItGGLGADNLNERIQGFKDALKG-SPGIEIVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 190 QQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAP 269
Cdd:cd06314 159 PLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVIAATVGQRP 238
|
250 260 270
....*....|....*....|....*....|...
gi 1046183786 270 IQLAKETYKVGKKVL-AGESVAKEILVPTFPIT 301
Cdd:cd06314 239 YEMGYLSVKLLYKLLkGGKPVPDVIDTGVDVVT 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
32-301 |
5.28e-35 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 127.84 E-value: 5.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILV--DPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQ 109
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVgpESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 110 KQIPVVVIDNPIsDDDLVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPFNRASVL-RADGFYAGLGENRSKFEVL 188
Cdd:cd06310 81 KGIPVIVIDSGI-KGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDqREEGFKEYLKKHPGGIKVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 189 SQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQA 268
Cdd:cd06310 160 ASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIVGFDSQEELLDALKNGKIDALVVQN 239
|
250 260 270
....*....|....*....|....*....|...
gi 1046183786 269 PIQLAKETYKVGKKVLAGESVAKEILVPTFPIT 301
Cdd:cd06310 240 PYEIGYEGIKLALKLLKGEEVPKNIDTGAELIT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
71-302 |
2.97e-34 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 125.81 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 71 DQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPIsDDDLVVSTVASDNFLAGKINGEQMAKDY 150
Cdd:cd20004 42 DVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDSDL-GGDAVISFVATDNYAAGRLAAKRMAKLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 151 PNGAKIAVIDCPFNRASVL-RADGFYAGLGENRSKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVV 229
Cdd:cd20004 121 NGKGKVALLRLAKGSASTTdRERGFLEALKKLAPGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGAL 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046183786 230 VALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVLAGESVAKEILVPTFPITK 302
Cdd:cd20004 201 RALRRLGLAGKVKFIGFDASDLLLDALRAGEISALVVQDPYRMGYLGVKTAVAALRGKPVPKRIDTGVVLVTK 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
44-301 |
1.06e-33 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 124.48 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 44 FFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISD 123
Cdd:cd19972 13 FFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNPED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 124 DDLVvSTVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPF-NRASVLRADGFYAGLGENRSKfEVLSQQNGKCALEVTMP 202
Cdd:cd19972 93 APGD-TFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLgTTPEVDRTKGFQEALAEAPGI-KVVAEQTADWDQDEGFK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 203 IAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKK 282
Cdd:cd19972 171 VAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDHKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKMGRLAVDSAID 250
|
250
....*....|....*....
gi 1046183786 283 VLAGESVAKEILVPTFPIT 301
Cdd:cd19972 251 LLNGKAVPKEQLQDAVLTT 269
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
32-297 |
2.76e-33 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380625 [Multi-domain] Cd Length: 275 Bit Score: 123.51 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILV---DPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAK 108
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEANGYELLVkgiKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 109 QKQIPVVVIDNPISDDDLV-----VSTVASDNFLAGKINGEQMAKDYPNGAKIAVID-CPFNRASVLRADGFYAGLGENr 182
Cdd:cd19970 81 DAGIAVINIDNRLDADALKegginVPFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEgIPGADNAQQRKAGFLKAFEEA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 183 sKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDIT 262
Cdd:cd19970 160 -GMKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGKVLVVGFDNIPAVRPLLKDGKML 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1046183786 263 LTVAQAPIQLAKETYKVGKKVLAGESVAKEILVPT 297
Cdd:cd19970 239 ATIDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPV 273
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
71-302 |
2.30e-28 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 110.38 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 71 DQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPIsDDDLVVSTVASDNFLAGKINGEQMAKDY 150
Cdd:cd20006 44 DIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSPV-NSKKADSFVATDNYEAGKKAGEKLASLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 151 PNGAKIAVIDcpFNRAS---VLRADGFYAGLGENrSKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALG 227
Cdd:cd20006 123 GEKGKVAIVS--FVKGSstaIEREEGFKQALAEY-PNIKIVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLG 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046183786 228 VVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVLAGESVAKEILVPTFPITK 302
Cdd:cd20006 200 AARALKELGLGGKVKVVGFDSSVEEIQLLEEGIIDALVVQNPFNMGYLSVQAAVDLLNGKKIPKRIDTGSVVITK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
36-273 |
2.73e-27 |
|
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: 107.94 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 36 ITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQY--DQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIP 113
Cdd:cd19973 5 ITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKIdgDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 114 VVVIDNPISDDDLVVSTVASDNFLAGKINGE-QMAKDYPNGAKIAVIDC-PFNRASVLRADGFYAGLG---------ENR 182
Cdd:cd19973 85 VIALDTPTDPIDAADATFATDNFKAGVLIGEwAKAALGAKDAKIATLDLtPGHTVGVLRHQGFLKGFGidekdpesnEDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 183 SKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDIT 262
Cdd:cd19973 165 DDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKEKGVLIVSVDGGCPGVKDVKDGIIG 244
|
250
....*....|.
gi 1046183786 263 LTVAQAPIQLA 273
Cdd:cd19973 245 ATSQQYPLRMA 255
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
32-314 |
1.14e-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: 380539 [Multi-domain] Cd Length: 294 Bit Score: 106.17 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTA----ISDTFSEiakqNGDQYILV-DPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLA 106
Cdd:cd06316 1 KVAIAMHTTGSDWSRLqvagIKDTFEE----LGIEVVAVtDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 107 AKQKQIPVVVIDNPISD----DDlVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVI--DCPFnRASVLRADGFYAGLGE 180
Cdd:cd06316 77 VADAGIKLVFMDNVPDGleagKD-YVSVVSSDNRGNGQIAAELLAEAIGGKGKVGIIyhDADF-YATNQRDKAFKDTLKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 181 NRSKFEVLSQQNGKCALEvTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKAsNKLKNVKVYTVDGSPDGKKAFSDGD 260
Cdd:cd06316 155 KYPDIKIVAEQGFADPND-AEEVASAMLTANPDIDGIYVSWDTPALGVISALRA-AGRSDIKITTVDLGTEIALDMAKGG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1046183786 261 ITL-TVAQAPIQLAKETYKVGKKVLAGESVAKEILVPTFPITKEMIDQYGVKVWQ 314
Cdd:cd06316 233 NVKgIGAQRPYDQGVAEALAAALALLGKEVPPFIGVPPLAVTKDNLLEAWKQIFK 287
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
40-300 |
1.18e-26 |
|
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: 105.74 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 40 LNNSFFTAISDTFSEIAKQNGDQYILVDPQ--YDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVI 117
Cdd:cd06306 9 LKDSYWVGVNYGIVDEAKRLGVKLTVYEAGgyTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 118 DNPISDDDlVVSTVASDNFLAGKINGEQMAKDYPNGA-KIAVIDCPFNRASV-LRADGFYAGLGEnrSKFEVLSQQNGKC 195
Cdd:cd06306 89 VNGIDSPK-VAARVLVDFYDMGYLAGEYLVEHHPGKPvKVAWFPGPAGAGWAeDREKGFKEALAG--SNVEIVATKYGDT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 196 ALEVTMPIAEDIIQAHPDLQAFFAvNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKE 275
Cdd:cd06306 166 GKAVQLNLVEDALQAHPDIDYIVG-NAVAAEAAVGALREAGLTGKVKVVSTYLTPGVYRGIKRGKILAAPSDQPVLQGRI 244
|
250 260
....*....|....*....|....*
gi 1046183786 276 TYKVGKKVLAGESVAKEILVPTFPI 300
Cdd:cd06306 245 AVDQAVRALEGKPVPKHVGPPILVV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
32-269 |
2.08e-24 |
|
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: 99.65 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQ-YDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQK 110
Cdd:cd19965 1 KFVFVTHVTTNPFFQPVKKGMDDACELLGAECQFTGPQtFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 111 QIPVVVIDNPISD-DDLVVSTVASDNFLAGKINGEQMAKDY-PNGAKIAVIDC-PFNRASVLRADGFYAGLGENRSKF-- 185
Cdd:cd19965 81 GIPVVAFNVDAPGgENARLAFVGQDLYPAGYVLGKRIAEKFkPGGGHVLLGIStPGQSALEQRLDGIKQALKEYGRGIty 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 186 EVLSQQNGkcaLEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTV 265
Cdd:cd19965 161 DVIDTGTD---LAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGKVLVGGFDLVPEVLQGIKAGYIDFTI 237
|
....
gi 1046183786 266 AQAP 269
Cdd:cd19965 238 DQQP 241
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
32-300 |
5.24e-23 |
|
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: 95.83 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFT-AISDTFSEIAKQnGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQK 110
Cdd:cd06305 1 TIAVVRNGTSGDWDQqALQGAVAEAEKL-GGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 111 QIPVVVIDNPISDDDLVVSTvaSDNFLAGKINGEQMAKDYPNGAKIAVidcpFNRASVL----RADGFYAGLGENRS-KF 185
Cdd:cd06305 80 GIPVVTFDTDSQVPGVNNIT--QDDYALGTLSLGQLVKDLNGEGNIAV----FNVFGVPpldkRYDIYKAVLKANPGiKK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 186 EV--LSQQNGKCALEvTMPIAEDIIQAHPD--LQAFFAVNDPSALGVVVALKASNKLKnVKVYTVDGSPDGKKAFSDGD- 260
Cdd:cd06305 154 IVaeLGDVTPNTAAD-AQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRTD-IKVYGVDISNQDLELMADEGs 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1046183786 261 -ITLTVAQAPIQLAKETYKVGKKVLAGESV-AKEILVPTFPI 300
Cdd:cd06305 232 pWVATAAQDPALIGTVAVRNVARKLAGEDLpDKYSLVPVLIT 273
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
50-312 |
9.31e-23 |
|
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: 95.34 E-value: 9.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 50 DTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDLVVs 129
Cdd:cd19992 19 EYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDRLILNADVDL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 130 TVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPFNRASVLRADGFYAGLGENRSKFE---VLSQQNGKCALEVTMPIAED 206
Cdd:cd19992 98 YVGRDNYKVGQLQAEYALEAVPKGNYVILSGDPGDNNAQLITAGAMDVLQPAIDSGDikiVLDQYVKGWSPDEAMKLVEN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 207 -IIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVLA 285
Cdd:cd19992 178 aLTANNNNIDAVLAPNDGMAGGAIQALKAQGLAGKVFVTGQDAELAALKRIVEGTQTMTVWKDLKELARAAADAAVKLAK 257
|
250 260
....*....|....*....|....*..
gi 1046183786 286 GEsvakeilvpTFPITKEMIDQYGVKV 312
Cdd:cd19992 258 GE---------KPQTTDETINNGGKDV 275
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
67-269 |
1.84e-22 |
|
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: 94.33 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 67 DPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVID--NPISDDdlvVSTVASDNFLAGKINGE 144
Cdd:cd19969 37 PATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDsdAPESKR---ISYVGTDNYEAGYAAAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 145 QMAKDYPNGAKIAVIDCPFNRASVLRADGFYAGLGENRSkFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPS 224
Cdd:cd19969 114 KLAELLGGKGKVAVLTGPGQPNHEERVEGFKEAFAEYPG-IEVVAVGDDNDDPEKAAQNTSALLQAHPDLVGIFGVDASG 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1046183786 225 ALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAP 269
Cdd:cd19969 193 GVGAAQAVREAGKTGKVKIVAFDDDPETLDLIKDGVIDASIAQRP 237
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
34-308 |
5.17e-22 |
|
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: 93.84 E-value: 5.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGD---QYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQK 110
Cdd:cd19996 3 GFSNAGLGNSWRVQMIAEFEAEAAKLKKlikELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 111 QIPVVVIDNPISDDDlVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVID-CPFNRASVLRADGFYAGLGENrSKFEVLS 189
Cdd:cd19996 83 GIPVVLFDSGVGSDK-YTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRgIAGVSVSEDRWAGAKEVFKEY-PGIKIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 190 QQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKnVKVyTVDGSPDGKKAFSDG-DITLTVAQA 268
Cdd:cd19996 161 EVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPL-VPM-TGEDNNGFLKAWKELpGFKSIAPSY 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1046183786 269 PIQLAKETYKVGKKVLAGESVAKEILVPTFPITKEMIDQY 308
Cdd:cd19996 239 PPWLGATALDAALAALEGEPVPKYVYIPLPVITDENLDQY 278
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
1-302 |
1.96e-21 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 92.24 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 1 MKKFIASFLTITFFLFTSCFQLVNADdkkpikFAFITSTLNNSFFTAISDTFSEIAKQNGdqyILVD-----PQYDQAKQ 75
Cdd:PRK09701 1 MNKYLKYFSGTLVGLMLSTSAFAAAE------YAVVLKTLSNPFWVDMKKGIEDEAKTLG---VSVDifaspSEGDFQSQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 76 ISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDL------VVSTVASDNFLAGKiNGEQMAKD 149
Cdd:PRK09701 72 LQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLkkaggnVEAFVTTDNVAVGA-KGASFIID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 150 Y--PNGAKIAVIDCPFNRASvlradgfyaglGENR-----------SKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQA 216
Cdd:PRK09701 151 KlgAEGGEVAIIEGKAGNAS-----------GEARrngateafkkaSQIKLVASQPADWDRIKALDVATNVLQRNPNIKA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 217 FFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKV------GKKVLAGESVA 290
Cdd:PRK09701 220 IYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLmvdaekSGKVIPLDKAP 299
|
330
....*....|..
gi 1046183786 291 KEILVPTFPITK 302
Cdd:PRK09701 300 EFKLVDSILVTQ 311
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
31-292 |
2.10e-21 |
|
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: 91.88 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 31 IKFAFITSTLNNSFFTAISDTFSEIAKQNGD-QYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQ 109
Cdd:cd01539 1 IKIGVFIYNYDDTFISSVRKALEKAAKAGGKiELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 110 KQIPVVVIDNPISDDDLVVST----VASDNFLAGKINGEQMAKDYPNGAKIA-----VIDC------PFNRASVLRADGF 174
Cdd:cd01539 81 ANIPVIFFNREPSREDLKSYDkayyVGTDAEESGIMQGEIIADYWKANPEIDkngdgKIQYvmlkgePGHQDAIARTKYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 175 YAGLGENRSKFEVLSQQNG----KCALEVTmpiaEDIIQAHPD-LQAFFAVNDPSALGVVVALKA-----SNKLKNVKVY 244
Cdd:cd01539 161 VKTLNDAGIKTEQLAEDTAnwdrAQAKDKM----DAWLSKYGDkIELVIANNDDMALGAIEALKAagyntGDGDKYIPVF 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1046183786 245 TVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVLAGESVAKE 292
Cdd:cd01539 237 GVDATPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLET 284
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
32-299 |
1.43e-20 |
|
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: 89.61 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDP-QYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQK 110
Cdd:cd06302 1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTGPtQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 111 QIPVVVIDNPISDDDLVVSTVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPFNRASV-LRADGFYAGLGENRSKFEVLS 189
Cdd:cd06302 81 GIKVITWDSDAPPSARDYFVNQADDEGLGEALVDSLAKEIGGKGKVAILSGSLTATNLnAWIKAMKEYLKSKYPDIELVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 190 QQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVdGSPDGKKAF-SDGDITLTVAQA 268
Cdd:cd06302 161 TYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGKVAVTGI-GLPNTARPYlKDGSVKEGVLWD 239
|
250 260 270
....*....|....*....|....*....|.
gi 1046183786 269 PIQLAKETYKVGKKVLAGESVAKEILVPTFP 299
Cdd:cd06302 240 PAKLGYLTVYAAYQLLKGKGFTEDSDDVGTG 270
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
74-297 |
9.08e-19 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 84.34 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 74 KQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDLVVsTVASDNFLAGKINGEQMAKDYPNG 153
Cdd:cd06311 43 EQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYDL-YVAGDNPGMGVVSAEYIGKKLGGK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 154 AKIAVIDCPFNRA-SVLRADGFYAGLGENrSKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVAL 232
Cdd:cd06311 122 GNVVVLEVPSSGSvNEERVAGFKEVIKGN-PGIKILAMQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAI 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046183786 233 KASnKLKNVKVYTVDGspdGKKAF-----SDGDITLTVAQAPIQLAKETYKVGKKVL-AGESVAKEILVPT 297
Cdd:cd06311 201 KEA-GRTDIKVMTGGG---GSQEYfkrimDGDPIWPASATYSPAMIADAIKLAVLILkGGKTVEKEVIIPS 267
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
34-236 |
1.21e-18 |
|
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.
Pssm-ID: 380491 [Multi-domain] Cd Length: 264 Bit Score: 83.72 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVD-IIYLIAVDSEGIrqgLLAAKQKQI 112
Cdd:cd06267 3 GLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDgIILAPSSLDDEL---LEELLAAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 113 PVVVIDNPISDDDlvVSTVASDNFLAGKINGEQMAKdypNGAK-IAVIDCPFN-RASVLRADGFYAGLGENRSKFEVLSQ 190
Cdd:cd06267 80 PVVLIDRRLDGLG--VDSVVVDNYAGAYLATEHLIE---LGHRrIAFIGGPLDlSTSRERLEGYRDALAEAGLPVDPELV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1046183786 191 QNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASN 236
Cdd:cd06267 155 VEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELG 200
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
32-308 |
1.28e-18 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 84.58 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFIT-STLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLL-AAKQ 109
Cdd:cd06324 1 RVVFINpGKEDEPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARPPKPDYLILVNEKGVAPELLeLAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 110 KQIPVVVIDNPISDDDLV------------VSTVASDNFLAGkingEQMAKD-------YPNGAKIAVI------DCPfn 164
Cdd:cd06324 81 AKIPVFLINNDLTDEERAllgkprekfkywLGSIVPDNEQAG----YLLAKAlikaarkKSDDGKIRVLaisgdkSTP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 165 rASVLRADGFYAGLGEnRSKFEVL-------SQQNGKcalevtmPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNK 237
Cdd:cd06324 155 -ASILREQGLRDALAE-HPDVTLLqivyanwSEDEAY-------QKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 238 L--KNVKVYTVDGSPDGKKAFSDGDITLTV-------AQAPIQLAKetYKVGKKVLAGESVakeILVPTFPITKEMIDQY 308
Cdd:cd06324 226 KpgKDVLVGGIDWSPEALQAVKDGELTASVgghflegAWALVLLYD--YHHGIDFAAGTSV---QLKPMLAITRDNVAQY 300
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
34-234 |
1.29e-18 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 84.87 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVD-IIYLIAVDSEGIRQGLLAAKqkqI 112
Cdd:COG1609 65 GVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDgLILAGSRLDDARLERLAEAG---I 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 113 PVVVIDNPISDDDlvVSTVASDNFLAGKINGEQMAKdypNGAK-IAVIDCPFN-RASVLRADGFYAGLGENRSKFEVLSQ 190
Cdd:COG1609 142 PVVLIDRPLPDPG--VPSVGVDNRAGARLATEHLIE---LGHRrIAFIGGPADsSSARERLAGYREALAEAGLPPDPELV 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1046183786 191 QNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKA 234
Cdd:COG1609 217 VEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALRE 260
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
32-269 |
1.34e-17 |
|
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: 80.74 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFIT-STLNNSFFTAISDTFSEIAK-QNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQ 109
Cdd:cd06312 1 TIYVIShGSPSDPFWSVVKKGAKDAAKdLGVTVQYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 110 KQIPVVVIDNPISDDDLVVST---VASDNFLAGKINGEQMAKDYPNGAKIaVIDCPFNRASVLRADGFYAGLGENRSKFE 186
Cdd:cd06312 81 AGIPVIAINSGDDRSKERLGAltyVGQDEYLAGQAAGERALEAGPKNALC-VNHEPGNPGLEARCKGFADAFKGAGILVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 187 VLS--QQNGKCALEVtmpiaEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLT 264
Cdd:cd06312 160 LLDvgGDPTEAQEAI-----KAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKVKIGTFDLSPETLEAIKDGKILFA 234
|
....*
gi 1046183786 265 VAQAP 269
Cdd:cd06312 235 IDQQP 239
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
34-275 |
3.55e-16 |
|
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380514 [Multi-domain] Cd Length: 264 Bit Score: 76.79 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVD-IIylIAVDSEGIRQgllaAKQKQI 112
Cdd:cd06291 3 GLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDgII--LGSHSLDIEE----YKKLNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 113 PVVVIDNPISDDdlvVSTVASDNFLAGKINGEQMAKdypNGAK-IAVIDCPFNR-ASVLRADGFYAGLGENRSKFEVLSQ 190
Cdd:cd06291 77 PIVSIDRYLSEG---IPSVSSDNYQGGRLAAEHLIE---KGCKkILHIGGPSNNsPANERYRGFEDALKEAGIEYEIIEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 191 QNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNK--LKNVKVYTVDGSPDGKKAFSdgDITlTVAQa 268
Cdd:cd06291 151 DENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIrvPEDVQIIGFDGIEISELLYP--ELT-TIRQ- 226
|
....*...
gi 1046183786 269 PI-QLAKE 275
Cdd:cd06291 227 PIeEMAKE 234
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
32-273 |
3.74e-15 |
|
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: 74.13 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVD----PQYDQAKQISMMEDvINQKVDIIYLIAVDSEGIRQGLLAA 107
Cdd:cd06307 1 RFGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRihfvDSLDPEALAAALRR-LAAGCDGVALVAPDHPLVRAAIDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 108 KQKQIPVVVIDNPISDDDLvVSTVASDNFLAGKINGEQMAK-DYPNGAKIAVID-CPFNRASVLRADGFYAGLGENRSKF 185
Cdd:cd06307 80 AARGIPVVTLVSDLPGSRR-LAYVGIDNRAAGRTAAWLMGRfLGRRPGKVLVILgSHRFRGHEEREAGFRSVLRERFPDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 186 EVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSAlGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTV 265
Cdd:cd06307 159 TVLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNE-GIARALREAGRARRVVFIGHELTPETRRLLRDGTIDAVI 237
|
....*...
gi 1046183786 266 AQAPIQLA 273
Cdd:cd06307 238 DQDPELQA 245
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
42-314 |
9.81e-15 |
|
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380523 [Multi-domain] Cd Length: 302 Bit Score: 73.13 E-value: 9.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 42 NSFFTAISDTFSEIAKQNGDQ-----YILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVV 116
Cdd:cd06300 11 NSWREQMIASLKADAAQSGQKglvkeLIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 117 IDNPISDDDLVVstVASDNFLAGKINGEQMAKDYPNGAKIAVID-CPFNRASVLRADGFYAGLGENrSKFEVLSQQNGKC 195
Cdd:cd06300 91 FDGAVTSPDAYN--VSNDQVEWGRLGAKWLFEALGGKGNVLVVRgIAGAPASADRHAGVKEALAEY-PGIKVVGEVFGGW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 196 ALEVTMPIAEDIIQAHPDLQAfFAVNDPSALGVVVALKASNKLKnVKVYTVDGSPDGKKAFSDGDITLTVAQA--PIQLA 273
Cdd:cd06300 168 DEATAQTAMLDFLATHPQVDG-VWTQGGEDTGVLQAFQQAGRPP-VPIVGGDENGFAKQWWKHPKKGLTGAAVwpPPAIG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1046183786 274 KETYKVGKKVLAGESVA-KEILVPTFPIT-KEMIDQYGVKVWQ 314
Cdd:cd06300 246 AAGLEVALRLLEGQGPKpQSVLLPPPLITnDDAKAWYKDDCPD 288
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
32-306 |
1.34e-14 |
|
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: 72.70 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDP-QYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQK 110
Cdd:cd20003 1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVDVTYDGPtEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 111 QIPVVVIDNPISDD--DLVVSTVASDNFlaGKINGEQMAKDYPNGAKIAVIDCPFNRASVLR-ADGFYAGLGENRSKFEV 187
Cdd:cd20003 81 GIKVVTWDSDVNPDarDFFVNQATPEGI--GKTLVDMVAEQTGEKGKVAIVTSSPTATNQNAwIKAMKAYIAEKYPDMKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 188 LSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVyTVDGSPDG-KKAFSDGDIT---- 262
Cdd:cd20003 159 VTTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTGKVAV-TGLSTPNVmRPYVKDGTVKsvvl 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046183786 263 --------LTVAQAPIQLAKETYKVGKKVLAG--------ESVAKEILVPT-FPITKEMID 306
Cdd:cd20003 238 wdvvdlgyLAVYVARALADGTLLKVGDFFVAGrlgtftvvPKGNGIILLGEpLIFTKENID 298
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
53-295 |
7.61e-14 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 70.58 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 53 SEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDlvVSTVA 132
Cdd:cd19993 22 KKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDRLIENPI--AFYIS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 133 SDNFLAGKINGEQMAKDYPNGAKIAVIDCPfnraSVLRADGFYAGLGE------NRSKFEVLSQQNGKCAL-EVTMPIAE 205
Cdd:cd19993 100 FDNVEVGRMQARGVLKAKPEGNYVFIKGSP----TDPNADFLRAGQMEvlqpaiDSGKIKIVGEQYTDGWKpANAQKNME 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 206 DIIQAHP-DLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVL 284
Cdd:cd19993 176 QILTANNnKVDAVVASNDGTAGGAVAALAAQGLAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELA 255
|
250
....*....|.
gi 1046183786 285 AGESVAKEILV 295
Cdd:cd19993 256 KGTKIEAIKGA 266
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
32-243 |
4.27e-13 |
|
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: 68.44 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDP-QYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQK 110
Cdd:cd20000 1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGPtTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 111 QIPVVVIDNPISDD--DLVVSTVASDnfLAGKINGEQMAKDYPNGAKIAVIDCPFNRA------SVLR---ADGFYAGL- 178
Cdd:cd20000 81 GIKVVTFDSDVAPEarDLFVNQADAD--GIGRAQVDMMAELIGGEGEFAILSATPTATnqnawiDAMKkelASPEYAGMk 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046183786 179 ------GENRSkfEVLSQQngkcalevtmpiAEDIIQAHPDLQAFFAvndPSALGVVVALKA---SNKLKNVKV 243
Cdd:cd20000 159 lvkvayGDDDA--QKSYQE------------AEALLQAYPDLKGIIA---PTTVGIAAAARAledSGLKGKVKV 215
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
50-249 |
5.11e-13 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380654 [Multi-domain] Cd Length: 313 Bit Score: 68.49 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 50 DTFSEIA---KQNG--DQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDD 124
Cdd:cd19999 19 ADFEEVAaeyKEEGviSDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPVSSP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 125 DLVvsTVASDNFLAGKINGEQMAKDYPNGAKIAVID-CPFNRASVLRADGFYAGLGENrSKFEVLSQQNGK----CALEV 199
Cdd:cd19999 99 DAI--NVVIDQYKWAAIQAQWLAEQLGGKGNIVAINgVAGNPANEARVKAADDVFAKY-PGIKVLASVPGGwdqaTAQQV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1046183786 200 TmpiaEDIIQAHPDLQAFFaVNDPSALGVVVALKASNKLknVKVYTVDGS 249
Cdd:cd19999 176 M----ATLLATYPDIDGVL-TQDGMAEGVLRAFQAAGKD--PPVMTGDYR 218
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
62-298 |
1.04e-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: 67.31 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 62 QYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDlVVSTVASDNFLAGKI 141
Cdd:cd19995 34 KVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGP-ADYYVSFDNVAVGEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 142 NGE----QMAKDYPNGAKIAVI--DCPFNRASVLR--ADGFYAGLGENrSKFEVLSQQNGKCALEVTMPIAED--IIQAH 211
Cdd:cd19995 113 QAQslvdHLKAIGKKGVNIVMIngSPTDNNAGLFKkgAHEVLDPLGDS-GELKLVCEYDTPDWDPANAQTAMEqaLTKLG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 212 PDLQAFFAVNDPSALGVVVALKAsNKLKNVKVYT-VDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVLAGESVA 290
Cdd:cd19995 192 NNIDGVLSANDGLAGGAIAALKA-QGLAGKVPVTgQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGETPP 270
|
....*...
gi 1046183786 291 KEILVPTF 298
Cdd:cd19995 271 SDLVTGTV 278
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
50-297 |
1.14e-12 |
|
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: 66.88 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 50 DTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDlVVS 129
Cdd:cd19991 19 DYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNAD-VDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 130 TVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPFNRASVLRADGFYAGLGE--NRSKFEVLSQQ-----NGKCALEvtmp 202
Cdd:cd19991 98 YVSFDNEKVGELQAEALVKAKPKGNYVLLGGSPTDNNAKLFREGQMKVLQPliDSGDIKVVGDQwvddwDPEEALK---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 203 IAEDIIQAH-PDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTV-----------AQAPI 270
Cdd:cd19991 174 IMENALTANnNKIDAVIASNDGTAGGAIQALAEQGLAGKVAVSGQDADLAACQRIVEGTQTMTIykpikelaekaAELAV 253
|
250 260
....*....|....*....|....*...
gi 1046183786 271 QLAKetykvGKKVLAGESVAK-EILVPT 297
Cdd:cd19991 254 ALAK-----GEKNEANRTINNgKKEVPS 276
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
34-234 |
1.86e-12 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 66.10 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAkqKQIP 113
Cdd:cd06285 3 GVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAA--RGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 114 VVVIDNPIsdDDLVVSTVASDNFLAGKINGEQMAKdypNG-AKIAVI-DCPFNRASVLRADGFYAGLgenrskfevlsqq 191
Cdd:cd06285 81 VVLVDRRI--GDTALPSVTVDNELGGRLATRHLLE---LGhRRIAVVaGPLNASTGRDRLRGYRRAL------------- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046183786 192 ngkcaLEVTMPI-AEDIIQAHPDLQ-----------------AFFAVNDPSALGVVVALKA 234
Cdd:cd06285 143 -----AEAGLPVpDERIVPGGFTIEagreaayrllsrperptAVFAANDLMAIGVLRAARD 198
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
49-287 |
8.78e-12 |
|
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: 64.37 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 49 SDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDlvV 128
Cdd:cd01538 18 RDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYDRLILNAD--V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 129 STVAS-DNFLAGKINGEQMAKDYPNGAKIAVIDCPFNRASVLRADG---FYAGLGENRsKFEVLSQQ-----NGKCALEv 199
Cdd:cd01538 96 DYYISfDNEKVGELQAQALLDAKPEGNYVLIGGSPTDNNAKLFRDGqmkVLQPAIDSG-KIKVVGDQwvddwLPANAQQ- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 200 tmpIAEDIIQAH-PDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYK 278
Cdd:cd01538 174 ---IMENALTANgNNVDAVVASNDGTAGGAIAALKAQGLSGGVPVSGQDADLAAIKRILAGTQTMTVYKDIRLLADAAAE 250
|
....*....
gi 1046183786 279 VGKKVLAGE 287
Cdd:cd01538 251 VAVALMRGE 259
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
50-307 |
1.38e-11 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 64.00 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 50 DTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPI--SDDDLV 127
Cdd:COG4213 22 DNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVIAYDRLIlnSDVDYY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 128 VSTvasDNFLAGKINGEQMAKDYPNGAK--IAVI-----DcpfNRASVLRaDGFYAGLGE--NRSKFEVLSQQ-----NG 193
Cdd:COG4213 102 VSF---DNVKVGELQGQYLVDGLPLKGKgnIELFggsptD---NNATLFF-EGAMSVLQPyiDSGKLVVVSGQwtlgwDP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 194 KCALEvtmpIAEDIIQAHP-DLQAFFAVNDPSALGVVVALKAsNKLKNVKVYT-VDGSPDGKKAFSDGDITLTVAQAPIQ 271
Cdd:COG4213 175 ETAQK----RMENLLTANGnKVDAVLAPNDGLAGGIIQALKA-QGLAGKVVVTgQDAELAAVQRILAGTQYMTVYKDTRE 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1046183786 272 LAKETYKVGKKVLAGESVA-------KEILVPTF-----PITKEMIDQ 307
Cdd:COG4213 250 LAEAAAELAVALAKGEKPEvngtydnGKKDVPSYllepvAVTKDNVKE 297
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
39-296 |
2.00e-11 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 63.07 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 39 TLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRqGLLAAKQKQIPVVVID 118
Cdd:cd06282 8 SLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSE-ALELLEEEGVPYVLLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 119 NPISDDDlvVSTVASDNFLAGKINGEQMAKdypNGAK-IAVIDCPFNRA--SVLRADGFYAGL---GENRSKF-EVLSQQ 191
Cdd:cd06282 87 NQTENSS--HPFVSVDNRLASYDVAEYLIA---LGHRrIAMVAGDFSASdrARLRYQGYRDALkeaGLKPIPIvEVDFPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 192 NGkCALEVTmpiaeDIIQAHPDLQAFFAVNDPSALGVVVALKASNKL--KNVKVYTVDGSPDGKKAfsdgDITL-TVAQA 268
Cdd:cd06282 162 NG-LEEALT-----SLLSGPNPPTALFCSNDLLALSVISALRRLGIRvpDDVSVIGFDGIAIGELL----TPTLaTVVQP 231
|
250 260
....*....|....*....|....*...
gi 1046183786 269 PIQLAKETYKVGKKVLAGESVAKEILVP 296
Cdd:cd06282 232 SRDMGRAAADLLLAEIEGESPPTSIRLP 259
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
71-296 |
3.74e-11 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380653 [Multi-domain] Cd Length: 302 Bit Score: 62.69 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 71 DQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDLVvsTVASDNFLAGKINGEQMAKDY 150
Cdd:cd19998 44 DVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVVDEPCAY--NVNTDQAKAGEQTAQWLVDKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 151 PNGAKIAVID-CPFNRASVLRADGFYAGLgENRSKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVnDPSAlGVV 229
Cdd:cd19998 122 GGKGNILMVRgVPGTSVDRDRYEGAKEVF-KKYPDIKVVAEYYGNWDDGTAQKAVADALAAHPDVDGVWTQ-GGET-GVI 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 230 VALKASNklKNVKVYTVDGSPDGKKAFSD---GDITLTVAQAPIQLAKETYKVGKKVLAGESVAKEILVP 296
Cdd:cd19998 199 KALQAAG--HPLVPVGGEAENGFRKAMLEplaNGLPGISAGSPPALSAVALKLAVAVLEGEKEPKTIELP 266
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
32-272 |
4.47e-11 |
|
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).
Pssm-ID: 395423 [Multi-domain] Cd Length: 281 Bit Score: 62.53 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNG-DQYILVDPQYDQAkQISMMEDVINQKVD--IIYLIAVDSEGIRqglLAAK 108
Cdd:pfam00532 3 KLGALVPQLDEPFFQDLVKGITKAAKDHGfDVFLLAVGDGEDT-LTNAIDLLLASGADgiIITTPAPSGDDIT---AKAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 109 QKQIPVVVIDNpISDDDLVVSTVASDNFLAGKINGEQMakdYPNGAK--IAVIDCPFNR-ASVLRADGFYAGL---GENR 182
Cdd:pfam00532 79 GYGIPVIAADD-AFDNPDGVPCVMPDDTQAGYESTQYL---IAEGHKrpIAVMAGPASAlTARERVQGFMAALaaaGREV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 183 SKFEVLSQQNgkcalevTMPIAEDIIQA----HPDLQAFFAVNDPSALGVVVALKASNKLK-----NVKVYTVDGSPDGK 253
Cdd:pfam00532 155 KIYHVATGDN-------DIPDAALAANAmlvsHPTIDAIVAMNDEAAMGAVRALLKQGRVKipdivGIGINSVVGFDGLS 227
|
250 260
....*....|....*....|.
gi 1046183786 254 KAFSDG--DITLTVAQAPIQL 272
Cdd:pfam00532 228 KAQDTGlyLSPLTVIQLPRQL 248
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
34-232 |
2.84e-10 |
|
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380489 [Multi-domain] Cd Length: 269 Bit Score: 59.82 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVD-SEGIRQGLLAAKqkqI 112
Cdd:cd01575 3 AVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEhTPATRKLLRAAG---I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 113 PVVVI----DNPIsddDLVVSTvasDNFLAGKINGEQM-AKDYpngAKIAVIDCPFN---RASvLRADGFYAGLGEN--- 181
Cdd:cd01575 80 PVVETwdlpDDPI---DMAVGF---SNFAAGRAMARHLiERGY---RRIAFVGARLDgdsRAR-QRLEGFRDALAEAglp 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1046183786 182 ----RSKFEVLSQQNGKCALEvtmpiaeDIIQAHPDLQAFFAVNDPSALGVVVAL 232
Cdd:cd01575 150 lplvLLVELPSSFALGREALA-------ELLARHPDLDAIFCSNDDLALGALFEC 197
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
37-296 |
5.53e-10 |
|
Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.
Pssm-ID: 380479 [Multi-domain] Cd Length: 265 Bit Score: 58.80 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 37 TSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVD--IIYLIAVDSEGIrqgLLAAKQKQIPV 114
Cdd:cd01537 6 IYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKglAINLVDPAAAGV---AEKARGQNVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 115 VVIDNPISDDDLVVStVASDNFLAGKINGEQMAKDYPNgaKIAVIDCPFNRASV-LRADGFYAGLGENRSKFEVLSQQNG 193
Cdd:cd01537 83 VFFDKEPSRYDKAYY-VITDSKEGGIIQGDLLAKHGHI--QIVLLKGPLGHPDAeARLAGVIKELNDKGIKTEQLQLDTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 194 KCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKL--KNVKVYTVDGSPDGKKAfsdGDITLTVAQAPIQ 271
Cdd:cd01537 160 DWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRvpSDISVFGYDALPEALKS---GPLLTTILQDANN 236
|
250 260
....*....|....*....|....*.
gi 1046183786 272 LAKETYKVGKKVL-AGESVAKEILVP 296
Cdd:cd01537 237 LGKTTFDLLLNLAdNWKIDNKVVRVP 262
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
45-287 |
1.03e-09 |
|
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: 58.48 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 45 FTAISDTFSEIAKQNG-DQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNP-IS 122
Cdd:cd20002 14 FNRMEQGVKKAGKEFGvNAYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVITHESPgQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 123 DDDLVVSTVASDNFlaGKINGEQMAKDYPNGAKIAVI----DCPfnrASVLRADGF-------YAGLGENRSKFEV--LS 189
Cdd:cd20002 94 GADWDVELIDNEKF--GEAQMELLAKEMGGKGEYAIFvgslTVP---LHNLWADAAveyqkekYPNMKQVTDRIPGgeDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 190 QQNGKCALEvtmpiaedIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAP 269
Cdd:cd20002 169 DVSRQTTLE--------LLKAYPDLKGIISFGSLGPIGAGQALREKGLKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDP 240
|
250
....*....|....*...
gi 1046183786 270 IQLAKETYKVGKKVLAGE 287
Cdd:cd20002 241 ADAGYAMVYIAKMLLDGK 258
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
36-232 |
1.10e-09 |
|
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380499 [Multi-domain] Cd Length: 269 Bit Score: 58.04 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 36 ITSTlNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAkQKQIPVV 115
Cdd:cd06275 6 VTSS-ENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAA-LRSIPVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 116 VIDNPISDDDlvVSTVASDNFLAGKINGEQMAKdypNG-AKIAVIDCPFNRA-SVLRADGFYAGLGEnrSKFEV------ 187
Cdd:cd06275 84 VLDREIAGDN--ADAVLDDSFQGGYLATRHLIE---LGhRRIGCITGPLEHSvSRERLAGFRRALAE--AGIEVppswiv 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1046183786 188 ---LSQQNGKCAlevtmpiAEDIIQAHPDLQAFFAVNDPSALGVVVAL 232
Cdd:cd06275 157 egdFEPEGGYEA-------MQRLLSQPPRPTAVFACNDMMALGALRAA 197
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
34-236 |
1.50e-09 |
|
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380506 [Multi-domain] Cd Length: 266 Bit Score: 57.56 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVD-IIyliaVDSEGI-RQGLLAAKQKQ 111
Cdd:cd06283 3 GVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDgLI----LQPTGNnNDAYLELAQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDNPIsdDDLVVSTVASDNFLAGKINGEQM-AKDYpngAKIAVIDCPFNRASV--LRADGFYAGLGENRSKFEVL 188
Cdd:cd06283 79 LPVVLVDRQI--EPLNWDTVVTDNYDATYEATEHLkEQGY---ERIVFVTEPIKGISTrrERLQGFLDALARYNIEGDVY 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1046183786 189 sQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASN 236
Cdd:cd06283 154 -VIEIEDTEDLQQALAAFLSQHDGGKTAIFAANGVVLLRVLRALKALG 200
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
32-233 |
3.13e-09 |
|
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380482 [Multi-domain] Cd Length: 294 Bit Score: 56.92 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVD---SEGIRQgllAAK 108
Cdd:cd01540 1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDqklGPAIAA---KAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 109 QKQIPVVVIDNPISDDDL--VVSTVASDNFLAGKINGEQMAK-----DYPNGAKIAVIDCPFNRASVL--RADGFYAGLG 179
Cdd:cd01540 78 AAGIPVIAVDDQLVDADPmkIVPFVGIDAYKIGEAVGEWLAKemkkrGWDDVKEVGVLAITMDTLSVCvdRTDGAKDALK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046183786 180 EN---RSK-FEV-LSQQNGKCALEVTMPiaedIIQAHPDLQAF--FAVNDPSALGVVVALK 233
Cdd:cd01540 158 AAgfpEDQiFQApYKGTDTEGAFNAANA----VITAHPEVKHWlvVGCNDEGVLGAVRALE 214
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
1-307 |
4.25e-09 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 56.88 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 1 MKKFIASFLTITFFLFTSCFQ------------------LVNAddKKPIKFAFITSTLNNSFFTAISDTFSEIAKQNGDQ 62
Cdd:PRK10936 1 MRKLLFLLLSLFLLSLTAFAAanlltwhlaqrtslqyspLLKA--KKAWKLCALYPHLKDSYWLSVNYGMVEEAKRLGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 63 YILVDP--QYDQAKQISMMEDVINQKVDIIYLIAVDSEGIrQGLLAAKQKQIPVVVIDNPISDDDlVVSTVASDNFLAGK 140
Cdd:PRK10936 79 LKVLEAggYYNLAKQQQQLEQCVAWGADAILLGAVTPDGL-NPDLELQAANIPVIALVNGIDSPQ-VTTRVGVSWYQMGY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 141 INGEQMAKDYPNG---AKIAVIDCPFNRASVLRAD-GFYAGLGenRSKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQA 216
Cdd:PRK10936 157 QAGRYLAQWHPKGskpLNVALLPGPEGAGGSKAVEqGFRAAIA--GSDVRIVDIAYGDNDKELQRNLLQELLERHPDIDY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 217 FF--AVNDPSALGVVVALKASNKLKNVKVYTvdgSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVLAGESVAKEIL 294
Cdd:PRK10936 235 IAgsAVAAEAAIGELRGRNLTDKIKLVSFYL---SHQVYRGLKRGKVLAAPSDQMVLQGRLAIDQAVRQLEGAPVPGDVG 311
|
330
....*....|...
gi 1046183786 295 VPTFPITKEMIDQ 307
Cdd:PRK10936 312 PKILVLTPKNLDS 324
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
36-297 |
5.90e-09 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380513 [Multi-domain] Cd Length: 267 Bit Score: 55.70 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 36 ITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAakqKQIPVV 115
Cdd:cd06290 5 LVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLA---EGIPVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 116 VIDNpiSDDDLVVSTVASDNFLAGKingeqMAKDY--PNGA-KIAVIDCP-FNRASVLRADGFY-----AGLGENrSKFE 186
Cdd:cd06290 82 LVDR--ELEGLNLPVVNVDNEQGGY-----NATNHliDLGHrRIVHISGPeDHPDAQERYAGYRraledAGLEVD-PRLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 187 V---LSQQNGKCALevtmpiaEDIIQAHPDLQAFFAVNDPSALGVVVALKASnKLK---NVKVYTVDGSPDGKkaFSDGD 260
Cdd:cd06290 154 VegdFTEESGYEAM-------KKLLKRGGPFTAIFAANDLMALGAMKALREA-GIRvpdDVSVIGFDDLPFSK--YTTPP 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 1046183786 261 ITlTVAQAPIQLAKETYKVGKKVLAGE-SVAKEILVPT 297
Cdd:cd06290 224 LT-TVRQPLYEMGKTAAEILLELIEGKgRPPRRIILPT 260
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
40-180 |
9.24e-09 |
|
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
Pssm-ID: 380498 [Multi-domain] Cd Length: 264 Bit Score: 55.29 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 40 LNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDiiYLIAVDSEGIRQGLLAAKQKQIPVVVIDN 119
Cdd:cd06274 9 LANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVD--GLIVAPSTPPDDIYYLCQAAGLPVVFLDR 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046183786 120 PISDDDLvvSTVASDNFLAGKINGEQMAKDypNGAKIAVIDC-PFNRASVLRADGFYAGLGE 180
Cdd:cd06274 87 PFSGSDA--PSVVSDNRAGARALTEKLLAA--GPGEIYFLGGrPELPSTAERIRGFRAALAE 144
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
42-296 |
1.65e-08 |
|
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380484 [Multi-domain] Cd Length: 259 Bit Score: 54.42 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 42 NSFFTAIS-DTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAvdSEGIRQGLLAAKQKQIPVVVIDNP 120
Cdd:cd01542 10 DSYSTSRVlEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFA--TEITDEHRKALKKLKIPVVVLGQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 121 ISDddlvVSTVASDNFLAGKINGEQMAKDypNGAKIAVIDCPFNRASV--LRADGFYAGLGENrsKFEVLSQQNGKCALE 198
Cdd:cd01542 88 HEG----FSCVYHDDYGAGKLLGEYLLKK--GHKNIAYIGVDEEDIAVgvARKQGYLDALKEH--GIDEVEIVETDFSME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 199 VTMPIAEDIIQAHPDlQAFFAVNDPSALGVVVALKASNKL--KNVKVYTVDGSPDGKkaFSDGDITlTVAQAPIQLAKET 276
Cdd:cd01542 160 SGYEAAKELLKENKP-DAIICATDNIALGAIKALRELGIKipEDISVAGFGGYDLSE--FVSPSLT-TVKFDYEEAGEKA 235
|
250 260
....*....|....*....|
gi 1046183786 277 YKVGKKVLAGESVAKEILVP 296
Cdd:cd01542 236 AELLLDMIEGEKVPKKQKLP 255
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
33-236 |
3.10e-08 |
|
ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380630 [Multi-domain] Cd Length: 269 Bit Score: 53.71 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 33 FAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQ---ISMMEDvinQKVD-IIYLIAVDSEGIRQGLlaaK 108
Cdd:cd19975 2 IGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREkkyLQLLKE---KRVDgIIFASGTLTEENKQLL---K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 109 QKQIPVVVIDNPISDDDLvvSTVASDNflagkingEQMAKD-----YPNGA-KIAVIDCPFNR--ASVLRADGFYAGLGE 180
Cdd:cd19975 76 NMNIPVVLVSTESEDPDI--PSVKIDD--------YQAAYDatnylIKKGHrKIAMISGPLDDpnAGYPRYEGYKKALKD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046183786 181 NRSKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASN 236
Cdd:cd19975 146 AGLPIKENLIVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHG 201
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
34-239 |
4.95e-08 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 52.92 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 34 AFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAkQISMMEDVINQKVD-IIYLIAVDSEGIRQgllAAKQKQI 112
Cdd:cd06278 3 GVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDD-VDDALRQLLQYRVDgVIVTSATLSSELAE---ECARRGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 113 PVVVIdNPiSDDDLVVSTVASDNFLAGKINGEQMAKdypNGAK-IAVIDCPFNRASVL-RADGFYAGLGE-NRSKFEVLS 189
Cdd:cd06278 79 PVVLF-NR-VVEDPGVDSVSCDNRAGGRLAADLLLA---AGHRrIAFLGGPEGTSTSReRERGFRAALAElGLPPPAVEA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1046183786 190 QQNGKcalEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLK 239
Cdd:cd06278 154 GDYSY---EGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGLV 200
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
35-236 |
8.32e-08 |
|
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380507 [Multi-domain] Cd Length: 267 Bit Score: 52.54 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 35 FITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVD-IIYLiavdSEGIRQGLLAAKQKQIP 113
Cdd:cd06284 4 VLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDgVILL----SGRLDAELLSELSKRYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 114 VVVIDNPIsdDDLVVSTVASDNFLAGKINGEQMAKdypNGAK-IAVIDCPF-NRASVLRADGFYAGLGENRSKFEVLSQQ 191
Cdd:cd06284 80 IVQCCEYI--PDSGVPSVSIDNEAAAYDATEYLIS---LGHRrIAHINGPLdNVYARERLEGYRRALAEAGLPVDEDLII 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1046183786 192 NGkcalEVTMPIAEDIIQA------HPDlqAFFAVNDPSALGVVVALKASN 236
Cdd:cd06284 155 EG----DFSFEAGYAAARAllalpeRPT--AIFCASDELAIGAIKALRRAG 199
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
36-232 |
1.47e-07 |
|
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380522 [Multi-domain] Cd Length: 268 Bit Score: 51.90 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 36 ITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIylIAVDSEGIRQGLLAAKQKQIPVV 115
Cdd:cd06299 5 LVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGI--IAVPTGENSEGLQALIAQGLPVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 116 VIDNPISDDDlVVSTVASDNFlagkiNGEQMAKDY---PNGAKIAVIDCPFNRASVL-RADGFYAGLGENRSKFEVLSQQ 191
Cdd:cd06299 83 FVDREVEGLG-GVPVVTSDNR-----PGAREAVEYlvsLGHRRIGYISGPLSTSTGReRLAAFRAALTAAGIPIDEELVA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1046183786 192 NGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVAL 232
Cdd:cd06299 157 FGDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQAL 197
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
42-232 |
1.59e-07 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 51.50 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 42 NSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQkqIPVVVIDNPI 121
Cdd:cd06293 11 NPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARG--TAVVLLDRPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 122 SDDDlvVSTVASDNFLAGkingeQMAKDYPNGA---KIAVIDCPFNRASVL-RADGFY-----AGLGENRSKFEVLSQQN 192
Cdd:cd06293 89 PGPA--GCSVSVDDVQGG-----ALAVDHLLELghrRIAFVSGPLRTRQVAeRLAGARaavaeAGLDPDEVVRELSAPDA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1046183786 193 GkcaLEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVAL 232
Cdd:cd06293 162 N---AELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGL 198
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
33-273 |
1.77e-07 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 51.50 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 33 FAFITSTLN---NSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKq 109
Cdd:cd01391 2 IGVVTSSLHqirEQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNLAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 110 KQIPVVVIDNPISDDDL------VVSTVASDNflAGKINGEQMAKDYpNGAKIAVIDCPFNRASVLRADGFYAGLGENRS 183
Cdd:cd01391 81 FDIPQLALDATSQDLSDktlykyFLSVVFSDT--LGARLGLDIVKRK-NWTYVAAIHGEGLNSGELRMAGFKELAKQEGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 184 KfEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAF--SDGDI 261
Cdd:cd01391 158 C-IVASDKADWNAGEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLVGDVSVIGSDGWADRDEVGyeVEANG 236
|
250
....*....|..
gi 1046183786 262 TLTVAQAPIQLA 273
Cdd:cd01391 237 LTTIKQQKMGFG 248
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
36-293 |
2.11e-07 |
|
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380632 [Multi-domain] Cd Length: 264 Bit Score: 51.38 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 36 ITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIylIAVDSEGIRQGLLAAKQKQIPVV 115
Cdd:cd19977 5 IVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGI--IIAPTGGNEDLIEKLVKSGIPVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 116 VIDNPISDDDlvVSTVASDNFLAGKINGEQMAKdypNGAK-IAVIDCPFNRASVL-RADGFYAGLGENRSKFEVLsqqng 193
Cdd:cd19977 83 FVDRYIPGLD--VDTVVVDNFKGAYQATEHLIE---LGHKrIAFITYPLELSTRQeRLEGYKAALADHGLPVDEE----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 194 kcaLEVTMPIAEDIIQA-------HPDLQAFFAVNDPSALGVVVALKaSNKLK---NVKVYTVDGSPdgkkAFSDGDITL 263
Cdd:cd19977 153 ---LIKHVDRQDDVRKAisellklEKPPDAIFAANNLITLEVLKAIK-ELGLRipdDIALIGFDDIP----WADLFNPPL 224
|
250 260 270
....*....|....*....|....*....|
gi 1046183786 264 TVAQAPIqlaketYKVGKKvlAGESVAKEI 293
Cdd:cd19977 225 TVIAQPT------YEIGRK--AAELLLDRI 246
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
66-289 |
5.25e-07 |
|
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: 50.32 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 66 VDPQY---DQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDLVVSTVASDNFLAGKIN 142
Cdd:cd19994 32 VDLQYaddDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYDRLIMNTDAVDYYVTFDNEKVGELQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 143 GEQMAKdypnGAKIAVIDCPFN------RASVLRADGFYAGL----------GENRSKFEVLSQQngKCAL-----EVTM 201
Cdd:cd19994 112 GQYLVD----KLGLKDGKGPFNielfagSPDDNNAQLFFKGAmevlqpyiddGTLVVRSGQTTFE--QVATpdwdtETAQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 202 PIAEDIIQAHP----DLQAFFAVNDPSALGVVVALKASNKLKNVKVYTV--DGSPDGKKAFSDGDITLTVAQAPIQLAKE 275
Cdd:cd19994 186 ARMETLLSAYYtggkKLDAVLSPNDGIARGVIEALKAAGYDTGPWPVVTgqDAEDASVKSILDGEQSMTVFKDTRLLAKA 265
|
250
....*....|....
gi 1046183786 276 TYKVGKKVLAGESV 289
Cdd:cd19994 266 TVELVDALLEGEEV 279
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
15-265 |
6.24e-07 |
|
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior.
Pssm-ID: 380526 [Multi-domain] Cd Length: 320 Bit Score: 50.06 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 15 LFTSCFQLVNAD-------DKKPIKFAFITSTLNNS-FFTAISDTFSEIAKQNGDQYIL----VDPQYDQAKQISMMEDV 82
Cdd:cd06303 5 LTEDFSERVRAPpvpaevtQKRPVKIAVVYPGLQVSdYWRRSIVSFRKRLDELGIKYQLdeffTRPGAEIRLQALQIREM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 83 INQKVDiiYLI-AVDSEGIRQGLLAAKQKQIPVVVIDN---PISD--DDLVVSTVASDNFLAGKINGEQMAKDYPNGAKI 156
Cdd:cd06303 85 LKSDPD--YLIfTLDALRHRRFVEILLDSGKPKLILQNittPLRDwdNHQPLLYVGFDHAEGSRMLAKHFIKIFPEEGKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 157 AVIDCPFNRASVLRADGFYAGLGENrSKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKASN 236
Cdd:cd06303 163 AILYLTEGYVSDQRGDTFIDEVARH-SNLELVSAYYTDFDRESAREAARALLARHPDLDFIYACSTDIALGAIDALQELG 241
|
250 260
....*....|....*....|....*....
gi 1046183786 237 KLKNVKVYTVDGSPDGKKAFSDGDITLTV 265
Cdd:cd06303 242 RETDIMINGWGGGSAELDALQKGGLDVTV 270
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
40-234 |
9.87e-07 |
|
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380512 [Multi-domain] Cd Length: 268 Bit Score: 49.10 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 40 LNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGiRQGLLAAKQKQIPVVVIDN 119
Cdd:cd06289 9 LSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTT-AELLRRLKAWGIPVVLALR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 120 PISDDDlvVSTVASDNFLAGKINGEQMAKdypNGAK-IAVI----DCPFNRAsvlRADGFYAGLGENRSKFE----VLSQ 190
Cdd:cd06289 88 DVPGSD--LDYVGIDNRLGAQLATEHLIA---LGHRrIAFLgglsDSSTRRE---RLAGFRAALAEAGLPLDesliVPGP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1046183786 191 QNGKCALEVtmpiAEDIIQAHPDLQAFFAVNDPSALGVVVALKA 234
Cdd:cd06289 160 ATREAGAEA----ARELLDAAPPPTAVVCFNDLVALGAMLALRR 199
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
42-237 |
1.54e-06 |
|
ligand-binding domain of putative DNA transcription regulators highly similar to that of the transcription regulator DegA; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the transcription regulator DegA, which is involved in the control of degradation of Bacillus subtilis amidophosphoribosyltransferase (purF). This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380631 [Multi-domain] Cd Length: 268 Bit Score: 48.78 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 42 NSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVD--IIYLIAVDSEGIRQGLlaaKQKQIPVVVIDN 119
Cdd:cd19976 11 NPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDgiIIASSNISDEAIIKLL---KEEKIPVVVLDR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 120 PISDDDlvVSTVASDNFlagkiNGEQMAKDY--PNG-AKIAVIDCPFNRASVL-RADGFYAGLGENrsKFEVLSQQNGKC 195
Cdd:cd19976 88 YIEDND--SDSVGVDDY-----RGGYEATKYliELGhTRIGCIVGPPSTYNEHeRIEGYKNALQDH--NLPIDESWIYSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1046183786 196 ALEVTM--PIAEDIIQAHPdLQAFFAVNDPSALGVVVALKASNK 237
Cdd:cd19976 159 ESSLEGgyKAAEELLKSKN-PTAIFAGNDLIAMGVYRAALELGL 201
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
44-269 |
2.67e-06 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380621 [Multi-domain] Cd Length: 278 Bit Score: 48.09 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 44 FFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQ-IPVVVIDNPIS 122
Cdd:cd19966 14 FWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTPLIEAAKKAgIIVTSFNTDLP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 123 DDDLVVST---VASDNFLAGKINGEQMAKDYP--NGAKIAVIDCPFNR-ASVLRADGFYAGLGENRSKFEVL---SQQNG 193
Cdd:cd19966 94 KLEYGDCGlgyVGADLYAAGYTLAKELVKRGGlkTGDRVFVPGLLPGQpYRVLRTKGVIDALKEAGIKVDYLeisLEPNK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046183786 194 KCALEVTMpiaEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKlKNVKVYTV--DGSPDGKKAFSDGDITLTVAQAP 269
Cdd:cd19966 174 PAEGIPVM---TGYLAANPDVKAIVGDGGGLTANVAKYLKAAGK-KPGEIPVAgfDLSPATVQAIKSGYVNATIDQQP 247
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
41-234 |
9.46e-06 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 46.46 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 41 NNSFFTAISDTFSEIAKQNGDQYIL--VDPQYDQAKQISMmedVINQKVDIIYLIAVDsegirqglLAAKQ------KQI 112
Cdd:cd06277 17 ETPFFSELIDGIEREARKYGYNLLIssVDIGDDFDEILKE---LTDDQSSGIILLGTE--------LEEKQiklfqdVSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 113 PVVVIDNpiSDDDLVVSTVASDNFlagkiNGEQMAKDYPNG---AKIAVIDCPFN-RASVLRADGFYAGLGENRskfevL 188
Cdd:cd06277 86 PVVVVDN--YFEDLNFDCVVIDNE-----DGAYEAVKYLVElghTRIGYLASSYRiKNFEERRRGFRKAMRELG-----L 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1046183786 189 SQQNGKC-ALEVTMPIAEDIIQAHPD-----LQAFFAVNDPSALGVVVALKA 234
Cdd:cd06277 154 SEDPEPEfVVSVGPEGAYKDMKALLDtgpklPTAFFAENDIIALGCIKALQE 205
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
33-234 |
1.70e-05 |
|
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380511 [Multi-domain] Cd Length: 268 Bit Score: 45.62 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 33 FAFITSTLNNSFFTA-ISDTFSEIAKQNGDQYILVDPQYDQ---AKQISMMEDvinQKVD-IIYLiavdSEGIRQGLLAA 107
Cdd:cd06288 2 IGLITDDIATTPFAGdIIRGAQDAAEEHGYLLLLANTGGDPeleAEAIRELLS---RRVDgIIYA----SMHHREVTLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 108 KQKQIPVVVIdNPISDDDLVVSTVAsDNFLAGKINGEQMAKdypNGA-KIAVIDCP-FNRASVLRADGFYAGLGENRSKF 185
Cdd:cd06288 75 ELTDIPLVLL-NCFDDDPSLPSVVP-DDEQGGYLATRHLIE---AGHrRIAFIGGPeDSLATRLRLAGYRAALAEAGIPY 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1046183786 186 EVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDPSALGVVVALKA 234
Cdd:cd06288 150 DPSLVVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAE 198
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
32-289 |
2.38e-05 |
|
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: 45.35 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNG-DQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQK 110
Cdd:cd20001 1 TIAVVVKVTGIAWFDRMETGVEQFAKDTGvNVYQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 111 QIpvVVIDNPISDDDLVVSTV-ASDNFLAGKINGEQMAKDYPN-GAKIAVIDCPFNRASVLRADGFYAGLGENRSKFEVL 188
Cdd:cd20001 81 GI--VVITHEASNLKNVDYDVeAFDNAAYGAFIMDKLAEAMGGkGKYVTFVGSLTSTSHMEWANAAVAYQKANYPDMLLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 189 -----SQQNGKCALEVtmpiAEDIIQAHPDLQAFFAVNDPSALGVVVALKASNKLKNVKVYTVdGSP-DGKKAFSDGDIT 262
Cdd:cd20001 159 tdrveTNDDSETAYEK----AKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGKIAVVGT-GLPsVAGEYLEDGTID 233
|
250 260
....*....|....*....|....*..
gi 1046183786 263 LTVAQAPIQLAKETYKVGKKVLAGESV 289
Cdd:cd20001 234 YIQFWDPADAGYAMNALAVMVLEGEKI 260
|
|
| PRK15408 |
PRK15408 |
autoinducer 2 ABC transporter substrate-binding protein LsrB; |
1-246 |
2.43e-05 |
|
autoinducer 2 ABC transporter substrate-binding protein LsrB;
Pssm-ID: 237961 Cd Length: 336 Bit Score: 45.17 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 1 MKKFIASFLTITFFLFTSCFQlvnADDKkpikFAFITSTLNNSFFTAISDTFSEIAKQNGdqyilVDPQYDQ------AK 74
Cdd:PRK15408 1 RKKKIALVSALGIALISMTVQ---AAER----IAFIPKLVGVGFFTSGGNGAKEAGKELG-----VDVTYDGptepsvSG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 75 QISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDLVV----STVASDNFLAGKINGEQMAKDy 150
Cdd:PRK15408 69 QVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYyinqGTPEQLGSMLVEMAAKQVGKD- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 151 pnGAKIA-------VIDcpfNRASVLRADgfyAGLGENRSKFEVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAvndP 223
Cdd:PRK15408 148 --KAKVAffyssptVTD---QNQWVKEAK---AKIAKEHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIA---P 216
|
250 260
....*....|....*....|...
gi 1046183786 224 SALGVVVALKASNKLKNVKVYTV 246
Cdd:PRK15408 217 DANALPAAAQAAENLKRDKVAIV 239
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
39-235 |
2.96e-05 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 44.81 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 39 TLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVD-SEGIRQgLLAakQKQIPVVVI 117
Cdd:cd06273 8 TLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDhDPELFE-LLE--QRQVPYVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 118 DnpISDDDLVVSTVASDNFLAGkingeQMAKDY--PNG-AKIAVI--DCPFNRASVLRADGFYAGLGENRSKFEVlsqqn 192
Cdd:cd06273 85 W--SYDEDSPHPSIGFDNRAAA-----ARAAQHllDLGhRRIAVIsgPTAGNDRARARLAGIRDALAERGLELPE----- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1046183786 193 gkcALEVTMP--------IAEDIIQAHPDLQAFFAVNDPSALGVVVALKAS 235
Cdd:cd06273 153 ---ERVVEAPysieegreALRRLLARPPRPTAIICGNDVLALGALAECRRL 200
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
50-311 |
2.61e-04 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 42.04 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 50 DTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDLVVs 129
Cdd:PRK10355 45 DIFVKKAESLGAKVFVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDF- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 130 TVASDNFLAGKINGEQMAKDYPNGAKIAVIDCPFNRASVLRADGFYAGLGE--NRSKFEVLSQQNGKCAL-EVTMPIAED 206
Cdd:PRK10355 124 YISFDNEKVGELQAKALVDKVPQGNYFLMGGSPVDNNAKLFRAGQMKVLKPyiDSGKIKVVGDQWVDGWLpENALKIMEN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 207 IIQAHPD-LQAFFAVNDPSALGVVVALKASNKLKNVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVLA 285
Cdd:PRK10355 204 ALTANNNkIDAVVASNDATAGGAIQALSAQGLSGKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGN 283
|
250 260 270
....*....|....*....|....*....|....*...
gi 1046183786 286 GESVA---------KEI---LVPTFPITKEMIDQYGVK 311
Cdd:PRK10355 284 GEEPKanttlnnglKDVpsrLLTPIDVNKNNIDSTVIK 321
|
|
| ChvE |
NF040907 |
sugar ABC transporter substrate-binding protein; |
66-144 |
4.89e-04 |
|
sugar ABC transporter substrate-binding protein;
Pssm-ID: 468842 Cd Length: 319 Bit Score: 41.38 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 66 VDPQY---DQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLAAKQKQIPVVVIDNPISDDDLVVSTVASDNFLAGKIN 142
Cdd:NF040907 31 TDLQYaedDVPTQVSQIENMITKGAKVLVIAAIDGTALTDVLQQAADAGIPVIAYDRLIRGSENVDYYATFDNFKVGVLQ 110
|
..
gi 1046183786 143 GE 144
Cdd:NF040907 111 GT 112
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
35-243 |
5.04e-04 |
|
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380494 [Multi-domain] Cd Length: 266 Bit Score: 40.97 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 35 FITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVD--IIYLIAVDSEGirqgLLAAKQKQI 112
Cdd:cd06270 4 LVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDaiILHSRALSDEE----LILIAEKIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 113 PVVVID---NPISDddlvvSTVASDNFLAGkingeQMAKDY--PNG-AKIAVIDCPF-NRASVLRADGFYAGLGENRSKF 185
Cdd:cd06270 80 PLVVINryiPGLAD-----RCVWLDNEQGG-----RLAAEHllDLGhRRIACITGPLdIPDARERLAGYRDALAEAGIPL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046183786 186 -EVL------SQQNGKCAlevtmpiAEDIIQAHPDLQAFFAVNDPSALGVVVALKAsnklKNVKV 243
Cdd:cd06270 150 dPSLiiegdfTIEGGYAA-------AKQLLARGLPFTALFAYNDDMAIGALAALHE----AGIKV 203
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
32-308 |
5.23e-04 |
|
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: 41.12 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 32 KFAFITSTLNNSFFTAISDTFSEIAKQNGDQYILVDPQY-----DQAKQISMMEDVINQKVDIIYLIAVDSEGIRQGLLA 106
Cdd:cd19997 1 VIALSNSYAGNTWRQQMVDAFEEAAKKAKADGLIADYIVvnadgSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 107 AKQKQIPVVVIDNPISDDDLVVSTVASDNFlaGKINGEQMAKDYPNGAKIAVIdcpfnR--ASVLRADGFYAGLGENRSK 184
Cdd:cd19997 81 ACDAGIKVVVFDSGVTEPCAYILNNDFEDY--GAASVEYVADRLGGKGNVLEV-----RgvAGTSPDEEIYAGQVEALKK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 185 F---EVLSQQNGKCALEVTMPIAEDIIQAHPDLQAFFAVNDpSALGVVVALKASNklKNVKVYTVDGSPDGKKAFSD--- 258
Cdd:cd19997 154 YpdlKVVAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGG-DGYGAAQAFEAAG--RPLPIIIGGNRGEFLKWWQEeya 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1046183786 259 --GDITLTVAQAPIQLAKETYkVGKKVLAGESVAKEILVPTFPITKEMIDQY 308
Cdd:cd19997 231 knGYETVSVSTDPGQGSAAFW-VALDILNGKDVPKEMILPVVTITEDDLDAW 281
|
|
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
213-308 |
1.44e-03 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 39.71 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 213 DLQAFFAVNDPSALGVVVALKASNKLKnVKVYTVDGSPDGKKAFSDGDITLTVAQAPIQLAKETYKVGKKVLAGESVA-- 290
Cdd:PRK15395 225 KIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAeg 303
|
90 100
....*....|....*....|....*
gi 1046183786 291 -------KEILVPTFPITKEMIDQY 308
Cdd:PRK15395 304 tnwkienKVVRVPYVGVDKDNLAEF 328
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
44-250 |
2.07e-03 |
|
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380520 [Multi-domain] Cd Length: 268 Bit Score: 38.99 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 44 FFTAISDTFSEIAKQNGDQYILVdPQYDQAKQISMMEDVINQK-VDIIYLIAVDSEGIRQGLLAAKQKqiPVVVIDNPIS 122
Cdd:cd06297 13 FYMRLLTGVERALDENRYDLAIF-PLLSEYRLEKYLRNSTLAYqCDGLVMASLDLTELFEEVIVPTEK--PVVLIDANSM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 123 DDDlvvsTVASDNFLAGKINGEQMAKDYPNGAKIAVIDC-PFNRASVLRA--DGFYAGLGENRSKFE----VLSQQNGKC 195
Cdd:cd06297 90 GYD----CVYVDNVKGGFMATEYLAGLGEREYVFFGIEEdTVFTETVFREreQGFLEALNKAGRPISssrmFRIDNSSKK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046183786 196 ALEVTMPIAEdiiQAHPDLqAFFAVNDPSALGVVVALKASNKL--KNVKVYTVDGSP 250
Cdd:cd06297 166 AECLARELLK---KADNPA-AFFAAADLVALGLIRAAQSLGLRvgEDVAVIGFDGQP 218
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
112-234 |
6.64e-03 |
|
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation; This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380519 [Multi-domain] Cd Length: 270 Bit Score: 37.64 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 112 IPVVVIDnPISDDDLVVSTVASDNFLAGKINGEQMAKdypNGAK-IAVIDCPFN-RASVLRADGFYAGLGENR---SKFE 186
Cdd:cd06296 79 IPFVLID-PVGEPDPDLPSVGATNWAGGRLATEHLLD---LGHRrIAVITGPPRsVSGRARLAGYRAALAEAGiavDPDL 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1046183786 187 VL-SQQNGKCALEVTMPIAEdiiqaHPDL-QAFFAVNDPSALGVVVALKA 234
Cdd:cd06296 155 VReGDFTYEAGYRAARELLE-----LPDPpTAVFAGNDEQALGVYRAARA 199
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
42-290 |
6.64e-03 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 37.58 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 42 NSFFTAISDTFSEIAKQNGDQYILVDPQYDQAKQISMMEDVINQKVDIIYLIAVDSegirQGLLAAKQKQIPVVV--IDN 119
Cdd:COG2984 17 DAAREGFKDGLAEAGYGKNLKLDYQNAQGDQATAAQIAAKLVADKPDLIVAIGTPA----AQAAANATKDIPVVFtaVTD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 120 PISDDDlvvstVASDNFLAGKING-----------EQMAKDYPNGAKIAVIDCPFNRASVLRADGFYAGLGENRSKFEVL 188
Cdd:COG2984 93 PVGAGL-----VKSLEKPGGNVTGvsdllpiekqlELIKKLLPDAKRIGVLYNPSEANSVAQVEELKKAAKKLGLELVEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046183786 189 SQQNgkcalevtmpiAEDIIQA----HPDLQAFFAVNDP---SALGVVVALKASNKlknVKVYTVDGSpdgkkAFSDGdI 261
Cdd:COG2984 168 TVTS-----------SNEIQQAlqslAGKVDAIYVPTDNtvvSALEAIAKVAARAK---IPVFGGDDS-----SVKAG-A 227
|
250 260
....*....|....*....|....*....
gi 1046183786 262 TLTVAQAPIQLAKETYKVGKKVLAGESVA 290
Cdd:COG2984 228 LAGYGIDYYELGRQAAEMALRILKGEKPA 256
|
|
| |
