|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
40-305 |
1.23e-131 |
|
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: 374.71 E-value: 1.23e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADK--SLKVVAKQA 197
Cdd:cd06323 81 IPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAKypKINVVASQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTDVVVVGFDATDDAVKAVNDGRMAATVAQKPELIG 277
Cdd:cd06323 161 ADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQPEEMG 240
|
250 260
....*....|....*....|....*...
gi 446681634 278 EKAMQTAKEITQGKKVDKSIPIELELIK 305
Cdd:cd06323 241 AKAVETADKYLKGEKVPKKIPVPLKLVT 268
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-306 |
5.98e-119 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 343.61 E-value: 5.98e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 1 MKKWLLILVACIMVITAGCSMEppewAKDSsdkgrnktikVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDA 80
Cdd:PRK10653 3 MKKLATLVSAVALSATVSANAM----AKDT----------IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 81 AKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEG 160
Cdd:PRK10653 69 AKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIAKKLGEG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 161 ANVAELEGIPGSSAARERGKGFHNVADKS-LKVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKS 239
Cdd:PRK10653 149 AKVIQLEGIAGTSAARERGEGFKQAVAAHkFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQT 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446681634 240 AGKTDVVVVGFDATDDAVKAVNDGRMAATVAQKPELIGEKAMQTAKEITQGKKVDKSIPIELELIKK 306
Cdd:PRK10653 229 AGKSDVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGVETADKVLKGEKVEAKIPVDLKLVTK 295
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
2-306 |
8.97e-92 |
|
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: 274.88 E-value: 8.97e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 2 KKWLLILVACIMVITAGCSMEPPEWAKDSSDKgrnktIKVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAA 81
Cdd:COG1879 2 RLALLAAVLALALALAACGSAAAEAAAAAAKG-----KTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 82 KQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGA 161
Cdd:COG1879 77 KQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 162 NVAELEGIPGSSAARERGKGFHNVADKS--LKVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKS 239
Cdd:COG1879 157 KVAILTGSPGAPAANERTDGFKEALKEYpgIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446681634 240 AGKT-DVVVVGFDATDDAVKAVNDGRMAATVAQKPELIGEKAMQTAKEITQGKKVDKSIPIELELIKK 306
Cdd:COG1879 237 AGRKgDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTK 304
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
40-303 |
1.39e-90 |
|
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: 270.59 E-value: 1.39e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDR-VANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKVVAKQ 196
Cdd:cd01536 81 IPVVAVDTdIDGGGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYpdIEIVAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 197 AADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAATVAQKPEL 275
Cdd:cd01536 161 PANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTgDIKIVGVDGTPEALKAIKDGELDATVAQDPYL 240
|
250 260
....*....|....*....|....*...
gi 446681634 276 IGEKAMQTAKEITQGKKVDKSIPIELEL 303
Cdd:cd01536 241 QGYLAVEAAVKLLNGEKVPKEILTPVTL 268
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
40-304 |
6.78e-81 |
|
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: 245.92 E-value: 6.78e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKA-KDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAA 118
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAaKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 119 NVPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKVVAKQ 196
Cdd:cd06308 81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYpgIKIVASQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 197 AADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGK-TDVVVVGFDATDDA-VKAVNDGRMAATVaqKPE 274
Cdd:cd06308 161 DGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGLPEAgEKAVKDGILAATF--LYP 238
|
250 260 270
....*....|....*....|....*....|
gi 446681634 275 LIGEKAMQTAKEITQGKKVDKSIPIELELI 304
Cdd:cd06308 239 TGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
40-304 |
8.72e-78 |
|
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: 238.66 E-value: 8.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDR---VANSGKVVSHIASNNIEGGQMASDYI-RELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKVV 193
Cdd:cd06309 81 IPVILVDRtidGEDGSLYVTFIGSDFVEEGRRAAEWLvKNYKGGKGNVVELQGTAGSSVAIDRSKGFREVIKKHpnIKIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 194 AKQAADFDRAKGLSVMENILQAN-SNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDDAVKAVNDGRMAATV 269
Cdd:cd06309 161 ASQSGNFTREKGQKVMENLLQAGpGDIDVIYAHNDDMALGAIQALKEAGLKpgkDVLVVGIDGQKDALEAIKAGELNATV 240
|
250 260 270
....*....|....*....|....*....|....*
gi 446681634 270 AQKPeLIGEKAMQTAKEITQGKKVDKSIPIELELI 304
Cdd:cd06309 241 ECNP-LFGPTAFDTIAKLLAGEKVPKLIIVEERLF 274
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
40-295 |
2.60e-77 |
|
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: 236.90 E-value: 2.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKVVAKQA 197
Cdd:cd19968 81 IPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAAGpkIKVVFEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDRAKGLSVMENILQANSN-IKAVFAHNDEMALGALEALKSAG--KTDVVVVGFDATDDAVKAVNDGRMAATVAQKPE 274
Cdd:cd19968 161 GNFERDEGLTVMENILTSLPGpPDAIICANDDMALGAIEAMRAAGldLKKVKVIGFDAVPDALQAIKDGELYATVEQPPG 240
|
250 260
....*....|....*....|..
gi 446681634 275 L-IGEKAMQTAKEITQGKKVDK 295
Cdd:cd19968 241 GqARTALRILVDYLKDKKAPKK 262
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
41-304 |
8.47e-71 |
|
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: 220.23 E-value: 8.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANV 120
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGKVVSHIASNNIEGGQMASDYIRE-LVGEGANVAELeGIPGSSAARERGKGFHNVADKS--LKVVAKQA 197
Cdd:cd06322 82 PVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKaLLGGGGKIAII-DYPEVESVVLRVNGFKEAIKKYpnIEIVAEQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTD-VVVVGFDATDDAVKAVN-DGRMAATVAQKPEL 275
Cdd:cd06322 161 GDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDkIKVIGFDGNPEAIKAIAkGGKIKADIAQQPDK 240
|
250 260
....*....|....*....|....*....
gi 446681634 276 IGEKAMQTAKEITQGKKVDKSIPIELELI 304
Cdd:cd06322 241 IGQETVEAIVKYLAGETVEKEILIPPKLY 269
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
40-307 |
9.77e-70 |
|
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: 217.90 E-value: 9.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSG--IELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANA 117
Cdd:cd06320 1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGvkVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 118 ANVPVITVDRVANS-------GKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNV--ADK 188
Cdd:cd06320 81 KGIPVINLDDAVDAdalkkagGKVTSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETfkKAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 189 SLKVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAA 267
Cdd:cd06320 161 GLKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTgKVLVVGTDGIPEAKKSIKAGELTA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446681634 268 TVAQKPELIGEKAMQTAKEITQGKKVDKSIPIELELIKKN 307
Cdd:cd06320 241 TVAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKD 280
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
39-304 |
4.30e-69 |
|
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: 215.94 E-value: 4.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 39 IKVGFSVSTLNNPFFVTLKKGAEKKAKD-SGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANA 117
Cdd:cd06301 1 IKIGVSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 118 ANVPVITVDR-VANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKVVA 194
Cdd:cd06301 81 AGIPLVYVNRePDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYpgMKIVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTD-VVVVGFDATDDAVKAVNDGRMAATVAQKP 273
Cdd:cd06301 161 EQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDdILVAGIDATPDALKAMKAGRLDATVFQDA 240
|
250 260 270
....*....|....*....|....*....|.
gi 446681634 274 ELIGEKAMQTAKEITQGKKVDKSIPIELELI 304
Cdd:cd06301 241 AGQGETAVDVAVKAAKGEEVESDIWIPFELV 271
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
40-306 |
1.12e-68 |
|
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: 214.83 E-value: 1.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADK--SLKVVAKQA 197
Cdd:cd06313 81 IPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIENVLKKypDIKVLAEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDRAKGLSVMENILQA-NSNIKAVFAHNDEMALGALEALKSAGKTDVVVVGFDATDDAVKAVNDGRMAATVAQKPELI 276
Cdd:cd06313 161 ANWSRDEAMSLMENWLQAyGDEIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDALQAVKSGELIATVLQDAEAQ 240
|
250 260 270
....*....|....*....|....*....|
gi 446681634 277 GEKAMQTAKEITQGKKVDKSIPIELELIKK 306
Cdd:cd06313 241 GKGAVEVAVDAVKGEGVEKKYYIPFVLVTK 270
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
40-303 |
5.02e-68 |
|
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: 212.83 E-value: 5.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVD-RVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEgIPGSSAARERGKGFHNV--ADKSLKVVAKQ 196
Cdd:cd19971 81 IPVINVDtPVKDTDLVDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLD-HPTAESCVDRIDGFLDAikKNPKFEVVAQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 197 AADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAATVAQKPEL 275
Cdd:cd19971 160 DGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKLgDILVYGVDGSPDAKAAIKDGKMTATAAQSPIE 239
|
250 260
....*....|....*....|....*...
gi 446681634 276 IGEKAMQTAKEITQGKKVDKSIPIELEL 303
Cdd:cd19971 240 IGKKAVETAYKILNGEKVEKEIVVPTFL 267
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
45-304 |
3.36e-66 |
|
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: 208.33 E-value: 3.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 45 VSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVIT 124
Cdd:cd19967 6 VSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 125 VDRVANS-GKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADK--SLKVVAKQAADFD 201
Cdd:cd19967 86 IDREINAeGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQypELKMVAQQSADWD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 202 RAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGK-TDVVVVGFDATDDAVKAVNDGRMAATVAQKPELIGEKA 280
Cdd:cd19967 166 RTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRaGDVIIVGFDGSNDVRDAIKEGKISATVLQPAKLIARLA 245
|
250 260
....*....|....*....|....*.
gi 446681634 281 MQTAKEITQGKKVDKS--IPIELELI 304
Cdd:cd19967 246 VEQADQYLKGGSTGKEekQLFDCVLI 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
40-306 |
1.49e-61 |
|
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: 196.81 E-value: 1.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGE----GANVAELEGIPGSSAARERGKGFHNVADK-SLKVVA 194
Cdd:cd06319 81 IPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKEngwgGGSVGIIAIPQSRVNGQARTAGFEDALEEaGVEEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 K-QAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAATVAQK 272
Cdd:cd06319 161 LrQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTgDILVVGFDGDPEALDLIKDGKLDGTVAQQ 240
|
250 260 270
....*....|....*....|....*....|....*
gi 446681634 273 PELIGEKAMQTAKEITQGKK-VDKSIPIELELIKK 306
Cdd:cd06319 241 PFGMGARAVELAIQALNGDNtVEKEIYLPVLLVTS 275
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
40-293 |
1.50e-61 |
|
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: 196.86 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVAN-SGKVVSHIASNNIEGGQMASDYIRELVG-EGANVAELEGIPGSSAARERGKGFH---------NVADK 188
Cdd:cd06318 81 IPVITVDSALDpSANVATQVGRDNKQNGVLVGKEAAKALGgDPGKIIELSGDKGNEVSRDRRDGFLagvneyqlrKYGKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 189 SLKVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTDVV-VVGFDATDDAVKAVNDGRMAA 267
Cdd:cd06318 161 NIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVkVAGADGQKEALKLIKDGKYVA 240
|
250 260
....*....|....*....|....*.
gi 446681634 268 TVAQKPELIGEKAMQTAKEITQGKKV 293
Cdd:cd06318 241 TGLNDPDLLGKTAVDTAAKVVKGEES 266
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
40-304 |
1.11e-60 |
|
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: 194.43 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGI--ELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANA 117
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPgaKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 118 ANVPVITVDRVANSgkVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPgSSAARERGKGFHNVADKS--LKVVAK 195
Cdd:cd06321 81 AGIIVVAVDVAAEG--ADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPP-VSAVIDRVNGCKEALAEYpgIKLVDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 196 QAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTDVVVVGFDATDDAVKAVND--GRMAATVAQKP 273
Cdd:cd06321 158 QNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSVDGSPEAVAALKRegSPFIATAAQDP 237
|
250 260 270
....*....|....*....|....*....|..
gi 446681634 274 ELIGEKAMQTAKEITQGKKV-DKSIPIELELI 304
Cdd:cd06321 238 YDMARKAVELALKILNGQEPaPELVLIPSTLV 269
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
41-292 |
1.10e-54 |
|
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: 178.66 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAV-DAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVgPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADK---SLKVVAK- 195
Cdd:pfam13407 81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEkypGIKVVAEv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 196 QAADFDRAKGLSVMENILQANSN-IKAVFAHNDEMALGALEALKSAGKTD-VVVVGFDATDDAVKAVNDGRMAATVAQKP 273
Cdd:pfam13407 161 EGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGkVVVTGFDATPEALEAIKDGTIDATVLQDP 240
|
250
....*....|....*....
gi 446681634 274 ELIGEKAMQTAKEITQGKK 292
Cdd:pfam13407 241 YGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
40-304 |
1.23e-54 |
|
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: 178.79 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKVVAKQA 197
Cdd:cd19972 81 IPVIAVDRNPEDAPGDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAEApgIKVVAEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGK-TDVVVVGFDATDDAVKAVNDGRMAATVAQKPELI 276
Cdd:cd19972 161 ADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLdHKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKM 240
|
250 260
....*....|....*....|....*...
gi 446681634 277 GEKAMQTAKEITQGKKVDKSIPIELELI 304
Cdd:cd19972 241 GRLAVDSAIDLLNGKAVPKEQLQDAVLT 268
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
40-304 |
2.44e-52 |
|
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: 172.81 E-value: 2.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQN-DAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAA 118
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQGPPTfDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 119 NVPVITVD-RVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADK--SLKVVAK 195
Cdd:cd20007 81 GIKVVTVDtTLGDPSFVLSQIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMKKypGIKVLGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 196 QAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTDVV-VVGFDATDDAVKAVNDGRMAATVAQKPE 274
Cdd:cd20007 161 QYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGKVkVVGFDASPAQVEQLKAGTIDALIAQKPA 240
|
250 260 270
....*....|....*....|....*....|
gi 446681634 275 LIGEKAMQTAKEITQGKKVDKSIPIELELI 304
Cdd:cd20007 241 EIGYLAVEQAVAALTGKPVPKDILTPFVVI 270
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
40-303 |
5.81e-52 |
|
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: 172.05 E-value: 5.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAK-DSGIELIAVDAQN--DAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAAN 116
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKeANGYELLVKGIKQetDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 117 AANVPVITVD------RVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHN-VADKS 189
Cdd:cd19970 81 DAGIAVINIDnrldadALKEGGINVPFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKaFEEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 190 LKVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTD-VVVVGFDATDDAVKAVNDGRMAAT 268
Cdd:cd19970 161 MKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKMLAT 240
|
250 260 270
....*....|....*....|....*....|....*
gi 446681634 269 VAQKPELIGEKAMQTAKEITQGKKVDKSIPIELEL 303
Cdd:cd19970 241 IDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPVEL 275
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
49-304 |
3.40e-50 |
|
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: 167.52 E-value: 3.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 49 NNPFFVTLKKGAEKKAKDSGIELI--AVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVD 126
Cdd:cd06310 10 TSAFWRTVREGAEAAAKDLGVKIIfvGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPVIVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 127 RVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVA---DKSLKVVAKQAADFDRA 203
Cdd:cd06310 90 SGIKGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLkkhPGGIKVLASQYAGSDYA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 204 KGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTD-VVVVGFDATDDAVKAVNDGRMAATVAQKPELIGEKAMQ 282
Cdd:cd06310 170 KAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGqIKIVGFDSQEELLDALKNGKIDALVVQNPYEIGYEGIK 249
|
250 260
....*....|....*....|..
gi 446681634 283 TAKEITQGKKVDKSIPIELELI 304
Cdd:cd06310 250 LALKLLKGEEVPKNIDTGAELI 271
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
40-296 |
2.44e-49 |
|
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: 165.45 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd19992 1 KIGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGaNVAELEGIPGSSAARERGKGFHNVADK-----SLKVVA 194
Cdd:cd19992 81 VPVISYDRLILNADVDLYVGRDNYKVGQLQAEYALEAVPKG-NYVILSGDPGDNNAQLITAGAMDVLQPaidsgDIKIVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQAAD-FDRAKGLSVMENILQANSN-IKAVFAHNDEMALGALEALKSAG-KTDVVVVGFDATDDAVKAVNDGRMAATVAQ 271
Cdd:cd19992 160 DQYVKgWSPDEAMKLVENALTANNNnIDAVLAPNDGMAGGAIQALKAQGlAGKVFVTGQDAELAALKRIVEGTQTMTVWK 239
|
250 260
....*....|....*....|....*
gi 446681634 272 KPELIGEKAMQTAKEITQGKKVDKS 296
Cdd:cd19992 240 DLKELARAAADAAVKLAKGEKPQTT 264
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
40-297 |
1.31e-45 |
|
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: 155.47 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELI--AVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANA 117
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTflGPATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 118 ANvPVITVDRVANSGKVVSHIASNNIEGGQMASDY----IRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS---L 190
Cdd:cd20008 81 GI-PVVLVDSGANTDDYDAFLATDNVAAGALAADElaelLKASGGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKypdI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 191 KVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAATV 269
Cdd:cd20008 160 EIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAgKIVLVGFDSSPDEVALLKSGVIKALV 239
|
250 260
....*....|....*....|....*....
gi 446681634 270 AQKPELIGEKAMQTAKEITQGKK-VDKSI 297
Cdd:cd20008 240 VQDPYQMGYEGVKTAVKALKGEEiVEKNV 268
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
48-304 |
5.56e-44 |
|
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: 151.20 E-value: 5.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 48 LNNPFFVTLKKGAEKKAKDSGIELI-AVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVD 126
Cdd:cd06314 9 LNNPFWDLAEAGAEKAAKELGVNVEfVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 127 RVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKVVAKQAADFDRAK 204
Cdd:cd06314 89 SDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKGSpgIEIVDPLSDNDDIAK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 205 GLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAATVAQKPELIGEKAMQT 283
Cdd:cd06314 169 AVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVgKVKIVGFDTLPETLQGIKDGVIAATVGQRPYEMGYLSVKL 248
|
250 260
....*....|....*....|..
gi 446681634 284 AKEITQGKK-VDKSIPIELELI 304
Cdd:cd06314 249 LYKLLKGGKpVPDVIDTGVDVV 270
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
47-307 |
1.53e-42 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 148.48 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 47 TLNNPFFVTLKKGAEKKAKDSGI--ELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVIT 124
Cdd:PRK09701 33 TLSNPFWVDMKKGIEDEAKTLGVsvDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 125 VDRVAN-------SGKVVSHIASNNIEGGQMASDYIRE-LVGEGANVAELEGIPG--SSAARERGKGFHNVADKSLKVVA 194
Cdd:PRK09701 113 LDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDkLGAEGGEVAIIEGKAGnaSGEARRNGATEAFKKASQIKLVA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAATVAQKP 273
Cdd:PRK09701 193 SQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTgKVLVVGTDGIPEARKMVEAGQMTATVAQNP 272
|
250 260 270
....*....|....*....|....*....|....*
gi 446681634 274 ELIGEKAMQTAKE-ITQGKKVDKSIPIELELIKKN 307
Cdd:PRK09701 273 ADIGATGLKLMVDaEKSGKVIPLDKAPEFKLVDSI 307
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
40-304 |
1.48e-41 |
|
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: 145.85 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAE---KKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAAN 116
Cdd:cd19996 1 TIGFSNAGLGNSWRVQMIAEFEaeaAKLKKLIKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 117 AANVPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKVVA 194
Cdd:cd19996 81 AAGIPVVLFDSGVGSDKYTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYpgIKIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTDVVVVGFDATDD--AVKAVNDGRMAATVaqK 272
Cdd:cd19996 161 EVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTGEDNNGFlkAWKELPGFKSIAPS--Y 238
|
250 260 270
....*....|....*....|....*....|..
gi 446681634 273 PELIGEKAMQTAKEITQGKKVDKSIPIELELI 304
Cdd:cd19996 239 PPWLGATALDAALAALEGEPVPKYVYIPLPVI 270
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
50-306 |
1.56e-41 |
|
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: 145.07 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 50 NPFFVTLKKGAEKKAKDSGIELIAVDAQ--NDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVDR 127
Cdd:cd20004 11 HDFWKSVKAGAEKAAQELGVEIYWRGPSreDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 128 VANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS---LKVVAKQAADFDRAK 204
Cdd:cd20004 91 DLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAKGSASTTDRERGFLEALKKLapgLKVVDDQYAGGTVGE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 205 GLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGK-TDVVVVGFDATDDAVKAVNDGRMAATVAQKPELIGEKAMQT 283
Cdd:cd20004 171 ARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLaGKVKFIGFDASDLLLDALRAGEISALVVQDPYRMGYLGVKT 250
|
250 260
....*....|....*....|...
gi 446681634 284 AKEITQGKKVDKSIPIELELIKK 306
Cdd:cd20004 251 AVAALRGKPVPKRIDTGVVLVTK 273
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
37-294 |
1.78e-40 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 142.97 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 37 KTIKVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAAN 116
Cdd:COG4213 1 GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 117 AANVPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGE--GANVAELEGIPGSSAARERGKGFHNV-----ADKS 189
Cdd:COG4213 81 AAGIPVIAYDRLILNSDVDYYVSFDNVKVGELQGQYLVDGLPLkgKGNIELFGGSPTDNNATLFFEGAMSVlqpyiDSGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 190 LKVVAKQAA-DFDRAKGLSVMENILQANSN-IKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMA 266
Cdd:COG4213 161 LVVVSGQWTlGWDPETAQKRMENLLTANGNkVDAVLAPNDGLAGGIIQALKAQGLAgKVVVTGQDAELAAVQRILAGTQY 240
|
250 260
....*....|....*....|....*....
gi 446681634 267 ATVAqKP-ELIGEKAMQTAKEITQGKKVD 294
Cdd:COG4213 241 MTVY-KDtRELAEAAAELAVALAKGEKPE 268
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
39-293 |
2.36e-40 |
|
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: 142.72 E-value: 2.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 39 IKVGFSVSTLNNPFFVTLKKGAEKKAK-DSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANA 117
Cdd:cd01539 1 IKIGVFIYNYDDTFISSVRKALEKAAKaGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 118 ANVPVITVDR-----VANSGKVVSHIASNNIEGG----QMASDYIRE-----LVGEGA-NVAELEGIPGSSAARERGKGF 182
Cdd:cd01539 81 ANIPVIFFNRepsreDLKSYDKAYYVGTDAEESGimqgEIIADYWKAnpeidKNGDGKiQYVMLKGEPGHQDAIARTKYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 183 HNVADKS---LKVVAKQAADFDRAKGLSVMENILQANS-NIKAVFAHNDEMALGALEALKSAGKTD------VVVVGFDA 252
Cdd:cd01539 161 VKTLNDAgikTEQLAEDTANWDRAQAKDKMDAWLSKYGdKIELVIANNDDMALGAIEALKAAGYNTgdgdkyIPVFGVDA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446681634 253 TDDAVKAVNDGRMAATVAQKPELIGEKAMQTAKEITQGKKV 293
Cdd:cd01539 241 TPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEP 281
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
40-301 |
3.79e-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: 380534 [Multi-domain] Cd Length: 270 Bit Score: 138.65 E-value: 3.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKD-SGIELIAVDAQNdAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAA 118
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKElADLEYKLVTSSN-ANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 119 NVPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKSL--KVVAKQ 196
Cdd:cd06311 80 GIPVVNFDRGLNVLIYDLYVAGDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNPgiKILAMQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 197 AADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTDV-VVVGFDATDDAVKAVNDGR--MAATVAQKP 273
Cdd:cd06311 160 AGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIkVMTGGGGSQEYFKRIMDGDpiWPASATYSP 239
|
250 260 270
....*....|....*....|....*....|.
gi 446681634 274 ELIGEkAMQTAKEITQGKK---VDKSIPIEL 301
Cdd:cd06311 240 AMIAD-AIKLAVLILKGGKtveKEVIIPSTL 269
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
52-297 |
9.11e-38 |
|
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: 135.06 E-value: 9.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 52 FFVTLKKGAEKKAKDSGIELIAV--DAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVDRVA 129
Cdd:cd20005 13 FWKAVKKGAEQAAKELGVKITFEgpDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 130 NSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADK---SLKVVAKQAADFDRAKGL 206
Cdd:cd20005 93 PSDLPLATVATDNYAAGALAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEkypDIKVVNVQYGVGDHAKAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 207 SVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAATVAQKPELIGEKAMQTAK 285
Cdd:cd20005 173 DIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLgKIKVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAAV 252
|
250
....*....|..
gi 446681634 286 EITQGKKVDKSI 297
Cdd:cd20005 253 KALKGEEVEKLI 264
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
52-306 |
2.11e-37 |
|
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: 134.43 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 52 FFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVDRVANS 131
Cdd:cd06317 13 FFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAVIPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 132 GKVVSHIASNNIEG----GQMASDYIRELVGEGANVAELeGIPGSSAARERGKGFHNVADK--SLKVVAKQAADFDRAKG 205
Cdd:cd06317 93 DFQAAQVGVDNLEGgkeiGKYAADYIKAELGGQAKIGVV-GALSSLIQNQRQKGFEEALKAnpGVEIVATVDGQNVQEKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 206 LSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKA-VNDGRMAATVAQKPELIGEKAMQT 283
Cdd:cd06317 172 LSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQgKIKVFGWDLTKQAIFLgIDEGVLQAVVQQDPEKMGYEAVKA 251
|
250 260
....*....|....*....|...
gi 446681634 284 AKEITQGKKVDKSIPIELELIKK 306
Cdd:cd06317 252 AVKAIKGEDVEKTIDVPPTIVTK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
46-306 |
4.35e-36 |
|
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: 130.80 E-value: 4.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 46 STLNNPFFVTLKKGAEKKAKDSGIEL--IAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVI 123
Cdd:cd20006 9 SDPNSDFWQTVKSGAEAAAKEYGVDLefLGPESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 124 TVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNV--ADKSLKVVAKQAADFD 201
Cdd:cd20006 89 TIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQAlaEYPNIKIVETEYCDSD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 202 RAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG-KTDVVVVGFDATDDAVKAVNDGRMAATVAQKPELIGEKA 280
Cdd:cd20006 169 EEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGlGGKVKVVGFDSSVEEIQLLEEGIIDALVVQNPFNMGYLS 248
|
250 260
....*....|....*....|....*.
gi 446681634 281 MQTAKEITQGKKVDKSIPIELELIKK 306
Cdd:cd20006 249 VQAAVDLLNGKKIPKRIDTGSVVITK 274
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
41-304 |
1.13e-35 |
|
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: 129.17 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAnv 120
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGKVvSHIASNNIEGGQMASDYireLVGEGA-NVAELEGIPGSSAARERGKGF------HNVADKSLKVV 193
Cdd:cd06267 80 PVVLIDRRLDGLGV-DSVVVDNYAGAYLATEH---LIELGHrRIAFIGGPLDLSTSRERLEGYrdalaeAGLPVDPELVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 194 AkqaADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDatddavkavnDGRMAA--- 267
Cdd:cd06267 156 E---GDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRvpeDISVVGFD----------DIPLAAllt 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446681634 268 ----TVAQKPELIGEKAMQTA-KEITQGKKVDKSIPIELELI 304
Cdd:cd06267 223 ppltTVRQPAYEMGRAAAELLlERIEGEEEPPRRIVLPTELV 264
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
33-304 |
2.21e-34 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 127.62 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 33 KGRNKTIkvGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAV 112
Cdd:COG1609 58 TGRTRTI--GVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLER 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 113 SAANAAnvPVITVDRVANSGKVvSHIASNNIEGGQMASDYireLVGEGA-NVAELEGIPGSSAARERGKGFHNV-ADKSL 190
Cdd:COG1609 136 LAEAGI--PVVLIDRPLPDPGV-PSVGVDNRAGARLATEH---LIELGHrRIAFIGGPADSSSARERLAGYREAlAEAGL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 191 KVVAKQ--AADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDatddavkavnDGRM 265
Cdd:COG1609 210 PPDPELvvEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRvpeDVSVVGFD----------DIPL 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446681634 266 AA-------TVAQKPELIGEKAMQTA-KEITQGKKVDKSIPIELELI 304
Cdd:COG1609 280 ARyltppltTVRQPIEEMGRRAAELLlDRIEGPDAPPERVLLPPELV 326
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
41-286 |
9.29e-32 |
|
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: 119.50 E-value: 9.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELI--AVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAA 118
Cdd:cd19973 2 IGLITKTDTNPFFVKMKEGAQKAAKALGIKLMtaAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 119 NVPVITVDRVANSGKVV-SHIASNNIEGGQMASDYIRELVGEG-ANVAELEGIPGSSAARERGKGF------------HN 184
Cdd:cd19973 82 GVLVIALDTPTDPIDAAdATFATDNFKAGVLIGEWAKAALGAKdAKIATLDLTPGHTVGVLRHQGFlkgfgidekdpeSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 185 VADKSLKVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGK-TDVVVVGFDATDDAVKAVNDG 263
Cdd:cd19973 162 EDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKeKGVLIVSVDGGCPGVKDVKDG 241
|
250 260
....*....|....*....|...
gi 446681634 264 RMAATVAQKPELIGEKAMQTAKE 286
Cdd:cd19973 242 IIGATSQQYPLRMAALGVEAIAA 264
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
41-305 |
6.27e-31 |
|
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: 116.85 E-value: 6.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAAnaanv 120
Cdd:cd06291 2 IGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYKKLNI----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGkvVSHIASNNIEGGQMAsdyIRELVGEGA-NVAELEGIPGSSAARERGKGF------HNVADKSLKVV 193
Cdd:cd06291 77 PIVSIDRYLSEG--IPSVSSDNYQGGRLA---AEHLIEKGCkKILHIGGPSNNSPANERYRGFedalkeAGIEYEIIEID 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 194 AKqaaDFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDDAvkavndgRMA---- 266
Cdd:cd06291 152 EN---DFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRvpeDVQIIGFDGIEIS-------ELLypel 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446681634 267 ATVAQKPELIGEKAMQTA-KEITQGKKVDKSIPIELELIK 305
Cdd:cd06291 222 TTIRQPIEEMAKEAVELLlKLIEGEEIEESRIVLPVELIE 261
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
40-292 |
1.83e-30 |
|
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: 115.98 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGaNVAELEGIPGSSAARERGKGFHNVADKS-----LKVVA 194
Cdd:cd01538 81 IKVIAYDRLILNADVDYYISFDNEKVGELQAQALLDAKPEG-NYVLIGGSPTDNNAKLFRDGQMKVLQPAidsgkIKVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQAAD-FDRAKGLSVMENILQANSN-IKAVFAHNDEMALGALEALKSAG-KTDVVVVGFDATDDAVKAVNDGRMAATVAQ 271
Cdd:cd01538 160 DQWVDdWLPANAQQIMENALTANGNnVDAVVASNDGTAGGAIAALKAQGlSGGVPVSGQDADLAAIKRILAGTQTMTVYK 239
|
250 260
....*....|....*....|.
gi 446681634 272 KPELIGEKAMQTAKEITQGKK 292
Cdd:cd01538 240 DIRLLADAAAEVAVALMRGEK 260
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
40-304 |
3.02e-30 |
|
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: 114.99 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQ--NDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANA 117
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGgyTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 118 ANVPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGA-NVAELEGIPGSSAARERGKGF-HNVADKSLKVVAK 195
Cdd:cd06306 81 AGIPVIDLVNGIDSPKVAARVLVDFYDMGYLAGEYLVEHHPGKPvKVAWFPGPAGAGWAEDREKGFkEALAGSNVEIVAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 196 QAADFDRAKGLSVMENILQANSNIKAVFAhNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAATVAQKPE 274
Cdd:cd06306 161 KYGDTGKAVQLNLVEDALQAHPDIDYIVG-NAVAAEAAVGALREAGLTgKVKVVSTYLTPGVYRGIKRGKILAAPSDQPV 239
|
250 260 270
....*....|....*....|....*....|
gi 446681634 275 LIGEKAMQTAKEITQGKKVDKSIPIELELI 304
Cdd:cd06306 240 LQGRIAVDQAVRALEGKPVPKHVGPPILVV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
40-270 |
1.52e-29 |
|
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: 114.24 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSV-STLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQ--KGVDVVVINPtDSDAVASAVSAAN 116
Cdd:cd06324 1 RVVFINpGKEDEPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLArpPKPDYLILVN-EKGVAPELLELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 117 AANVPVITVDRV------ANSGK-------VVSHIASNNIEGG-QMASDYIRELV----GEGANVAELEGIPGSSAARER 178
Cdd:cd06324 80 QAKIPVFLINNDltdeerALLGKprekfkyWLGSIVPDNEQAGyLLAKALIKAARkksdDGKIRVLAISGDKSTPASILR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 179 GKGFHNVADKSLKVVAKQA--ADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDAT 253
Cdd:cd06324 160 EQGLRDALAEHPDVTLLQIvyANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKpgkDVLVGGIDWS 239
|
250
....*....|....*..
gi 446681634 254 DDAVKAVNDGRMAATVA 270
Cdd:cd06324 240 PEALQAVKDGELTASVG 256
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
40-299 |
1.72e-29 |
|
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: 113.49 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd19991 1 KIGFSMDSLRVERWQRDRDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGaNVAELEGIPGSSAARERGKGFHNV-----ADKSLKVVA 194
Cdd:cd19991 81 VPVLAYDRLILNADVDLYVSFDNEKVGELQAEALVKAKPKG-NYVLLGGSPTDNNAKLFREGQMKVlqpliDSGDIKVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQ-AADFDRAKGLSVMENILQANSN-IKAVFAHNDEMALGALEALKSAG-KTDVVVVGFDATDDAVKAVNDGRMAATVAQ 271
Cdd:cd19991 160 DQwVDDWDPEEALKIMENALTANNNkIDAVIASNDGTAGGAIQALAEQGlAGKVAVSGQDADLAACQRIVEGTQTMTIYK 239
|
250 260
....*....|....*....|....*...
gi 446681634 272 KPELIGEKAMQTAKEITQGKKVDKSIPI 299
Cdd:cd19991 240 PIKELAEKAAELAVALAKGEKNEANRTI 267
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
40-307 |
5.61e-29 |
|
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: 111.55 E-value: 5.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAan 119
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLAEGI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 vPVITVDRVANSGKVVShIASNNIEGGQMASDYIRELvgeGA-NVAELEGIPGSSAARERGKGF-HNVADKSLKVVAK-- 195
Cdd:cd06290 79 -PVVLVDRELEGLNLPV-VNVDNEQGGYNATNHLIDL---GHrRIVHISGPEDHPDAQERYAGYrRALEDAGLEVDPRli 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 196 QAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG---KTDVVVVGFDatDDAVKAVNDGRMaATVAQK 272
Cdd:cd06290 154 VEGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGirvPDDVSVIGFD--DLPFSKYTTPPL-TTVRQP 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 446681634 273 PELIGEKAMQTAKEITQGKKVDKSIPI-ELELIKKN 307
Cdd:cd06290 231 LYEMGKTAAEILLELIEGKGRPPRRIIlPTELVIRE 266
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
41-295 |
6.43e-29 |
|
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: 111.57 E-value: 6.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINpTDSDAVASAVSAANAANV 120
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAIN-LVDPAAAGVAEKARGQNV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEgaNVAELEGIPGSSAARERGKGFHN-VADKSLKV--VAKQA 197
Cdd:cd01537 81 PVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHI--QIVLLKGPLGHPDAEARLAGVIKeLNDKGIKTeqLQLDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGK---TDVVVVGFDATDDAVKAvndGRMAATVAQKPE 274
Cdd:cd01537 159 GDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLrvpSDISVFGYDALPEALKS---GPLLTTILQDAN 235
|
250 260
....*....|....*....|.
gi 446681634 275 LIGEKAMQTAKEITQGKKVDK 295
Cdd:cd01537 236 NLGKTTFDLLLNLADNWKIDN 256
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
41-304 |
6.81e-28 |
|
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: 108.85 E-value: 6.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTdsDAVASAVSAANAANV 120
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPA--RDDAPDLQELAARGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGKVVShIASNNIEGGQMASDYIRELvgeG-ANVAELEGIPGSSAARERGKGFHNV---ADKSLKVVAKQ 196
Cdd:cd06285 80 PVVLVDRRIGDTALPS-VTVDNELGGRLATRHLLEL---GhRRIAVVAGPLNASTGRDRLRGYRRAlaeAGLPVPDERIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 197 AADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDDAvkavndgRMAA----TV 269
Cdd:cd06285 156 PGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRvpeDLSVVGFDDIPLA-------AFLPppltTV 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 446681634 270 AQKPELIGEKAMQTAKEITQGKKVDK-SIPIELELI 304
Cdd:cd06285 229 RQPKYEMGRRAAELLLQLIEGGGRPPrSITLPPELV 264
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
41-304 |
7.53e-28 |
|
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus 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: 380503 [Multi-domain] Cd Length: 266 Bit Score: 108.50 E-value: 7.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTdsDAVASAVSAANAANV 120
Cdd:cd06280 2 IGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPS--AGPSRELKRLLKHGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVAnSGKVVSHIASNNIEGGQMASDYIRELVGEgaNVAELEGIPGSSAARERGKGFHN-VADKSLKVVAK--QA 197
Cdd:cd06280 80 PIVLIDREV-EGLELDLVAGDNREGAYKAVKHLIELGHR--RIGLITGPLEISTTRERLAGYREaLAEAGIPVDESliFE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDDAvkAVNDGRMAAtVAQKPE 274
Cdd:cd06280 157 GDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEipqDISVVGFDDSDWF--EIVDPPLTV-VAQPAY 233
|
250 260 270
....*....|....*....|....*....|.
gi 446681634 275 LIGEKAMQTAKEITQGKKVDK-SIPIELELI 304
Cdd:cd06280 234 EIGRIAAQLLLERIEGQGEEPrRIVLPTELI 264
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
51-297 |
1.59e-27 |
|
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: 108.53 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 51 PFFVtlkkgAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVDRVAN 130
Cdd:cd19995 20 PGFE-----KAMKKLCPDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 131 SGKVVSHIASNNIEGGQMASDYIRELV----GEGANVAELEGIPGSSAARERGKGFHNVADKS-----LKVVAKQ-AADF 200
Cdd:cd19995 95 GGPADYYVSFDNVAVGEAQAQSLVDHLkaigKKGVNIVMINGSPTDNNAGLFKKGAHEVLDPLgdsgeLKLVCEYdTPDW 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 201 DRAKGLSVMENIL-QANSNIKAVFAHNDEMALGALEALKSAG-KTDVVVVGFDATDDAVKAVNDGRMAATVAQKPELIGE 278
Cdd:cd19995 175 DPANAQTAMEQALtKLGNNIDGVLSANDGLAGGAIAALKAQGlAGKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAA 254
|
250
....*....|....*....
gi 446681634 279 KAMQTAKEITQGKKVDKSI 297
Cdd:cd19995 255 AAAKVAVALLKGETPPSDL 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
40-297 |
2.60e-27 |
|
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: 108.16 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKA---KDSGI--ELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSA 114
Cdd:cd19999 1 VIGVSNGYVGNEWRAQMIADFEEVAaeyKEEGVisDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 115 ANAANVPVITVDRVANSGKVVShIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKV 192
Cdd:cd19999 81 AQAAGILVVSFDQPVSSPDAIN-VVIDQYKWAAIQAQWLAEQLGGKGNIVAINGVAGNPANEARVKAADDVFAKYpgIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 193 VAKQAADFDRAKGLSVMENILQANSNIKAVFAHnDEMALGALEALKSAGKTDVVVVGfDATDDAVKAVNDGRMAA--TVA 270
Cdd:cd19999 160 LASVPGGWDQATAQQVMATLLATYPDIDGVLTQ-DGMAEGVLRAFQAAGKDPPVMTG-DYRKGFLRKWKELDLPDfeSIG 237
|
250 260
....*....|....*....|....*...
gi 446681634 271 Q-KPELIGEKAMQTAKEITQGKKVDKSI 297
Cdd:cd19999 238 VvNPPGIGATALRIAVRLLQGKELKEDA 265
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
51-283 |
3.06e-27 |
|
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: 107.42 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 51 PFFVTLKKGAEKKAKDSGIEL-IAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVDRVA 129
Cdd:cd19969 12 PYWDDVKEGFEDAGAELGVKTeYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSDA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 130 NSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEGiPGSSAARERGKGFHNVADK--SLKVVAKQAADFDRAKGLS 207
Cdd:cd19969 92 PESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTG-PGQPNHEERVEGFKEAFAEypGIEVVAVGDDNDDPEKAAQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446681634 208 VMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAATVAQKPELIGEKAMQT 283
Cdd:cd19969 171 NTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTgKVKIVAFDDDPETLDLIKDGVIDASIAQRPWMMGYWSLQF 247
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
40-292 |
4.19e-27 |
|
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: 107.41 E-value: 4.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGI-----ELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSA 114
Cdd:cd06300 1 TIGLSNTYAGNSWREQMIASLKADAAQSGQkglvkELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 115 ANAANVPVITVDRVANSGKVVsHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKV 192
Cdd:cd06300 81 AADAGIPVVAFDGAVTSPDAY-NVSNDQVEWGRLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEALAEYpgIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 193 VAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEmALGALEALKSAGKTDVVVVGFDATDDA---VKAVNDGRMAATV 269
Cdd:cd06300 160 VGEVFGGWDEATAQTAMLDFLATHPQVDGVWTQGGE-DTGVLQAFQQAGRPPVPIVGGDENGFAkqwWKHPKKGLTGAAV 238
|
250 260
....*....|....*....|...
gi 446681634 270 AQkPELIGEKAMQTAKEITQGKK 292
Cdd:cd06300 239 WP-PPAIGAAGLEVALRLLEGQG 260
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
40-302 |
7.48e-27 |
|
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: 106.41 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd19993 1 VVGVSWSNFQEERWKTDEAAMKKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSgKVVSHIASNNIEGGQMASDYIRELVGEGaNVAELEGIPGSSAARERGKGFHNVADKSL-----KVVA 194
Cdd:cd19993 81 IPVIAYDRLIEN-PIAFYISFDNVEVGRMQARGVLKAKPEG-NYVFIKGSPTDPNADFLRAGQMEVLQPAIdsgkiKIVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQAAD-FDRAKGLSVMENILQANSN-IKAVFAHNDEMALGALEALKSAGKTDVV-VVGFDATDDAVKAVNDGRMAATVAQ 271
Cdd:cd19993 159 EQYTDgWKPANAQKNMEQILTANNNkVDAVVASNDGTAGGAVAALAAQGLAGKVpVSGQDADKAALNRIALGTQTVTVWK 238
|
250 260 270
....*....|....*....|....*....|.
gi 446681634 272 KPELIGEKAMQTAKEITQGKKVDKSIPIELE 302
Cdd:cd19993 239 DARELGKEAAEIAVELAKGTKIEAIKGAALT 269
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
40-284 |
1.64e-25 |
|
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: 102.37 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVsHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAAReRGKGFHNVAD---KSLKVVAKQ 196
Cdd:cd06305 81 IPVVTFDTDSQVPGVN-NITQDDYALGTLSLGQLVKDLNGEGNIAVFNVFGVPPLDK-RYDIYKAVLKanpGIKKIVAEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 197 AADFD--RAKGLSVMENILQANSN--IKAVFAHNDEMALGALEALKSAGKTDVVVVGFDATDDAVKAV--NDGRMAATVA 270
Cdd:cd06305 159 GDVTPntAADAQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISNQDLELMadEGSPWVATAA 238
|
250
....*....|....
gi 446681634 271 QKPELIGEKAMQTA 284
Cdd:cd06305 239 QDPALIGTVAVRNV 252
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
41-280 |
3.34e-25 |
|
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: 101.49 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANv 120
Cdd:cd06289 2 VGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTTAELLRRLKAWGI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDR-VANSGkvVSHIASNNIEGGQMASDYireLVGEGA-NVAELEGIPGSSAARERGKGFHNVADK------SLKV 192
Cdd:cd06289 81 PVVLALRdVPGSD--LDYVGIDNRLGAQLATEH---LIALGHrRIAFLGGLSDSSTRRERLAGFRAALAEaglpldESLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 193 VAKQAadfDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDatDdavkaVNDGRMA--- 266
Cdd:cd06289 156 VPGPA---TREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEpgrDIAVVGFD--D-----VPEAALWtpp 225
|
250
....*....|....*
gi 446681634 267 -ATVAQKPELIGEKA 280
Cdd:cd06289 226 lTTVSVHPREIGRRA 240
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
41-307 |
8.18e-25 |
|
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: 100.29 E-value: 8.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAnv 120
Cdd:cd06270 2 IGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIP-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRvansgkvvsHIAS--------NNIEGGQMASDYireLVGEG-ANVAELEGIPGSSAARERGKGF------HNV 185
Cdd:cd06270 80 PLVVINR---------YIPGladrcvwlDNEQGGRLAAEH---LLDLGhRRIACITGPLDIPDARERLAGYrdalaeAGI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 186 ADKSLKVVAkqaADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG---KTDVVVVGFDatddavkavnD 262
Cdd:cd06270 148 PLDPSLIIE---GDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGikvPEDVSVIGFD----------D 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446681634 263 GRMAA-------TVAQKPELIGEKAMQTAKEITQGKKVDKSIPIELELIKKN 307
Cdd:cd06270 215 VPLARylspkltTVHYPIEEMAQAAAELALNLAYGEPLPISHEFTPTLIERD 266
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
41-304 |
1.14e-24 |
|
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: 100.02 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVD-VVVInpTDSDAVASAVSAANAAN 119
Cdd:cd06275 2 IGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDgLLLM--CSEMTDDDAELLAALRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKVVShIASNNIEGGQMASDYireLVGEG-ANVAELEGIPGSSAARERGKGFHNV-ADKSLKVVAKQA 197
Cdd:cd06275 80 IPVVVLDREIAGDNADA-VLDDSFQGGYLATRH---LIELGhRRIGCITGPLEHSVSRERLAGFRRAlAEAGIEVPPSWI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 A--DFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG---KTDVVVVGFDatddavkavnDGRMAA----- 267
Cdd:cd06275 156 VegDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGlrvPQDISIIGYD----------DIELARyfspa 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446681634 268 --TVAQKPELIGEKAMQTAKE-ITQGKKVDKSIPIELELI 304
Cdd:cd06275 226 ltTIHQPKDELGELAVELLLDrIENKREEPQSIVLEPELI 265
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
41-282 |
1.73e-24 |
|
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: 99.53 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAkQTNDVEDLIQKGVDVVVInpTDSDAVASAVSAANAANV 120
Cdd:cd06278 2 VGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDD-VDDALRQLLQYRVDGVIV--TSATLSSELAEECARRGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVaNSGKVVSHIASNNIEGGQMASDYireLVGEGA-NVAELEGIPGSSAARERGKGFHN-VADKSLKVVAKQAA 198
Cdd:cd06278 79 PVVLFNRV-VEDPGVDSVSCDNRAGGRLAADL---LLAAGHrRIAFLGGPEGTSTSRERERGFRAaLAELGLPPPAVEAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 199 DFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT----DVVVVGFDatddavkavnDGRMAA------- 267
Cdd:cd06278 155 DYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGLvvpeDISVVGFD----------DIPMAAwpsydlt 224
|
250
....*....|....*
gi 446681634 268 TVAQKPELIGEKAMQ 282
Cdd:cd06278 225 TVRQPIEEMAEAAVD 239
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
40-293 |
1.86e-24 |
|
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: 100.00 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAV-DAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAA 118
Cdd:cd06316 1 KVAIAMHTTGSDWSRLQVAGIKDTFEELGIEVVAVtDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 119 NVPVITVDRVAN---SGK-VVSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNV-ADKS--LK 191
Cdd:cd06316 81 GIKLVFMDNVPDgleAGKdYVSVVSSDNRGNGQIAAELLAEAIGGKGKVGIIYHDADFYATNQRDKAFKDTlKEKYpdIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 192 VVAKQAADfDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTDVVVVGFD-ATDDAVKAVNDGRMAATVA 270
Cdd:cd06316 161 IVAEQGFA-DPNDAEEVASAMLTANPDIDGIYVSWDTPALGVISALRAAGRSDIKITTVDlGTEIALDMAKGGNVKGIGA 239
|
250 260
....*....|....*....|....
gi 446681634 271 QKPELIGE-KAMQTAKEITqGKKV 293
Cdd:cd06316 240 QRPYDQGVaEALAAALALL-GKEV 262
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
45-304 |
1.03e-22 |
|
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: 94.91 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 45 VSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVD-VVVINPTDSDAVASAVSAANaanvP-V 122
Cdd:cd06284 6 VPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDgVILLSGRLDAELLSELSKRY----PiV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 123 ITVDRVANSGkvVSHIASNNIEGGQMASDYIRELvgeG-ANVAELEGIPGSSAARERGKGF------HNVADKSLkvvAK 195
Cdd:cd06284 82 QCCEYIPDSG--VPSVSIDNEAAAYDATEYLISL---GhRRIAHINGPLDNVYARERLEGYrralaeAGLPVDED---LI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 196 QAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDdavkavndgrMAA----- 267
Cdd:cd06284 154 IEGDFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRvpeDVSVIGFDDIE----------FAEmfsps 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446681634 268 --TVAQKPELIGEKAMQTAKEITQGKKVD-KSIPIELELI 304
Cdd:cd06284 224 ltTIRQPRYEIGETAAELLLEKIEGEGVPpEHIILPHELI 263
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
50-305 |
1.83e-22 |
|
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: 94.24 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 50 NPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTdSDAVASAVSAANAANVPVITVDRVA 129
Cdd:cd19976 11 NPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASS-NISDEAIIKLLKEEKIPVVVLDRYI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 130 NSGKVVShIASNNIEGGQMASDYIRELVGEgaNVAELEGIPGSSAARERGKGFHNvADKSLKVVAKQAADF---DRAKGL 206
Cdd:cd19976 90 EDNDSDS-VGVDDYRGGYEATKYLIELGHT--RIGCIVGPPSTYNEHERIEGYKN-ALQDHNLPIDESWIYsgeSSLEGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 207 SVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDdavkavndgrMA-------ATVAQKPELI 276
Cdd:cd19976 166 YKAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKipeDLSVIGFDNII----------LSeyitpalTTIAQPIFEM 235
|
250 260 270
....*....|....*....|....*....|
gi 446681634 277 GEKAMQTA-KEITQGKKVDKSIPIELELIK 305
Cdd:cd19976 236 GQEAAKLLlKIIKNPAKKKEEIVLPPELIK 265
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
41-304 |
6.56e-22 |
|
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: 92.72 E-value: 6.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTdsDAVASAVSAANAANV 120
Cdd:cd06293 2 IGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPS--DDDLSHLARLRARGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVAnSGKVVSHIASNNIEGGQMAsdyIRELVGEGAN-VAELEGIPGSSAARERGKGFHNVA-----DKSLKVVA 194
Cdd:cd06293 80 AVVLLDRPA-PGPAGCSVSVDDVQGGALA---VDHLLELGHRrIAFVSGPLRTRQVAERLAGARAAVaeaglDPDEVVRE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG---KTDVVVVGFDATDDAvkavndgRMAA---- 267
Cdd:cd06293 156 LSAPDANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGlrvPDDVSVVGYDDLPFA-------AAANpplt 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 446681634 268 TVAQKPELIGEKAMQTA-KEITQGKKVDKSIPIELELI 304
Cdd:cd06293 229 TVRQPSYELGRAAADLLlDEIEGPGHPHEHVVFQPELV 266
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
41-304 |
7.13e-22 |
|
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: 92.59 E-value: 7.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTdsDAVASAVSAANAANV 120
Cdd:cd19977 2 IGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPT--GGNEDLIEKLVKSGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANsGKVVSHIASNNIEGGQMAsdyIRELVGEGA-NVAELEGIPGSSAARERGKGFHN-VADKSLKVVAKQ-A 197
Cdd:cd19977 80 PVVFVDRYIP-GLDVDTVVVDNFKGAYQA---TEHLIELGHkRIAFITYPLELSTRQERLEGYKAaLADHGLPVDEELiK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATdDAVKAVNDGRMaaTVAQKPE 274
Cdd:cd19977 156 HVDRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRipdDIALIGFDDI-PWADLFNPPLT--VIAQPTY 232
|
250 260 270
....*....|....*....|....*....|..
gi 446681634 275 LIGEKAMQT-AKEITQGKKVDKS-IPIELELI 304
Cdd:cd19977 233 EIGRKAAELlLDRIENKPKGPPRqIVLPTELI 264
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
55-297 |
5.88e-21 |
|
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: 90.81 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 55 TLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVDRVAnSGKV 134
Cdd:cd19998 20 IAKAAAKQPPYADKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVV-DEPC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 135 VSHIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS--LKVVAKQAADFDRAKGLSVMENI 212
Cdd:cd19998 99 AYNVNTDQAKAGEQTAQWLVDKLGGKGNILMVRGVPGTSVDRDRYEGAKEVFKKYpdIKVVAEYYGNWDDGTAQKAVADA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 213 LQANSNIKAVFAHNDEMalGALEALKSAGKtDVVVVGFDATDDAVKAvndgrMAATVAQK--------PELIGEKAMQTA 284
Cdd:cd19998 179 LAAHPDVDGVWTQGGET--GVIKALQAAGH-PLVPVGGEAENGFRKA-----MLEPLANGlpgisagsPPALSAVALKLA 250
|
250
....*....|...
gi 446681634 285 KEITQGKKVDKSI 297
Cdd:cd19998 251 VAVLEGEKEPKTI 263
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
40-294 |
9.03e-21 |
|
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: 90.38 E-value: 9.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd19994 1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDR-VANSGKVVSHIASNNIEGGQMASDYIRE---LVGEGANVaELEGIPGSSA----------ARERGKGFhnV 185
Cdd:cd19994 81 IPVIAYDRlIMNTDAVDYYVTFDNEKVGELQGQYLVDklgLKDGKGPF-NIELFAGSPDdnnaqlffkgAMEVLQPY--I 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 186 ADKSLKVVAKQA-------ADFDRAKGLSVMENILQAN----SNIKAVFAHNDEMALGALEALKSAGKTD---VVVVGFD 251
Cdd:cd19994 158 DDGTLVVRSGQTtfeqvatPDWDTETAQARMETLLSAYytggKKLDAVLSPNDGIARGVIEALKAAGYDTgpwPVVTGQD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446681634 252 ATDDAVKAVNDGRMAATVAQKPELIGEKAMQTAKEITQGKKVD 294
Cdd:cd19994 238 AEDASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVE 280
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
36-251 |
8.35e-20 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 87.83 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 36 NKTIKVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAA 115
Cdd:PRK10423 54 NQTRTIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMQR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 116 NAANvPVITVDRVANSGkVVSHIASNNIEGGQMASDYireLVGEG-ANVAELEGIPGSSAARERGKGFHNVADKSLKVVA 194
Cdd:PRK10423 134 YPSV-PTVMMDWAPFDG-DSDLIQDNSLLGGDLATQY---LIDKGyTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIP 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446681634 195 KQ---AADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFD 251
Cdd:PRK10423 209 DGyevTGDFEFNGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLSvpqDIAVIGYD 271
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
44-293 |
1.00e-18 |
|
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: 84.24 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 44 SVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN---- 119
Cdd:cd01391 8 SLHQIREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNLAQLFDIpqla 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 -VPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGegANVAELEGiPGSSAARERGKGFHNVADK-SLKVVAKQA 197
Cdd:cd01391 88 lDATSQDLSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNW--TYVAAIHG-EGLNSGELRMAGFKELAKQeGICIVASDK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDR-AKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-DVVVVGFDATDDA--VKAVNDGRMAATVAQKP 273
Cdd:cd01391 165 ADWNAgEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLVgDVSVIGSDGWADRdeVGYEVEANGLTTIKQQK 244
|
250 260
....*....|....*....|
gi 446681634 274 ELIGEKAMQTAKEITQGKKV 293
Cdd:cd01391 245 MGFGITAIKAMADGSQNMHE 264
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
41-304 |
6.85e-18 |
|
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: 81.45 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVInpTDSDAVASAVSAANAANV 120
Cdd:cd19975 2 IGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIF--ASGTLTEENKQLLKNMNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGKVVShIASNNIeggQMASDYIRELVGEGA-NVAELEGIPGS-SAARERGKGFHN-VADKSLKVVAK-- 195
Cdd:cd19975 80 PVVLVSTESEDPDIPS-VKIDDY---QAAYDATNYLIKKGHrKIAMISGPLDDpNAGYPRYEGYKKaLKDAGLPIKENli 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 196 QAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG---KTDVVVVGFDATDDAvkavndgRMA----AT 268
Cdd:cd19975 156 VEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGirvPEDISVIGFDNTEIA-------EMSipplTT 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 446681634 269 VAQKPELIGEKAMQTAKEITQG-KKVDKSIPIELELI 304
Cdd:cd19975 229 VSQPFYEMGKKAVELLLDLIKNeKKEEKSIVLPHQII 265
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
40-277 |
6.87e-18 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380620 [Multi-domain] Cd Length: 272 Bit Score: 81.55 E-value: 6.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAekkaKDSGiELIAVDAQ------NDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVS 113
Cdd:cd19965 1 KFVFVTHVTTNPFFQPVKKGM----DDAC-ELLGAECQftgpqtFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 114 AANAANVPVIT--VDRVANSGKVVSHIASNNIEGGQMASDYIRELVG-EGANVAELEGIPGSSAARERGKGFHNVADKSL 190
Cdd:cd19965 76 RALDAGIPVVAfnVDAPGGENARLAFVGQDLYPAGYVLGKRIAEKFKpGGGHVLLGISTPGQSALEQRLDGIKQALKEYG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 191 KVVAKQAAD--FDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTD-VVVVGFDATDDAVKAVNDGRMAA 267
Cdd:cd19965 156 RGITYDVIDtgTDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGkVLVGGFDLVPEVLQGIKAGYIDF 235
|
250
....*....|
gi 446681634 268 TVAQKPELIG 277
Cdd:cd19965 236 TIDQQPYLQG 245
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
40-291 |
1.86e-17 |
|
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: 80.75 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAV-DAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAA 118
Cdd:cd06302 1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 119 NVPVITVDRVANSG--KVVSHIASNNIEGGQMAsDYIRELVGEGANVAELEGIPGSS-------AARERGKGFHNVadks 189
Cdd:cd06302 81 GIKVITWDSDAPPSarDYFVNQADDEGLGEALV-DSLAKEIGGKGKVAILSGSLTATnlnawikAMKEYLKSKYPD---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 190 LKVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTD-VVVVGFDATDDAVKAVNDGRMAAT 268
Cdd:cd06302 156 IELVDTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGkVAVTGIGLPNTARPYLKDGSVKEG 235
|
250 260
....*....|....*....|...
gi 446681634 269 VAQKPELIGEKAMQTAKEITQGK 291
Cdd:cd06302 236 VLWDPAKLGYLTVYAAYQLLKGK 258
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
31-293 |
2.04e-17 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 81.33 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 31 SDKGRNKTIKVGFSVSTL-------NNPFFVtlkkgaeKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPT 103
Cdd:PRK10355 18 SVAAHAKEVKIGMAIDDLrlerwqkDRDIFV-------KKAESLGAKVFVQSANGNEETQMSQIENMINRGVDVLVIIPY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 104 DSDAVASAVSAANAANVPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELVGEGaNVAELEGIPGSSAARERGKGFH 183
Cdd:PRK10355 91 NGQVLSNVIKEAKQEGIKVLAYDRMINNADIDFYISFDNEKVGELQAKALVDKVPQG-NYFLMGGSPVDNNAKLFRAGQM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 184 NV-----ADKSLKVVAKQAAD-FDRAKGLSVMENILQANSN-IKAVFAHNDEMALGALEALKS---AGKtdVVVVGFDAT 253
Cdd:PRK10355 170 KVlkpyiDSGKIKVVGDQWVDgWLPENALKIMENALTANNNkIDAVVASNDATAGGAIQALSAqglSGK--VAISGQDAD 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446681634 254 DDAVKAVNDGRMAATVAQKPELIGEKAMQTAKEITQGKKV 293
Cdd:PRK10355 248 LAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEP 287
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
41-307 |
2.19e-17 |
|
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: 80.01 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTdsDAVASAVSAANAANV 120
Cdd:cd06299 2 IGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPT--GENSEGLQALIAQGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGKVVSHIASNNIEGGQMASDYireLVGEG-ANVAELEGIPGSSAARERGKGF------HNVADKSLKVV 193
Cdd:cd06299 80 PVVFVDREVEGLGGVPVVTSDNRPGAREAVEY---LVSLGhRRIGYISGPLSTSTGRERLAAFraaltaAGIPIDEELVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 194 AKqaaDFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG---KTDVVVVGFDatDDAVKAVNDGRMAAtVA 270
Cdd:cd06299 157 FG---DFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGlriGDDVSLISFD--DVPWFELLSPPLTV-IA 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 446681634 271 QKPELIGEKAMQTAKEITQGKKVDKSIPIELELIKKN 307
Cdd:cd06299 231 QPVERIGRRAVELLLALIENGGRATSIRVPTELIPRE 267
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
49-284 |
3.09e-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: 79.97 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 49 NNPFFVTLKKGAEKKAKDSGIEL-IAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVdr 127
Cdd:cd06312 11 SDPFWSVVKKGAKDAAKDLGVTVqYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAI-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 128 vaNSGKVVS--------HIASNNIEGGQMASDYIRELVGEGANVAELEgiPGSSAARERGKGFHNVADKSLKVVAKQAAD 199
Cdd:cd06312 89 --NSGDDRSkerlgaltYVGQDEYLAGQAAGERALEAGPKNALCVNHE--PGNPGLEARCKGFADAFKGAGILVELLDVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 200 FDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTDVVVVG-FDATDDAVKAVNDGRMAATVAQKPELIGE 278
Cdd:cd06312 165 GDPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKVKIGtFDLSPETLEAIKDGKILFAIDQQPYLQGY 244
|
....*.
gi 446681634 279 KAMQTA 284
Cdd:cd06312 245 LAVVFL 250
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
59-304 |
1.09e-16 |
|
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of LacI 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: 380488 [Multi-domain] Cd Length: 265 Bit Score: 78.01 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 59 GAEKKAKDSG--IELIAVDAQNDAAKQTNdVEDLIQKGVD-VVVINPTDSDAVASAVSAANAanvPVITVDrvANSGKVV 135
Cdd:cd01574 20 GIERAARERGysVSIATVDEDDPASVREA-LDRLLSQRVDgIIVIAPDEAVLEALRRLPPGL---PVVIVG--SGPSPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 136 SHIASNNIEGGQMASDYireLVGEGA-NVAELEGIPGSSAARERGKGFHN-VADKSLKVVAKQAADFDRAKGLSVMENIL 213
Cdd:cd01574 94 PTVSIDQEEGARLATRH---LLELGHrRIAHIAGPLDWVDARARLRGWREaLEEAGLPPPPVVEGDWSAASGYRAGRRLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 214 qANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDatddavkavnDGRMAA-------TVAQKPELIGEKAMQT 283
Cdd:cd01574 171 -DDGPVTAVFAANDQMALGALRALHERGLRvpeDVSVVGFD----------DIPEAAyfvppltTVRQDFAELGRRAVEL 239
|
250 260
....*....|....*....|..
gi 446681634 284 AKEITQGKK-VDKSIPIELELI 304
Cdd:cd01574 240 LLALIEGPApPPESVLLPPELV 261
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
38-306 |
4.92e-16 |
|
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: 76.78 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 38 TIKVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINpTDSDAVASAVSAANA 117
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIIT-TPAPSGDDITAKAEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 118 ANVPVITVDRVANSGKVVSHIASNNIEGGQMASDYIRELvGEGANVAELEGIPGSSAARERGKGFHN---VADKSLKVVA 194
Cdd:pfam00532 80 YGIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAE-GHKRPIAVMAGPASALTARERVQGFMAalaAAGREVKIYH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG----KTDVV-----VVGFDATDDAVKAVNDGRM 265
Cdd:pfam00532 159 VATGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrvkiPDIVGiginsVVGFDGLSKAQDTGLYLSP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446681634 266 AATVAQKPELIGEKA----MQtakEITQGKKVDKSIPIELELIKK 306
Cdd:pfam00532 239 LTVIQLPRQLLGIKAsdmvYQ---WIPKFREHPRVLLIPRDFFKE 280
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
41-301 |
1.75e-15 |
|
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: 75.01 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAnv 120
Cdd:cd06296 2 IDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGKVVSHIASNNIEGGQMASDYireLVGEG-ANVAELEGIPGSSAARERGKGF------HNVADKSLKVV 193
Cdd:cd06296 80 PFVLIDPVGEPDPDLPSVGATNWAGGRLATEH---LLDLGhRRIAVITGPPRSVSGRARLAGYraalaeAGIAVDPDLVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 194 AkqaADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG---KTDVVVVGFDATDDAvkavndGRMA---A 267
Cdd:cd06296 157 E---GDFTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGlrvPDDLSVIGFDDTPPA------RWTSpplT 227
|
250 260 270
....*....|....*....|....*....|....
gi 446681634 268 TVAQKPELIGEKAMQTAKEITQGKKVDkSIPIEL 301
Cdd:cd06296 228 TVHQPLREMGAVAVRLLLRLLEGGPPD-ARRIEL 260
|
|
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
40-291 |
1.89e-15 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 75.54 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDS-GIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAA 118
Cdd:PRK15395 26 RIGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAPTVIEKARGQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 119 NVPVITVDRVANSGKVVSH-----IASNNIEGGQMASDYIR---------ELVGEGA-NVAELEGIPGSSAARERGK-GF 182
Cdd:PRK15395 106 DVPVVFFNKEPSRKALDSYdkayyVGTDSKESGIIQGDLIAkhwkanpawDLNKDGKiQYVLLKGEPGHPDAEARTTyVI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 183 HNVADKSLKV--VAKQAADFDRAKGLSVMENILQ-ANSN-IKAVFAHNDEMALGALEALKSAGKTDVVVVGFDATDDAVK 258
Cdd:PRK15395 186 KELNDKGIKTeqLQLDTAMWDTAQAKDKMDAWLSgPNANkIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALA 265
|
250 260 270
....*....|....*....|....*....|...
gi 446681634 259 AVNDGRMAATVAQKPELIGEKAMQTAKEITQGK 291
Cdd:PRK15395 266 LVKSGAMAGTVLNDANNQAKATFDLAKNLADGK 298
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
40-306 |
3.21e-15 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380652 [Multi-domain] Cd Length: 305 Bit Score: 74.63 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAE---KKAKDSGI--ELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSA 114
Cdd:cd19997 1 VIALSNSYAGNTWRQQMVDAFEeaaKKAKADGLiaDYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 115 ANAANVPVITVDRVANSGKVvsHIASNNIEG-GQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADK--SLK 191
Cdd:cd19997 81 ACDAGIKVVVFDSGVTEPCA--YILNNDFEDyGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKKypDLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 192 VVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEmALGALEALKSAGKtDVVVVGFDATDDAVKAVNDGRMAA---T 268
Cdd:cd19997 159 VVAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGD-GYGAAQAFEAAGR-PLPIIIGGNRGEFLKWWQEEYAKNgyeT 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 446681634 269 VAQ-KPELIGEKAMQTAKEITQGKKVDKSIPIELELIKK 306
Cdd:cd19997 237 VSVsTDPGQGSAAFWVALDILNGKDVPKEMILPVVTITE 275
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
40-293 |
3.75e-15 |
|
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: 74.25 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAAN 119
Cdd:cd01540 1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRV---ANSGKVVSH--IASNNI--EGGQMASDYIREL-VGEGANVA-------ELegipgsSAARERGKGFHN 184
Cdd:cd01540 81 IPVIAVDDQlvdADPMKIVPFvgIDAYKIgeAVGEWLAKEMKKRgWDDVKEVGvlaitmdTL------SVCVDRTDGAKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 185 V-------ADKSLKVVAKQAadfDRAKGLSVMENILQANSNIK--AVFAHNDEMALGALEALKSAG--KTDVVVVGFDAT 253
Cdd:cd01540 155 AlkaagfpEDQIFQAPYKGT---DTEGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAGfdAEDIIGVGIGGY 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446681634 254 D--DAVKAVNDGRMAATVAQKPELIGEKAMQT-AKEITQGKKV 293
Cdd:cd01540 232 LaaDEEFKKQPTGFKASLYISPDKHGYIAAEElYNWITDGKPP 274
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
36-304 |
5.15e-15 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 74.38 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 36 NKTIKVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINpTDSDAVASAVSAA 115
Cdd:PRK10703 57 NHTKSIGLLATSSEAPYFAEIIEAVEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVM-CSEYPEPLLAMLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 116 NAANVPVITVDRVANSGKVVSHIASNNIEGGQMASDYireLVGEG-ANVAELEGIPGSSAARERGKGF-HNVADKSLKVV 193
Cdd:PRK10703 136 EYRHIPMVVMDWGEAKADFTDAIIDNAFEGGYLAGRY---LIERGhRDIGVIPGPLERNTGAGRLAGFmKAMEEANIKVP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 194 AK--QAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG---KTDVVVVGFDatddavkAVNDGRMAA- 267
Cdd:PRK10703 213 EEwiVQGDFEPESGYEAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGlrvPQDISVIGYD-------NVRNARYFTp 285
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446681634 268 ---TVAQKPELIGEKAMQTAKE-ITQGKKVDKSIPIELELI 304
Cdd:PRK10703 286 altTIHQPKDRLGETAFNMLLDrIVNKREEPQTIEVHPRLV 326
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
51-282 |
8.04e-15 |
|
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: 72.97 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 51 PFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVD-VVVINPTDSDAVASAVSAANaanvPVITVDRVA 129
Cdd:cd06288 13 PFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDgIIYASMHHREVTLPPELTDI----PLVLLNCFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 130 NSGKVVSHIAsNNIEGGQMAsdyIRELVGEGA-NVAELEGIPGSSAARERGKGF------HNVADKSLKVVAkqaADFDR 202
Cdd:cd06288 89 DDPSLPSVVP-DDEQGGYLA---TRHLIEAGHrRIAFIGGPEDSLATRLRLAGYraalaeAGIPYDPSLVVH---GDWGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 203 AKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGK---TDVVVVGFDatddavkavnDGRMAA-------TVAQK 272
Cdd:cd06288 162 ESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLrvpEDLSVVGFD----------NQELAAylrppltTVALP 231
|
250
....*....|
gi 446681634 273 PELIGEKAMQ 282
Cdd:cd06288 232 YYEMGRRAAE 241
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
50-292 |
2.24e-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: 71.92 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 50 NPFFVTLKKGAEKKAKDSGIELI---AVDAqnDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVD 126
Cdd:cd20003 11 VPYFTAAGQGAQEAAKELGVDVTydgPTEA--SVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVTWD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 127 rvANSGKVVSHIASNNIEGGQMAS---DYIRELVGEGANVAELEGIPGS-------SAARERGKGFHnvadKSLKVVAKQ 196
Cdd:cd20003 89 --SDVNPDARDFFVNQATPEGIGKtlvDMVAEQTGEKGKVAIVTSSPTAtnqnawiKAMKAYIAEKY----PDMKIVTTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 197 AADFDRAKGLSVMENILQANSNIKAVFAHnDEMAL-GALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAATVAQKPE 274
Cdd:cd20003 163 YGQEDPAKSLQVAENILKAYPDLKAIIAP-DSVALpGAAEAVEQLGRTgKVAVTGLSTPNVMRPYVKDGTVKSVVLWDVV 241
|
250
....*....|....*...
gi 446681634 275 LIGEKAMQTAKEITQGKK 292
Cdd:cd20003 242 DLGYLAVYVARALADGTL 259
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
51-277 |
2.51e-14 |
|
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: 71.59 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 51 PFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVD--VVVINPtDSDAVASAVSAANAANVPVITVD-- 126
Cdd:cd19966 13 PFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDgiAIMGHP-GDGAYTPLIEAAKKAGIIVTSFNtd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 127 --RVANSGKVVSHIASNNIEGGQMASDYI--RELVGEGANVAELEGIPGSSAARERGKGFHNVADK---SLKVVAKQAAD 199
Cdd:cd19966 92 lpKLEYGDCGLGYVGADLYAAGYTLAKELvkRGGLKTGDRVFVPGLLPGQPYRVLRTKGVIDALKEagiKVDYLEISLEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 200 FDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT--DVVVVGFDATDDAVKAVNDGRMAATVAQKPELIG 277
Cdd:cd19966 172 NKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKKpgEIPVAGFDLSPATVQAIKSGYVNATIDQQPYLQG 251
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
137-269 |
3.84e-14 |
|
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: 71.63 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 137 HIASNNIEGGQMASDYIRELVGEGANVAELEGIPGSsAARERGKGF-HNVA-DKSLKVVAKQAADFDRAKGLSVMENILQ 214
Cdd:cd06303 136 YVGFDHAEGSRMLAKHFIKIFPEEGKYAILYLTEGY-VSDQRGDTFiDEVArHSNLELVSAYYTDFDRESAREAARALLA 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446681634 215 ANSNIKAVFAHNDEMALGALEALKSAGK-TDVVVVGFDATDDAVKAVNDGRMAATV 269
Cdd:cd06303 215 RHPDLDFIYACSTDIALGAIDALQELGReTDIMINGWGGGSAELDALQKGGLDVTV 270
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
41-283 |
5.13e-13 |
|
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: 67.58 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTdsDAVASAVSAANAANV 120
Cdd:cd06283 2 IGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPT--GNNNDAYLELAQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRvANSGKVVSHIASNNIeggQMASDYIRELVGEG-ANVAEL-EGIPGSSAARERGKGFHNVADKSLKvvAKQAA 198
Cdd:cd06283 80 PVVLVDR-QIEPLNWDTVVTDNY---DATYEATEHLKEQGyERIVFVtEPIKGISTRRERLQGFLDALARYNI--EGDVY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 199 DFDRAKGLSVMENILQ----ANSNIKAVFAHNDEMALGALEALKSAGK---TDVVVVGFDATDDAvKAVNDGrmAATVAQ 271
Cdd:cd06283 154 VIEIEDTEDLQQALAAflsqHDGGKTAIFAANGVVLLRVLRALKALGIripDDVGLCGFDDWDWA-DLIGPG--ITTIRQ 230
|
250
....*....|..
gi 446681634 272 KPELIGEKAMQT 283
Cdd:cd06283 231 PTYEIGKAAAEI 242
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
121-304 |
3.65e-12 |
|
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum 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: 380502 [Multi-domain] Cd Length: 284 Bit Score: 65.31 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGkvVSHIASNNIEGGQMASDYIREL-----------VGEGANVAELEGIPGSSA----ARERGKGF--- 182
Cdd:cd06279 81 PLVVVDGPAPPG--IPSVGIDDRAAARAAARHLLDLghrriailslrLDRGRERGPVSAERLAAAtnsvARERLAGYrda 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 183 ---HNVADKSLKVVakQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDDA 256
Cdd:cd06279 159 leeAGLDLDDVPVV--EAPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRvpeDLSVTGFDDIPEA 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446681634 257 VKAvndGRMAATVAQKPELIGEKAMQTAKEITQGkKVDKSIPIELELI 304
Cdd:cd06279 237 AAA---DPGLTTVRQPAVEKGRAAARLLLGLLPG-APPRPVILPTELV 280
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
41-304 |
8.85e-12 |
|
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to 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 I 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: 380515 [Multi-domain] Cd Length: 273 Bit Score: 64.21 E-value: 8.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLN----NPFFVTLKKGAEKKAKDSGIELIaVDAQNDAAKQTNDVEDLIQ-KGVDVVVINPTDSDAVASAVSAA 115
Cdd:cd06292 2 IGYVVPELPggfsDPFFDEFLAALGHAAAARGYDVL-LFTASGDEDEIDYYRDLVRsRRVDGFVLASTRHDDPRVRYLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 116 NAAnvPVITVDRVANSGKVvSHIASNNIEGGQMAsdyIRELVGEG-ANVAELEGIPGSSAARERGKGFHNVADKSLKVVA 194
Cdd:cd06292 81 AGV--PFVAFGRANPDLDF-PWVDVDGAAGMRQA---VRHLIALGhRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQA---ADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDatddavkavnDGRMAA- 267
Cdd:cd06292 155 PGLvveGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRvgrDVSVVGFD----------DSPLAAf 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446681634 268 ------TVAQKPELIGEKAMQTAKEITQGKKV-DKSIPIELELI 304
Cdd:cd06292 225 thppltTVRQPIDEIGRAVVDLLLAAIEGNPSePREILLQPELV 268
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
40-304 |
1.31e-11 |
|
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: 63.73 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDS---GIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAAN 116
Cdd:cd06307 1 RFGFLLPSPENPFYELLRRAIEAAAAALrdrRVRLRIHFVDSLDPEALAAALRRLAAGCDGVALVAPDHPLVRAAIDELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 117 AANVPVITVDRVANSGKVVSHIASNNIEGGQMASDYI-RELVGEGANVAELEGIPGSSAARERGKGFHNVADKS---LKV 192
Cdd:cd06307 81 ARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMgRFLGRRPGKVLVILGSHRFRGHEEREAGFRSVLRERfpdLTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 193 VAKQAADFDRAKGLSVMENILQANSNIKAVF---AHNDemalGALEALKSAGKT-DVVVVGFDATDDAVKAVNDGRMAAT 268
Cdd:cd06307 161 LEVLEGLDDDELAYELLRELLARHPDLVGIYnagGGNE----GIARALREAGRArRVVFIGHELTPETRRLLRDGTIDAV 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 446681634 269 VAQKPELIGEKAMQTAKEITQGKKVD-KSIPIELELI 304
Cdd:cd06307 237 IDQDPELQARRAIEVLLAHLGGKGPApPQPPIPIEII 273
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
121-306 |
1.59e-11 |
|
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: 63.25 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDrvANSgKVVSHIASNNIEGGQMASDYIRELvGEG---ANVAELEGIPGSSAARERGKGFHNVADKSLKVVA--- 194
Cdd:cd06297 80 PVVLID--ANS-MGYDCVYVDNVKGGFMATEYLAGL-GEReyvFFGIEEDTVFTETVFREREQGFLEALNKAGRPISssr 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 195 KQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFdatDDAVKAVNDGrmAATVAQ 271
Cdd:cd06297 156 MFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRvgeDVAVIGF---DGQPWAASPG--LTTVRQ 230
|
170 180 190
....*....|....*....|....*....|....*.
gi 446681634 272 KPELIGEKAMQTAKEITQGKKVD-KSIPIELELIKK 306
Cdd:cd06297 231 PVEEMGEAAAKLLLKRLNEYGGPpRSLKFEPELIVR 266
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
48-305 |
1.63e-11 |
|
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR 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. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. 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 structurally homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380486 [Multi-domain] Cd Length: 269 Bit Score: 63.31 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 48 LNNPFFVTLKKGAEKKAKDSGIELIAVdaqndaaKQTNDVEDLIQKGVD-VVVINPTDSDAVASAVSAANaanvPVITVD 126
Cdd:cd01544 14 LEDPYYLSIRLGIEKEAKKLGYEIKTI-------FRDDEDLESLLEKVDgIIAIGKFSKEEIEKLKKLNP----NIVFVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 127 RVANSGKVVShIASNNIEGGQMASDYIREL-------VGeGANVAELEGIPGSSaarERGKGFHNVAdKSLKVVAKQ--- 196
Cdd:cd01544 83 SNPDPDGFDS-VVPDFEQAVRQALDYLIELghrrigfIG-GKEYTSDDGEEIED---PRLRAFREYM-KEKGLYNEEyiy 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 197 AADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDdavkavndgrMAA------ 267
Cdd:cd01544 157 IGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKvpeDISIISFNDIE----------VAKyvtppl 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446681634 268 -TVAQKPELIGEKAMQTAKE-ITQGKKVDKSIPIELELIK 305
Cdd:cd01544 227 tTVHIPTEEMGRTAVRLLLErINGGRTIPKKVLLPTKLIE 266
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
138-251 |
1.77e-11 |
|
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators; This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. 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: 380518 [Multi-domain] Cd Length: 273 Bit Score: 63.42 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 138 IASNNIEGGQMASDYireLVGEGA-NVAELeGIPGSSAARERGKGF---HNVADKSLKVVAKQAADFDRAKGLSVMENIL 213
Cdd:cd06295 104 VGSDNVKGGALATEH---LIEIGRrRIAFL-GDPPHPEVADRLQGYrdaLAEAGLEADPSLLLSCDFTEESGYAAMRALL 179
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446681634 214 QANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFD 251
Cdd:cd06295 180 DSGTAFDAIFAASDLIAMGAIRALRERGISvpgDVAVVGYD 220
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
41-307 |
1.30e-10 |
|
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR 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: 380483 [Multi-domain] Cd Length: 274 Bit Score: 60.65 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVS---AANA 117
Cdd:cd01541 2 IGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSALPNPNLDlyeELQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 118 ANVPVITVDRVANSGKVvSHIASNNIEGGQMASDYireLVGEG-ANVAeleGI------PGssaaRERGKGF------HN 184
Cdd:cd01541 82 KGIPVVFINSYYPELDA-PSVSLDDEKGGYLATKH---LIDLGhRRIA---GIfksddlQG----VERYQGFikalreAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 185 VADKSLKVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFdatDDAVKAVN 261
Cdd:cd01541 151 LPIDDDRILWYSTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRvpeDLSVVGF---DDSYLASL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446681634 262 DGRMAATVAQKPELIGEKAMQTAKEITQGKKVDKSIPIELELIKKN 307
Cdd:cd01541 228 SEPPLTSVVHPKEELGRKAAELLLRMIEEGRKPESVIFPPELIERE 273
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
40-291 |
2.04e-10 |
|
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380655 Cd Length: 298 Bit Score: 60.35 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVD-AQNDAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAA 118
Cdd:cd20000 1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGpTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 119 NVPVITVDRVANSGKVVSHIASNNIEG-GQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS----LKVV 193
Cdd:cd20000 81 GIKVVTFDSDVAPEARDLFVNQADADGiGRAQVDMMAELIGGEGEFAILSATPTATNQNAWIDAMKKELASPeyagMKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 194 AKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTD-VVVVGFDATDDAVKAVNDGRMAATVAQK 272
Cdd:cd20000 161 KVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGkVKVTGLGLPSEMAKYVKDGTVPAFALWN 240
|
250
....*....|....*....
gi 446681634 273 PELIGEKAMQTAKEITQGK 291
Cdd:cd20000 241 PIDLGYLAAYAAAALAQGE 259
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
167-294 |
2.26e-10 |
|
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 58.12 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 167 EGIPGSSAARERGKGF-HNVADKSLKVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT-- 243
Cdd:pfam13377 16 EGDRDDPYSDLRERGFrEAARELGLDVEPTLYAGDDEAEAAAARERLRWLGALPTAVFVANDEVALGVLQALREAGLRvp 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446681634 244 -DVVVVGFDATDDAVKAVndgRMAATVAQKPELIGEKAMQTAKEITQGKKVD 294
Cdd:pfam13377 96 eDLSVIGFDDSPLAALVS---PPLTTVRVDAEELGRAAAELLLDLLNGEPAP 144
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
41-306 |
2.41e-10 |
|
ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to 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. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree.
Pssm-ID: 380509 [Multi-domain] Cd Length: 262 Bit Score: 59.87 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVI----NPTDSDAVASAVSaan 116
Cdd:cd06286 2 IGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIItsreNDWEVIEPYAKYG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 117 aanvPVITVDRVANsgKVVSHIASNNIEGGQMASDYIRElvgEGA-NVAELEGIP--GSSAARERGKGFHNVADKSLKVV 193
Cdd:cd06286 79 ----PIVLCEETDS--PDIPSVYIDRYEAYLEALEYLKE---KGHrKIGYCLGRPesSSASTQARLKAYQDVLGEHGLSL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 194 AKQ-----AADFDraKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGK---TDVVVVGFDATDDAvKAVNdgrm 265
Cdd:cd06286 150 REEwiftnCHTIE--DGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIrvpEDLAVIGFDNQPIS-ELLN---- 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446681634 266 AATVAQKPELIGEKAMQTAKEITQGKKVDKsIPIELELIKK 306
Cdd:cd06286 223 LTTIDQPLEEMGKEAFELLLSQLESKEPTK-KELPSKLIER 262
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
62-307 |
4.40e-10 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 59.62 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 62 KKAKDSGIE-LIAVDAQNDAAKQTNDVEDLIQKGVDVVVIN-PtdSDAVASAVSAANAANVPVITVDRVANSgkVVSHIA 139
Cdd:PRK09526 87 SRADQLGYSvVISMVERSGVEACQAAVNELLAQRVSGVIINvP--LEDADAEKIVADCADVPCLFLDVSPQS--PVNSVS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 140 SNNIEGGQMASDYIRELvgEGANVAELEGIPGSSAARERGKGFHNV-ADKSLKVVAKQAADFDRAKGLSVMENILQANSN 218
Cdd:PRK09526 163 FDPEDGTRLGVEHLVEL--GHQRIALLAGPESSVSARLRLAGWLEYlTDYQLQPIAVREGDWSAMSGYQQTLQMLREGPV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 219 IKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDDAvkavndgrmA------ATVAQKPELIGEKAMQTAKEITQ 289
Cdd:PRK09526 241 PSAILVANDQMALGVLRALHESGLRvpgQISVIGYDDTEDS---------SyfipplTTIKQDFRLLGKEAVDRLLALSQ 311
|
250
....*....|....*...
gi 446681634 290 GKKVDKSIPIELELIKKN 307
Cdd:PRK09526 312 GQAVKGSQLLPTSLVVRK 329
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
49-304 |
6.88e-10 |
|
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-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: 380487 [Multi-domain] Cd Length: 270 Bit Score: 58.72 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 49 NNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQK-GVDVVVINPtdsdavasavsaanaanvPV----- 122
Cdd:cd01545 10 SASYVSALQVGALRACREAGYHLVVEPCDSDDEDLADRLRRFLSRsRPDGVILTP------------------PLsddpa 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 123 ---------ITVDRVA--NSGKVVSHIASNNIEGGQMASDYireLVGEG-ANVAELEGIPGSSAARERGKGF------HN 184
Cdd:cd01545 72 lldaldelgIPYVRIApgTDDDRSPSVRIDDRAAAREMTRH---LIALGhRRIGFIAGPPDHGASAERLEGFrdalaeAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 185 VADKSLKVVAkqaADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDatddavkavn 261
Cdd:cd01545 149 LPLDPDLVVQ---GDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRvpdDLSVAGFD---------- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446681634 262 DGRMAA-------TVAQKPELIGEKAMQT-AKEITQGKKVDKSIPIELELI 304
Cdd:cd01545 216 DSPIARlvwppltTVRQPIAEMARRAVELlIAAIRGAPAGPERETLPHELV 266
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
40-254 |
2.00e-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: 380504 [Multi-domain] Cd Length: 270 Bit Score: 57.25 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 40 KVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPtDSDAVASAVSAANAAN 119
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTP-GDEDDPELAAALARLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDR-VANSGKVVShiaSNNIEGGQMASDYIRELvgeG-ANVAELEGIPGSSAARERGKGF------HNVADKSLK 191
Cdd:cd06281 80 IPVVLIDRdLPGDIDSVL---VDHRSGVRQATEYLLSL---GhRRIALLTGGPDIRPGRERIAGFkaafaaAGLPPDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446681634 192 VvakQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATD 254
Cdd:cd06281 154 V---RLGSFSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRipgDLSVVSIGDSD 216
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
38-251 |
1.46e-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: 380500 [Multi-domain] Cd Length: 275 Bit Score: 54.55 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 38 TIKVGFSVSTLNNPFFVTLKKGAEKKAKDSGIELI--AVDAQNDAAKQTNDVEDLIQKGVDVVVINptdsdAVASAVSAA 115
Cdd:cd06277 6 IYSDNGDGVVNETPFFSELIDGIEREARKYGYNLLisSVDIGDDFDEILKELTDDQSSGIILLGTE-----LEEKQIKLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 116 NAANVPVITVDRvANSGKVVSHIASNNIEGGQMASDYIRELvgeG-ANVAELEGIPGSSAARERGKGFHN-VADKSLKVV 193
Cdd:cd06277 81 QDVSIPVVVVDN-YFEDLNFDCVVIDNEDGAYEAVKYLVEL---GhTRIGYLASSYRIKNFEERRRGFRKaMRELGLSED 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446681634 194 AKQAADFDraKGLSVMENILQANSNIK-----AVFAHNDEMALGALEALKSAG---KTDVVVVGFD 251
Cdd:cd06277 157 PEPEFVVS--VGPEGAYKDMKALLDTGpklptAFFAENDIIALGCIKALQEAGirvPEDVSVIGFD 220
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
51-292 |
3.65e-08 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380657 Cd Length: 295 Bit Score: 53.86 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 51 PFFVTLKKGAEKKAKDSGIELIAVDAQN-DAAKQTNDVEDLIQKGVDVVVINPTDSDAVASAVSAANAANVPVITVDRVA 129
Cdd:cd20002 12 PWFNRMEQGVKKAGKEFGVNAYQVGPADaDPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVITHESPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 130 NSGKVVSHIASNNIEGGQMASDYIRELVGEGANVAELEG---IPGssaarergkgfHNV-ADKSLKVVAKQAADF----- 200
Cdd:cd20002 92 QKGADWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGsltVPL-----------HNLwADAAVEYQKEKYPNMkqvtd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 201 ------DRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG-KTDVVVVGFDATDDAVKAVNDGRMAATVAQKP 273
Cdd:cd20002 161 ripggeDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGlKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDP 240
|
250
....*....|....*....
gi 446681634 274 ELIGEKAMQTAKEITQGKK 292
Cdd:cd20002 241 ADAGYAMVYIAKMLLDGKR 259
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
41-304 |
4.22e-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: 380497 [Multi-domain] Cd Length: 268 Bit Score: 53.28 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVInpTDSDAVASAVSAANAANV 120
Cdd:cd06273 2 IGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLIL--VGSDHDPELFELLEQRQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGKVVShIASNNIEGGQMASDYireLVGEG-ANVAELEGIPGSSA-ARERGKGFHNVADK---SLKVVAK 195
Cdd:cd06273 80 PYVLTWSYDEDSPHPS-IGFDNRAAAARAAQH---LLDLGhRRIAVISGPTAGNDrARARLAGIRDALAErglELPEERV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 196 QAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDdavkavndgrMAA----- 267
Cdd:cd06273 156 VEAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISvpeDLSITGFDDLE----------LAAhlspp 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 446681634 268 --TVAQKPELIGEKAMQTAKEITQGKKVDKSIPIELELI 304
Cdd:cd06273 226 ltTVRVPAREIGELAARYLLALLEGGPPPKSVELETELI 264
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
41-238 |
6.64e-08 |
|
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: 52.59 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPTdsDAVASAVSAANAANV 120
Cdd:cd06274 2 IGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPS--TPPDDIYYLCQAAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGKVVShIASNNIEGgqmASDYIRELVGEGAN-VAELEGIPGSSAARERGKGFHNV---ADKSLKVVAKQ 196
Cdd:cd06274 80 PVVFLDRPFSGSDAPS-VVSDNRAG---ARALTEKLLAAGPGeIYFLGGRPELPSTAERIRGFRAAlaeAGITEGDDWIL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446681634 197 AADFDRAKGLSVMENILQANSNI-KAVFAHNDEMALGALEALK 238
Cdd:cd06274 156 AEGYDRESGYQLMAELLARLGGLpQALFTSSLTLLEGVLRFLR 198
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
198-304 |
9.75e-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: 52.11 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDRAKGLSVMENILQaNSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDDAvKAVNDGrmAATVAQKPE 274
Cdd:cd01542 154 TDFSMESGYEAAKELLK-ENKPDAIICATDNIALGAIKALRELGIKipeDISVAGFGGYDLS-EFVSPS--LTTVKFDYE 229
|
90 100 110
....*....|....*....|....*....|
gi 446681634 275 LIGEKAMQTAKEITQGKKVDKSIPIELELI 304
Cdd:cd01542 230 EAGEKAAELLLDMIEGEKVPKKQKLPYELI 259
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
41-243 |
3.29e-07 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 50.86 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINPtDSDAVASAVSAANAANV 120
Cdd:PRK10014 67 IGLIVRDLSAPFYAELTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAG-AAGSSDDLREMAEEKGI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRvANSGKVVSHIASNNIEGGQMASDYireLVGEG-ANVAELEGIPGSSAARERGKGF------HNVADKSLKVV 193
Cdd:PRK10014 146 PVVFASR-ASYLDDVDTVRPDNMQAAQLLTEH---LIRNGhQRIAWLGGQSSSLTRAERVGGYcatllkFGLPFHSEWVL 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446681634 194 -----AKQAADfdrakglsVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT 243
Cdd:PRK10014 222 ectssQKQAAE--------AITALLRHNPTISAVVCYNETIAMGAWFGLLRAGRQ 268
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
41-282 |
4.06e-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: 380505 [Multi-domain] Cd Length: 267 Bit Score: 50.36 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINpTDSDAVASAVSAANAANV 120
Cdd:cd06282 2 IGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILT-VGDAQGSEALELLEEEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 121 PVITVDRVANSGKVvshiASNNIEGGQMASDYIRELVGEG-ANVAELEG-IPGSSAARERGKGFHNVA-DKSLKVVAKQA 197
Cdd:cd06282 81 PYVLLFNQTENSSH----PFVSVDNRLASYDVAEYLIALGhRRIAMVAGdFSASDRARLRYQGYRDALkEAGLKPIPIVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 198 ADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFDATDdavkavnDGRMA----ATVA 270
Cdd:cd06282 157 VDFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRvpdDVSVIGFDGIA-------IGELLtptlATVV 229
|
250
....*....|..
gi 446681634 271 QKPELIGEKAMQ 282
Cdd:cd06282 230 QPSRDMGRAAAD 241
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
175-304 |
4.43e-07 |
|
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: 50.19 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 175 ARERGKGFHN-VADKSLKVVAKQAADFDR--AKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVV 248
Cdd:cd01575 132 ARQRLEGFRDaLAEAGLPLPLVLLVELPSsfALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRvpgDIAIA 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446681634 249 GFdatddavkavNDGRMAA-------TVAQKPELIGEKAMQTA-KEITQGKKVDKSIPIELELI 304
Cdd:cd01575 212 GF----------GDLDIAAalppaltTVRVPRYEIGRKAAELLlARLEGEEPEPRVVDLGFELV 265
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
45-293 |
5.13e-07 |
|
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: 50.35 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 45 VSTLNNPFFVTLKKGAEKKAKDSGIELIAVD-AQNDAAKQTNDVEDLIQKGVDVVVINPtdsdavasavsAANAANVPVI 123
Cdd:cd20001 6 VKVTGIAWFDRMETGVEQFAKDTGVNVYQIGpATADAAQQVQIIEDLIAQGVDAICVVP-----------NDPEALEPVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 124 TVDRVANSgKVVSHIASN------------NIEGGQMASDYIRELVGEGANVAELEGIPGSSAARERGKGFHNVADKS-- 189
Cdd:cd20001 75 KKARDAGI-VVITHEASNlknvdydveafdNAAYGAFIMDKLAEAMGGKGKYVTFVGSLTSTSHMEWANAAVAYQKANyp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 190 --LKVVAKQAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKTD-VVVVGFDATDDAVKAVNDGRMA 266
Cdd:cd20001 154 dmLLVTDRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGkIAVVGTGLPSVAGEYLEDGTID 233
|
250 260
....*....|....*....|....*..
gi 446681634 267 ATVAQKPELIGEKAMQTAKEITQGKKV 293
Cdd:cd20001 234 YIQFWDPADAGYAMNALAVMVLEGEKI 260
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
199-304 |
1.42e-06 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 48.84 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 199 DFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAG---KTDVVVVGFDatDDAVKAVNDGRMaATVAQKPEL 275
Cdd:PRK11041 194 DFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGlrvPQDLSIIGFD--DIDLAQYCDPPL-TTVAQPRYE 270
|
90 100 110
....*....|....*....|....*....|
gi 446681634 276 IGEKAMQTAKEITQGKKVDK-SIPIELELI 304
Cdd:PRK11041 271 IGREAMLLLLEQLQGHHVSSgSRLLDCELI 300
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
59-297 |
2.29e-06 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 48.41 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 59 GAEKKAKDSGIELIAVDAQN--DAAKQTNDVEDLIQKGVDVVVINpTDSDAVASAVSAANAANVPVI-TVDRVaNSGKVV 135
Cdd:PRK10936 67 GMVEEAKRLGVDLKVLEAGGyyNLAKQQQQLEQCVAWGADAILLG-AVTPDGLNPDLELQAANIPVIaLVNGI-DSPQVT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 136 SHIASNNIEGGQMASDYIRELVGEG---ANVAELEGIPGSSAARERGKGF-HNVADKSLKVVAKQAADFDRAKGLSVMEN 211
Cdd:PRK10936 145 TRVGVSWYQMGYQAGRYLAQWHPKGskpLNVALLPGPEGAGGSKAVEQGFrAAIAGSDVRIVDIAYGDNDKELQRNLLQE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 212 ILQANSNIK-----AVFAhndEMALGaleALKSAGKTD-VVVVGFDATDDAVKAVNDGRMAATVAQKPELIGEKAMQTAK 285
Cdd:PRK10936 225 LLERHPDIDyiagsAVAA---EAAIG---ELRGRNLTDkIKLVSFYLSHQVYRGLKRGKVLAAPSDQMVLQGRLAIDQAV 298
|
250
....*....|..
gi 446681634 286 EITQGKKVDKSI 297
Cdd:PRK10936 299 RQLEGAPVPGDV 310
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
34-224 |
9.19e-06 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 46.41 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 34 GRNKTIkvGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVDVVVINpTDSDAVASAVS 113
Cdd:PRK11303 59 GRTRSI--GLIIPDLENTSYARIAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVS-TSLPPEHPFYQ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 114 AANAANVPVITVDRVANSGKVVShIASNNIEGGQMASDYIRELvgEGANVAELEGIPGSSAARERGKGFHN-VADKSLKV 192
Cdd:PRK11303 136 RLQNDGLPIIALDRALDREHFTS-VVSDDQDDAEMLAESLLKF--PAESILLLGALPELSVSFEREQGFRQaLKDDPREV 212
|
170 180 190
....*....|....*....|....*....|..
gi 446681634 193 VAKQAADFDRAKGLSVMENILQANSNIKAVFA 224
Cdd:PRK11303 213 HYLYANSFEREAGAQLFEKWLETHPMPDALFT 244
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
201-251 |
3.01e-05 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 45.15 E-value: 3.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446681634 201 DRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFD 251
Cdd:PRK10401 220 DMQGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAiplHLSIIGFD 273
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
196-251 |
3.38e-05 |
|
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member 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 the sugar-binding domain of ABC-type transport systems that contain the type I 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: 380665 [Multi-domain] Cd Length: 269 Bit Score: 44.46 E-value: 3.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446681634 196 QAADFDRAKGLSVMENILQANSNIKAVFAHNDEMALGALEALKSAGKT---DVVVVGFD 251
Cdd:cd20010 159 REGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSpgkDVSVIGHD 217
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
41-253 |
4.21e-04 |
|
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain 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: 380521 [Multi-domain] Cd Length: 268 Bit Score: 41.12 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 41 VGFSVSTLNNPFFVTLKKGAEKKAKDSGIELIAVDAQNDAAKQTNDVEDLIQKGVD-VVVINptdSDAVASAVSAANAAN 119
Cdd:cd06298 2 VGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDgIIFMG---DELTEEIREEFKRSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446681634 120 VPVITVDRVANSGKvvshIASNNIEGGQMASDYIRELVGEG-ANVAELEGIPGSSAARE-RGKGFHN-VADKSLKVVAKQ 196
Cdd:cd06298 79 VPVVLAGTVDSDHE----IPSVNIDYEQAAYDATKSLIDKGhKKIAFVSGPLKEYINNDkKLQGYKRaLEEAGLEFNEPL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446681634 197 --AADFDRAKGLSVMENILqANSNIKAVFAHNDEMALGALEALKSAGK---TDVVVVGFDAT 253
Cdd:cd06298 155 ifEGDYDYDSGYELYEELL-ESGEPDAAIVVRDEIAVGLLNAAQDRGLkvpEDLEIIGFDNT 215
|
|
| |
