|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
22-302 |
8.28e-120 |
|
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: 344.99 E-value: 8.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREPVNVnslPDNQAFVASNEADSGTLETKEVCRLfkeaGKKEANVYVIMGELSNQAAVQRTKDIEEVIATpd 181
Cdd:cd06301 82 GIPLVYVNREPDSK---PKGVAFVGSDDIESGELQMEYLAKL----LGGKGNIAILDGVLGHEAQILRTEGNKDVLAK-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 182 CSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKsVVVGGVDATQDALAAMQAGD 261
Cdd:cd06301 153 YPGMKIVAEQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDD-ILVAGIDATPDALKAMKAGR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 518701315 262 LDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVT 302
Cdd:cd06301 232 LDATVFQDAAGQGETAVDVAVKAAKGEEVESDIWIPFELVT 272
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
22-310 |
3.58e-77 |
|
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: 236.78 E-value: 3.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKEL-NVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREPVNvnslPDNQAFVASNEADSGTLETKEVCRLFKEAGkkeaNVYVIMGELSNQAAVQRTKDIEEVIAT-P 180
Cdd:cd06313 80 GIPLVGVNALIEN----EDLTAYVGSDDVVAGELEGQAVADRLGGKG----NVVILEGPIGQSAQIDRGKGIENVLKKyP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 181 DcsfIKIIDKQTSNWNRDEAQNLMTNWLST-GKKFDGVIANNDESAIGAIQAMKAANidMKSVVVGGVDATQDALAAMQA 259
Cdd:cd06313 152 D---IKVLAEQTANWSRDEAMSLMENWLQAyGDEIDGIIAQNDDMALGALQAVKAAG--RDDIPVVGIDGIEDALQAVKS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 518701315 260 GDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVTPANIDKFL 310
Cdd:cd06313 227 GELIATVLQDAEAQGKGAVEVAVDAVKGEGVEKKYYIPFVLVTKDNVDDYL 277
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
4-306 |
3.11e-74 |
|
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: 230.58 E-value: 3.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 4 LLLGVAFAALISSSAFAA-------KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAAS 76
Cdd:COG1879 10 LALALALAACGSAAAEAAaaaakgkTIGFVVKTLGNPFFVAVRKGAEAAAKEL-GVELIVVDAEGDAAKQISQIEDLIAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 77 GVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNREPVNvnslPDNQAFVASNEADSGTLETKEVCRLFKEAGKkeanVYV 156
Cdd:COG1879 89 GVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDG----SDRVAYVGSDNYAAGRLAAEYLAKALGGKGK----VAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 157 IMGELSNQAAVQRTKDIEEVIAtpDCSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAAN 236
Cdd:COG1879 161 LTGSPGAPAANERTDGFKEALK--EYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 237 IDMKsVVVGGVDATQDALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVTPANI 306
Cdd:COG1879 239 RKGD-VKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
22-300 |
1.59e-72 |
|
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: 224.75 E-value: 1.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKEL-GVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREPvnvNSLPDNQAFVASNEADSGTLETKEVCRLFKeagkKEANVYVIMGELSNQAAVQRTKDIEEVIAtpD 181
Cdd:cd01536 80 GIPVVAVDTDI---DGGGDVVAFVGTDNYEAGKLAGEYLAEALG----GKGKVAILEGPPGSSTAIDRTKGFKEALK--K 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 182 CSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKsVVVGGVDATQDALAAMQAGD 261
Cdd:cd01536 151 YPDIEIVAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGD-IKIVGVDGTPEALKAIKDGE 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 518701315 262 LDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQL 300
Cdd:cd01536 230 LDATVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPVTL 268
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
22-299 |
8.42e-62 |
|
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: 198.19 E-value: 8.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREPV--NVNSLpDNQAFVASNEADSGTLETKEVCRLFKEAGKKEAN-----VYVI-MGELSNQAAVQRTKDI 173
Cdd:cd01539 82 NIPVIFFNREPSreDLKSY-DKAYYVGTDAEESGIMQGEIIADYWKANPEIDKNgdgkiQYVMlKGEPGHQDAIARTKYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 174 EEVIATPDCSfIKIIDKQTSNWNRDEAQNLMTNWLST-GKKFDGVIANNDESAIGAIQAMKAA--NIDM--KSVVVGGVD 248
Cdd:cd01539 161 VKTLNDAGIK-TEQLAEDTANWDRAQAKDKMDAWLSKyGDKIELVIANNDDMALGAIEALKAAgyNTGDgdKYIPVFGVD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518701315 249 ATQDALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGE---------KVEHK-VYVPFQ 299
Cdd:cd01539 240 ATPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKepletgykfLVEGKyVRIPYK 300
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
22-310 |
1.23e-55 |
|
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: 182.03 E-value: 1.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKgMSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAK-KRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREpVNVNSLPDNQAFVASNEADSGTLETKEVCrlfKEAGKKEANVYVIMGELSNQAAVQRTKDIEEVIATPd 181
Cdd:cd06309 80 GIPVILVDRT-IDGEDGSLYVTFIGSDFVEEGRRAAEWLV---KNYKGGKGNVVELQGTAGSSVAIDRSKGFREVIKKH- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 182 cSFIKIIDKQTSNWNRDEAQNLMTNWL-STGKKFDGVIANNDESAIGAIQAMKAANI-DMKSVVVGGVDATQDALAAMQA 259
Cdd:cd06309 155 -PNIKIVASQSGNFTREKGQKVMENLLqAGPGDIDVIYAHNDDMALGAIQALKEAGLkPGKDVLVVGIDGQKDALEAIKA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 518701315 260 GDLDATVfQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVTPANIDKFL 310
Cdd:cd06309 234 GELNATV-ECNPLFGPTAFDTIAKLLAGEKVPKLIIVEERLFDKDNAAEEL 283
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
22-301 |
1.71e-52 |
|
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: 173.12 E-value: 1.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNRepvNVNSlPDNQAFVASNEADSGTLETKEVCRLFKEAGkkeaNVYVIMGELSNQAAVQRTKDIEEVIA-TP 180
Cdd:cd06308 81 GIPVIVLDR---KVSG-DDYTAFIGADNVEIGRQAGEYIAELLNGKG----NVVEIQGLPGSSPAIDRHKGFLEAIAkYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 181 DcsfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDmKSVVVGGVDATQDALAAM-QA 259
Cdd:cd06308 153 G---IKIVASQDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGRE-KEIKIIGVDGLPEAGEKAvKD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518701315 260 GDLDATVFQDAAgqGAGALDAALKLSKGEKVEHKVYVPFQLV 301
Cdd:cd06308 229 GILAATFLYPTG--GKEAIEAALKILNGEKVPKEIVLPTPLI 268
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
22-302 |
2.54e-51 |
|
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: 170.17 E-value: 2.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKEL-GVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNRepvNVNSlPDNQAFVASNEADSGtletKEVCRLFKEAGKKEANVYVIMGELSNQAAVQRTKDIEEVIAtpD 181
Cdd:cd06323 80 GIPVITVDR---SVTG-GKVVSHIASDNVAGG----EMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIA--K 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 182 CSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANidMKSVVVGGVDATQDALAAMQAGD 261
Cdd:cd06323 150 YPKINVVASQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG--RKDVIVVGFDGTPDAVKAVKDGK 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 518701315 262 LDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVT 302
Cdd:cd06323 228 LAATVAQQPEEMGAKAVETADKYLKGEKVPKKIPVPLKLVT 268
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
22-302 |
2.48e-46 |
|
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: 157.55 E-value: 2.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKL-GVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREPVNVNSLPdnqaFVASNEADSGTLETKEVCRLFKEAGKkeanVYVIMGELSNQAAVQRTKDIEEVIATPD 181
Cdd:cd19968 80 GIPVVTVDRRAEGAAPVP----HVGADNVAGGREVAKFVVDKLPNGAK----VIELTGTPGSSPAIDRTKGFHEELAAGP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 182 CsfIKIIDKQTSNWNRDEAQNLMTNWL-STGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGGVDATQDALAAMQAG 260
Cdd:cd19968 152 K--IKVVFEQTGNFERDEGLTVMENILtSLPGPPDAIICANDDMALGAIEAMRAAGLDLKKVKVIGFDAVPDALQAIKDG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518701315 261 DLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVT 302
Cdd:cd19968 230 ELYATVEQPPGGQARTALRILVDYLKDKKAPKKVNLKPKLIT 271
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
23-289 |
3.90e-46 |
|
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433182 [Multi-domain] Cd Length: 259 Bit Score: 156.70 E-value: 3.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDNFLTVLRNGMIAQAKGMSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAK 102
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 103 IPLVYVNREPVNVNSLpdnqAFVASNEADSGTLETKevcrLFKEAGKKEANVYVIMGELSNQAAVQRTKDIEEVIATPDC 182
Cdd:pfam13407 81 IPVVTFDSDAPSSPRL----AYVGFDNEAAGEAAGE----LLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 183 SFIKIIDKQTSNWNRDEAQNLMTNWLSTGK-KFDGVIANNDESAIGAIQAMKAANIDmKSVVVGGVDATQDALAAMQAGD 261
Cdd:pfam13407 153 GIKVVAEVEGTNWDPEKAQQQMEALLTAYPnPLDGIISPNDGMAGGAAQALEAAGLA-GKVVVTGFDATPEALEAIKDGT 231
|
250 260
....*....|....*....|....*...
gi 518701315 262 LDATVFQDAAGQGAGALDAALKLSKGEK 289
Cdd:pfam13407 232 IDATVLQDPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
22-291 |
5.07e-43 |
|
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: 149.27 E-value: 5.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd19992 1 KIGVSFPTQQEERWQKDKEYMEEEAKEL-GVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREPVNvnslPDNQAFVASNEADSGTLETKEvcrLFKEAGKkeANVYVIMGELSNQAAVQRTKDIEEVIAT-P 180
Cdd:cd19992 80 GVPVISYDRLILN----ADVDLYVGRDNYKVGQLQAEY---ALEAVPK--GNYVILSGDPGDNNAQLITAGAMDVLQPaI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 181 DCSFIKIIDKQ-TSNWNRDEAQNLMTNWLS-TGKKFDGVIANNDESAIGAIQAMKAANIDMKsVVVGGVDATQDALAAMQ 258
Cdd:cd19992 151 DSGDIKIVLDQyVKGWSPDEAMKLVENALTaNNNNIDAVLAPNDGMAGGAIQALKAQGLAGK-VFVTGQDAELAALKRIV 229
|
250 260 270
....*....|....*....|....*....|...
gi 518701315 259 AGDLDATVFQDAAGQGAGALDAALKLSKGEKVE 291
Cdd:cd19992 230 EGTQTMTVWKDLKELARAAADAAVKLAKGEKPQ 262
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
22-300 |
1.09e-41 |
|
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: 145.42 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKgMSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVE-ANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREPVNVNSLpdnQAFVASNEADSGTLETKEVCRLFKEAGKkeanvYVIMGELSNQAAVQRTKDIEEVIAtpD 181
Cdd:cd19971 80 GIPVINVDTPVKDTDLV---DSTIASDNYNAGKLCGEDMVKKLPEGAK-----IAVLDHPTAESCVDRIDGFLDAIK--K 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 182 CSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIdMKSVVVGGVDATQDALAAMQAGD 261
Cdd:cd19971 150 NPKFEVVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGK-LGDILVYGVDGSPDAKAAIKDGK 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 518701315 262 LDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQL 300
Cdd:cd19971 229 MTATAAQSPIEIGKKAVETAYKILNGEKVEKEIVVPTFL 267
|
|
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
1-311 |
6.32e-39 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 139.86 E-value: 6.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 1 MKKLLLGVAFAA--LISSSAFAA--KIGVSMAKFDDNFLTVLRNGMIAQAKGMSGVELQVEDAQNDVAKQLDQIKNFAAS 76
Cdd:PRK15395 1 NKKVLTLSALMAsmLFGAAAAAAdtRIGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 77 GVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNREP-VNVNSLPDNQAFVASNEADSGTLETKEVCRLFKEAGKKEAN-- 153
Cdd:PRK15395 81 GVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPsRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANPAWDLNkd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 154 ---VYVIM-GELSNQAAVQRTKdieEVIATPDCSFIKI--IDKQTSNWNRDEAQNLMTNWLST--GKKFDGVIANNDESA 225
Cdd:PRK15395 161 gkiQYVLLkGEPGHPDAEARTT---YVIKELNDKGIKTeqLQLDTAMWDTAQAKDKMDAWLSGpnANKIEVVIANNDAMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 226 IGAIQAMKAANidMKSVVVGGVDATQDALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGE--------KVEHKVY-V 296
Cdd:PRK15395 238 MGAVEALKAHN--KSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKgaaegtnwKIENKVVrV 315
|
330
....*....|....*
gi 518701315 297 PFQLVTPANIDKFLK 311
Cdd:PRK15395 316 PYVGVDKDNLAEFTK 330
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
22-307 |
1.12e-38 |
|
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: 137.78 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQN--DVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAA 99
Cdd:cd06320 1 KIGVVLKTLSNPFWVAMKDGIEAEAKKL-GVKVDVQAAPSetDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 100 AAKIPLVYVNrEPVNVNSLP----DNQAFVASNEADSGTLETKEVCRLFKEAGKkeanVYVIMGELSNQAAVQRTKDIEE 175
Cdd:cd06320 80 KKGIPVINLD-DAVDADALKkaggKVTSFIGTDNVAAGALAAEYIAEKLPGGGK----VAIIEGLPGNAAAEARTKGFKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 176 VI-ATPDcsfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGgVDATQDAL 254
Cdd:cd06320 155 TFkKAPG---LKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTGKVLVVG-TDGIPEAK 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 518701315 255 AAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVTPANID 307
Cdd:cd06320 231 KSIKAGELTATVAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKDNVD 283
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
22-302 |
4.32e-38 |
|
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: 136.03 E-value: 4.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGmSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKK-KGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREPVNVnslpDNQAFVASNEADSgtleTKEVCR-LFKEAGKKeANVYVIMGELSNQAAVQRTKDIEEVIAtp 180
Cdd:cd19972 80 GIPVIAVDRNPEDA----PGDTFIATDSVAA----AKELGEwVIKQTGGK-GEIAILHGQLGTTPEVDRTKGFQEALA-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 181 DCSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVgGVDATQDALAAMQAG 260
Cdd:cd19972 149 EAPGIKVVAEQTADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDHKIWVV-GFDGDVAGLKAVKDG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518701315 261 DLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVT 302
Cdd:cd19972 228 VLDATMTQQTQKMGRLAVDSAIDLLNGKAVPKEQLQDAVLTT 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
23-302 |
2.18e-37 |
|
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: 133.94 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAK 102
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAEL-GVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 103 IPLVYVNREPVNVNSLpdnqAFVASNEADSGTLETKEVcrlFKEAGKKEANVyVIMGELSNQAAVQRTKDIEEVIAT-PD 181
Cdd:cd06322 81 IPVFTVDVKADGAKVV----THVGTDNYAGGKLAGEYA---LKALLGGGGKI-AIIDYPEVESVVLRVNGFKEAIKKyPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 182 csfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVgGVDATQDALAAMQAGD 261
Cdd:cd06322 153 ---IEIVAEQPGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDKIKVI-GFDGNPEAIKAIAKGG 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518701315 262 -LDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVT 302
Cdd:cd06322 229 kIKADIAQQPDKIGQETVEAIVKYLAGETVEKEILIPPKLYT 270
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
22-305 |
9.66e-36 |
|
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: 130.22 E-value: 9.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKL-GVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNRepvNVNSLPDNQAFVASNEADSGTLETKEVCrlfKEAGKKEANVYVIMGELSNQAAVQRTKD-----IEEV 176
Cdd:cd06318 80 GIPVITVDS---ALDPSANVATQVGRDNKQNGVLVGKEAA---KALGGDPGKIIELSGDKGNEVSRDRRDGflagvNEYQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 177 IATPDCSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDmKSVVVGGVDATQDALAA 256
Cdd:cd06318 154 LRKYGKSNIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGML-DKVKVAGADGQKEALKL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 518701315 257 MQAGDLDATVFQDAAGQGAGALDAALKLSKGE-KVEHKVYVPFQLVTPAN 305
Cdd:cd06318 233 IKDGKYVATGLNDPDLLGKTAVDTAAKVVKGEeSFPEFTYTPTALITKDN 282
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
31-302 |
3.58e-35 |
|
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: 128.21 E-value: 3.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 31 DDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNR 110
Cdd:cd19967 10 NNPFFVVEAEGAKEKAKEL-GYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLIDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 111 EpvnVNSLPDNQAFVASNEADSGTLETKEVCRLFKEAGKkeanvYVIM-GELSNQAAVQRTKDIEEVIAT-PDcsfIKII 188
Cdd:cd19967 89 E---INAEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGL-----YVELlGKESDTNAQLRSQGFHSVIDQyPE---LKMV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 189 DKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDmKSVVVGGVDATQDALAAMQAGDLDATVFQ 268
Cdd:cd19967 158 AQQSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRA-GDVIIVGFDGSNDVRDAIKEGKISATVLQ 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 518701315 269 DAAGQGAGALDAALKLSKGEK--VEHKVYVPFQLVT 302
Cdd:cd19967 237 PAKLIARLAVEQADQYLKGGStgKEEKQLFDCVLIT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
22-313 |
1.88e-33 |
|
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: 124.66 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGM--SGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAA 99
Cdd:cd19996 1 TIGFSNAGLGNSWRVQMIAEFEAEAAKLkkLIKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 100 AAKIPLvyvnrepVNVNSLPDNQAFVASNEADSGTLETKEVCRLFKEAGKKeANVYVIMGELSNQAAVQRTKDIEEVIA- 178
Cdd:cd19996 81 AAGIPV-------VLFDSGVGSDKYTAFVGVDDAAFGRVGAEWLVKQLGGK-GNIIALRGIAGVSVSEDRWAGAKEVFKe 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 179 TPDcsfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANidMKSVVVGGVDATQDALAAMQ 258
Cdd:cd19996 153 YPG---IKIVGEVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAG--RPLVPMTGEDNNGFLKAWKE 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 518701315 259 AGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVTPANIDKFLKKN 313
Cdd:cd19996 228 LPGFKSIAPSYPPWLGATALDAALAALEGEPVPKYVYIPLPVITDENLDQYVKPD 282
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
22-306 |
1.08e-31 |
|
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: 119.39 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEEL-GYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNrepVNVNSlPDNQAFVASNEADSGTLETKEVCRLFKEAGKKEANVYVIMGELSNQAAVQRTKDIEEVIAtpD 181
Cdd:cd06319 80 KIPVVIAD---IGTGG-GDYVSYIISDNYDGGYQAGEYLAEALKENGWGGGSVGIIAIPQSRVNGQARTAGFEDALE--E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 182 CSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKsVVVGGVDATQDALAAMQAGD 261
Cdd:cd06319 154 AGVEEVALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGD-ILVVGFDGDPEALDLIKDGK 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 518701315 262 LDATVFQDAAGQGAGALDAALKLSKGEKVEHK-VYVPFQLVTPANI 306
Cdd:cd06319 233 LDGTVAQQPFGMGARAVELAIQALNGDNTVEKeIYLPVLLVTSENV 278
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
22-302 |
2.52e-30 |
|
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: 115.46 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMS-GVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAA 100
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINpGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 101 AKIPLVYVNrepVNVNSLpdnQAFVASNEADSGTLetkeVCRLFKEAGKKEANVYVIMGeLSNQAAVQRTKDIEEVIAT- 179
Cdd:cd06321 81 AGIIVVAVD---VAAEGA---DATVTTDNVQAGYL----ACEYLVEQLGGKGKVAIIDG-PPVSAVIDRVNGCKEALAEy 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 180 PDcsfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDmkSVVVGGVDATQDALAAMQA 259
Cdd:cd06321 150 PG---IKLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRD--DIVITSVDGSPEAVAALKR 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 518701315 260 GD--LDATVFQDAAGQGAGALDAALKLSKGEKVEHK-VYVPFQLVT 302
Cdd:cd06321 225 EGspFIATAAQDPYDMARKAVELALKILNGQEPAPElVLIPSTLVT 270
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
21-308 |
1.88e-29 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 114.08 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 21 AKIGVSMAKFD------DnfltvlRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAM 94
Cdd:COG4213 3 IKIGVSLPTKTserwirD------GDNFKAALKEL-GYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 95 SDAAAAAKIPLVYVNREPVNVNSlpdnQAFVASNEADSGTLETKevcRLFKEAGKK-EANVYVIMGELS-NQAAVQRT-- 170
Cdd:COG4213 76 LEKAKAAGIPVIAYDRLILNSDV----DYYVSFDNVKVGELQGQ---YLVDGLPLKgKGNIELFGGSPTdNNATLFFEga 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 171 -KDIEEVIATPDcsfIKIIDKQ-TSNWNRDEAQNLMTNWL-STGKKFDGVIANNDESAIGAIQAMKAANIDMKsVVVGGV 247
Cdd:COG4213 149 mSVLQPYIDSGK---LVVVSGQwTLGWDPETAQKRMENLLtANGNKVDAVLAPNDGLAGGIIQALKAQGLAGK-VVVTGQ 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518701315 248 DATQDALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVE-------HKVYVPFQLVTPANIDK 308
Cdd:COG4213 225 DAELAAVQRILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPEvngtydnGKKDVPSYLLEPVAVTK 292
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
22-302 |
4.43e-29 |
|
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: 112.05 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAK--GMSGVELQVEDaQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAA 99
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKdlGVKIIFVGPES-EEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 100 AAKIPLVYVNRepvnvNSLPD-NQAFVASNEADSGTLetkeVCRLFKEAGKKEANVYVIMGELSNQAAVQRTKDIEEVIA 178
Cdd:cd06310 80 DKGIPVIVIDS-----GIKGDaYLSYIATDNYAAGRL----AAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 179 TPDCSfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGgVDATQDALAAMQ 258
Cdd:cd06310 151 KHPGG-IKVLASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIVG-FDSQEELLDALK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 518701315 259 AGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVT 302
Cdd:cd06310 229 NGKIDALVVQNPYEIGYEGIKLALKLLKGEEVPKNIDTGAELIT 272
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
22-291 |
4.44e-29 |
|
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: 112.57 E-value: 4.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGmSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd19993 1 VVGVSWSNFQEERWKTDEAAMKKALEK-AGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNRepvnvnsLPDNQ--AFVASNEADSGTLETKEVCRLfkeagKKEANVYVIMGELS-NQAAVQRTKDIEEVIA 178
Cdd:cd19993 80 GIPVIAYDR-------LIENPiaFYISFDNVEVGRMQARGVLKA-----KPEGNYVFIKGSPTdPNADFLRAGQMEVLQP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 179 TPDCSFIKIIDKQ-TSNWNRDEAQNLMTNWLS-TGKKFDGVIANNDESAIGAIQAMKAANIdMKSVVVGGVDATQDALAA 256
Cdd:cd19993 148 AIDSGKIKIVGEQyTDGWKPANAQKNMEQILTaNNNKVDAVVASNDGTAGGAVAALAAQGL-AGKVPVSGQDADKAALNR 226
|
250 260 270
....*....|....*....|....*....|....*
gi 518701315 257 MQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVE 291
Cdd:cd19993 227 IALGTQTVTVWKDARELGKEAAEIAVELAKGTKIE 261
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
42-312 |
7.47e-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: 112.70 E-value: 7.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 42 MIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAAS--GVDAIIVNPVDTSATQAMSdAAAAAKIPLVYVNrepvnvNSLP 119
Cdd:cd06324 22 MQAAAKDL-GIELEVLYANRNRFKMLELAEELLARppKPDYLILVNEKGVAPELLE-LAEQAKIPVFLIN------NDLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 120 DNQ---------------AFVASNEADSGTLETKEvcrLFKEAGK----KEANVYVIMGELSNQAAVQRTKDIEEVIA-T 179
Cdd:cd06324 94 DEErallgkprekfkywlGSIVPDNEQAGYLLAKA---LIKAARKksddGKIRVLAISGDKSTPASILREQGLRDALAeH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 180 PDCSFIKIIDkqtSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANID-MKSVVVGGVDATQDALAAMQ 258
Cdd:cd06324 171 PDVTLLQIVY---ANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKpGKDVLVGGIDWSPEALQAVK 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 259 AGDLDATVfqdaAG---QGAGALDAALKLSKGE---KVEHKVYVPFQLVTPANIDKFLKK 312
Cdd:cd06324 248 DGELTASV----GGhflEGAWALVLLYDYHHGIdfaAGTSVQLKPMLAITRDNVAQYLKL 303
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
32-310 |
8.78e-29 |
|
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: 111.70 E-value: 8.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 32 DNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNre 111
Cdd:cd06317 11 AQFFNQINQGAQAAAKDL-GVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYD-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 112 pVNVNSlPDNQAFVASNEADSGTLETKEVCRLFKEAGKKEANVYViMGELSNQAAVQRTKDIEEVI-ATPDCSFIKIIDk 190
Cdd:cd06317 88 -AVIPS-DFQAAQVGVDNLEGGKEIGKYAADYIKAELGGQAKIGV-VGALSSLIQNQRQKGFEEALkANPGVEIVATVD- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 191 qtsNWNRDE-----AQNLMTnwlsTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGGVDATQDALAAMQAGDLDAT 265
Cdd:cd06317 164 ---GQNVQEkalsaAENLLT----ANPDLDAIYATGEPALLGAVAAVRSQGRQGKIKVFGWDLTKQAIFLGIDEGVLQAV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 518701315 266 VFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVTPANIDKFL 310
Cdd:cd06317 237 VQQDPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTKENVDQFR 281
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-302 |
2.06e-28 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 110.95 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 1 MKK---LLLGVAFAALISSSAFAAK-IGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAAS 76
Cdd:PRK10653 3 MKKlatLVSAVALSATVSANAMAKDtIALVVSTLNNPFFVSLKDGAQKEADKL-GYNLVVLDSQNNPAKELANVQDLTVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 77 GVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNRepvnVNSLPDNQAFVASNEADSGTLETKEVCrlfKEAGKKeANVYV 156
Cdd:PRK10653 82 GTKILLINPTDSDAVGNAVKMANQANIPVITLDR----GATKGEVVSHIASDNVAGGKMAGDFIA---KKLGEG-AKVIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 157 IMGELSNQAAVQRTKDIEEVIATPDcsfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAAN 236
Cdd:PRK10653 154 LEGIAGTSAARERGEGFKQAVAAHK---FNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518701315 237 idMKSVVVGGVDATQDALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVT 302
Cdd:PRK10653 231 --KSDVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGVETADKVLKGEKVEAKIPVDLKLVT 294
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
22-300 |
5.11e-26 |
|
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: 103.87 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMSGVELQVEDAQN--DVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAA 99
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEANGYELLVKGIKQetDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 100 AAKIPLVYVNrepvnvNSLPD--------NQAFVASNEADSGTLETKEVCRLFKEAGKkeanVYVIMGELSNQAAVQRTK 171
Cdd:cd19970 81 DAGIAVINID------NRLDAdalkeggiNVPFVGPDNRQGAYLAGDYLAKKLGKGGK----VAIIEGIPGADNAQQRKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 172 DIEEVIATPDcsfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKsVVVGGVDATQ 251
Cdd:cd19970 151 GFLKAFEEAG---MKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGK-VLVVGFDNIP 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 518701315 252 DALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQL 300
Cdd:cd19970 227 AVRPLLKDGKMLATIDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPVEL 275
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
31-303 |
1.44e-25 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 102.68 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 31 DDNFLTVLRNGMIAQAKGmSGVELQVE--DAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYV 108
Cdd:cd20006 12 NSDFWQTVKSGAEAAAKE-YGVDLEFLgpESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 109 NREpvnVNSlPDNQAFVASNEADSGTLETKEVCRLFKEAGKkeanVYVIMGELSNQAAVQRTKDIEEVIAtpDCSFIKII 188
Cdd:cd20006 91 DSP---VNS-KKADSFVATDNYEAGKKAGEKLASLLGEKGK----VAIVSFVKGSSTAIEREEGFKQALA--EYPNIKIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 189 DKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDmKSVVVGGVDATQDALAAMQAGDLDATVFQ 268
Cdd:cd20006 161 ETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLG-GKVKVVGFDSSVEEIQLLEEGIIDALVVQ 239
|
250 260 270
....*....|....*....|....*....|....*
gi 518701315 269 DAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVTP 303
Cdd:cd20006 240 NPFNMGYLSVQAAVDLLNGKKIPKRIDTGSVVITK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
59-295 |
1.81e-25 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 102.69 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 59 AQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMsDAAAAAKIPLVYVNREpvnVNSlPDNQAFVASNEADSGTLETK 138
Cdd:cd20008 39 TEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPA-VEAADAGIPVVLVDSG---ANT-DDYDAFLATDNVAAGALAAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 139 EVCRLFKEAGKKEANVYVIMGELSNQAAVQRTKDIEEVIATpDCSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVI 218
Cdd:cd20008 114 ELAELLKASGGGKGKVAIISFQAGSQTLVDREEGFRDYIKE-KYPDIEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518701315 219 ANNDESAIGAIQAMKAANIDmKSVVVGGVDATQDALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVY 295
Cdd:cd20008 193 GANNPSAVGVAQALAEAGKA-GKIVLVGFDSSPDEVALLKSGVIKALVVQDPYQMGYEGVKTAVKALKGEEIVEKNV 268
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
23-300 |
3.64e-25 |
|
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: 101.55 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATqAMSDAAAAAK 102
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQP-GVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAA-GVAEKARGQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 103 IPLVYVNREPvnvnSLPDNQAFVASNEADSGTLETkevcRLFKEAGKKEanVYVIMGELSNQAAVQRT----KDIEE-VI 177
Cdd:cd01537 80 VPVVFFDKEP----SRYDKAYYVITDSKEGGIIQG----DLLAKHGHIQ--IVLLKGPLGHPDAEARLagviKELNDkGI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 178 ATPDcsfikiIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDM-KSVVVGGVDATQDALaa 256
Cdd:cd01537 150 KTEQ------LQLDTGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVpSDISVFGYDALPEAL-- 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 518701315 257 mQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHK-VYVPFQL 300
Cdd:cd01537 222 -KSGPLLTTILQDANNLGKTTFDLLLNLADNWKIDNKvVRVPYVL 265
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
22-290 |
1.16e-24 |
|
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: 101.23 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSmakfDDNFLTVLRNGMIA---------QAKGMSgVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQ 92
Cdd:cd19999 1 VIGVS----NGYVGNEWRAQMIAdfeevaaeyKEEGVI-SDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 93 AMSDAAAAAKIPLVYVNREPVNVNSLpdnqaFVASNEADSGTLETkevcRLFKEAGKKEANVYVIMGELSNQAAVQRTKD 172
Cdd:cd19999 76 PVIEKAQAAGILVVSFDQPVSSPDAI-----NVVIDQYKWAAIQA----QWLAEQLGGKGNIVAINGVAGNPANEARVKA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 173 IEEVIA-TPDcsfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIaNNDESAIGAIQAMKAANIDMKsVVVGgvDATQ 251
Cdd:cd19999 147 ADDVFAkYPG---IKVLASVPGGWDQATAQQVMATLLATYPDIDGVL-TQDGMAEGVLRAFQAAGKDPP-VMTG--DYRK 219
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518701315 252 DAL---AAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKV 290
Cdd:cd19999 220 GFLrkwKELDLPDFESIGVVNPPGIGATALRIAVRLLQGKEL 261
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
22-289 |
1.61e-24 |
|
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: 100.19 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEK-GAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREPVNVnslpDNQAFVASNEADSGTLETKevcRLFKEAGKKEanvYVIMG--ELSNQAAVQRTKDIEEVIAT 179
Cdd:cd01538 80 GIKVIAYDRLILNA----DVDYYISFDNEKVGELQAQ---ALLDAKPEGN---YVLIGgsPTDNNAKLFRDGQMKVLQPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 180 PDCSFIKIIDKQ-TSNWNRDEAQNLMTNWLSTGK-KFDGVIANNDESAIGAIQAMKAANIdMKSVVVGGVDATQDALAAM 257
Cdd:cd01538 150 IDSGKIKVVGDQwVDDWLPANAQQIMENALTANGnNVDAVVASNDGTAGGAIAALKAQGL-SGGVPVSGQDADLAAIKRI 228
|
250 260 270
....*....|....*....|....*....|..
gi 518701315 258 QAGDLDATVFQDAAGQGAGALDAALKLSKGEK 289
Cdd:cd01538 229 LAGTQTMTVYKDIRLLADAAAEVAVALMRGEK 260
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
41-293 |
1.62e-24 |
|
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: 100.44 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 41 GMIAQAKGM-SGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNREPVNVNSlp 119
Cdd:cd19995 21 GFEKAMKKLcPDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPA-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 120 dnQAFVASNEADSGTLETKEVCRLFKEAGKKEANVYVIMGELSNQAAVQRTKDIEEVI--ATPDCSFIKIIDKQTSNWNR 197
Cdd:cd19995 99 --DYYVSFDNVAVGEAQAQSLVDHLKAIGKKGVNIVMINGSPTDNNAGLFKKGAHEVLdpLGDSGELKLVCEYDTPDWDP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 198 DEAQNLMTNWLS-TGKKFDGVIANNDESAIGAIQAMKAANIDMKsVVVGGVDATQDALAAMQAGDLDATVFQDAAGQGAG 276
Cdd:cd19995 177 ANAQTAMEQALTkLGNNIDGVLSANDGLAGGAIAALKAQGLAGK-VPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAAA 255
|
250
....*....|....*..
gi 518701315 277 ALDAALKLSKGEKVEHK 293
Cdd:cd19995 256 AAKVAVALLKGETPPSD 272
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
52-306 |
8.94e-24 |
|
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: 98.51 E-value: 8.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 52 VELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLV-YVNR--EPVNVNslpdnqafVASN 128
Cdd:cd19998 34 VELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVaFDNVvdEPCAYN--------VNTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 129 EADSGTLETKEVCRLFKEAGkkeaNVYVIMGELSNQAAVQRTKDIEEVI-ATPDcsfIKIIDKQTSNWNRDEAQNLMTNW 207
Cdd:cd19998 106 QAKAGEQTAQWLVDKLGGKG----NILMVRGVPGTSVDRDRYEGAKEVFkKYPD---IKVVAEYYGNWDDGTAQKAVADA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 208 LSTGKKFDGVIANNDESaiGAIQAMKAANIDMKSVVVGGVDATQDALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKG 287
Cdd:cd19998 179 LAAHPDVDGVWTQGGET--GVIKALQAAGHPLVPVGGEAENGFRKAMLEPLANGLPGISAGSPPALSAVALKLAVAVLEG 256
|
250
....*....|....*....
gi 518701315 288 EKVEHKVYVPFQLVTPANI 306
Cdd:cd19998 257 EKEPKTIELPLPWVTTDDV 275
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
53-311 |
1.16e-22 |
|
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: 95.47 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 53 ELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNrepvnvNSLPDNQAF-VASNEAD 131
Cdd:cd06300 36 ELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFD------GAVTSPDAYnVSNDQVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 132 SGTLETKEvcrLFKEAGKKeANVYVIMGELSNQAAVQRTKDIEEVIA-TPDcsfIKIIDKQTSNWNRDEAQNLMTNWLST 210
Cdd:cd06300 110 WGRLGAKW---LFEALGGK-GNVLVVRGIAGAPASADRHAGVKEALAeYPG---IKVVGEVFGGWDEATAQTAMLDFLAT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 211 GKKFDGVIANNDESaIGAIQAMKAANidMKSVVVGGVDATQDALAAMQAGDLD---ATVFQDAAgQGAGALDAALKLSKG 287
Cdd:cd06300 183 HPQVDGVWTQGGED-TGVLQAFQQAG--RPPVPIVGGDENGFAKQWWKHPKKGltgAAVWPPPA-IGAAGLEVALRLLEG 258
|
250 260
....*....|....*....|....*
gi 518701315 288 EK-VEHKVYVPFQLVTPANIDKFLK 311
Cdd:cd06300 259 QGpKPQSVLLPPPLITNDDAKAWYK 283
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
22-303 |
1.92e-22 |
|
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: 94.61 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd19991 1 KIGFSMDSLRVERWQRDRDYFVKKAKEL-GAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREPVNVnslpDNQAFVASNeadsgtleTKEVCRLFKEA---GKKEANVYVIMGELSNQAAVQRTKDIEEVIA 178
Cdd:cd19991 80 GVPVLAYDRLILNA----DVDLYVSFD--------NEKVGELQAEAlvkAKPKGNYVLLGGSPTDNNAKLFREGQMKVLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 179 tP--DCSFIKIIDKQ-TSNWNRDEAQNLMTNWLS-TGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGgvdatQDA- 253
Cdd:cd19991 148 -PliDSGDIKVVGDQwVDDWDPEEALKIMENALTaNNNKIDAVIASNDGTAGGAIQALAEQGLAGKVAVSG-----QDAd 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 254 LAAMQ---AGDLDATVFQDAAGQGAGALDAALKLSKGEKVEH-------KVYVPFQLVTP 303
Cdd:cd19991 222 LAACQrivEGTQTMTIYKPIKELAEKAAELAVALAKGEKNEAnrtinngKKEVPSILLDP 281
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
22-301 |
1.32e-21 |
|
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: 91.87 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQ--NDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAA 99
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRL-GVKLTVYEAGgyTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 100 AAKIPLV-YVNRepvnVNSlPDNQAFVASNEADSGTLETKEVCrlfKEAGKKEANVYVIMGELSNQAAVQRTKDIEEVIA 178
Cdd:cd06306 80 AAGIPVIdLVNG----IDS-PKVAARVLVDFYDMGYLAGEYLV---EHHPGKPVKVAWFPGPAGAGWAEDREKGFKEALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 179 TPDcsfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDgVIANNDESAIGAIQAMKAANIDMKsVVVGGVDATQDALAAMQ 258
Cdd:cd06306 152 GSN---VEIVATKYGDTGKAVQLNLVEDALQAHPDID-YIVGNAVAAEAAVGALREAGLTGK-VKVVSTYLTPGVYRGIK 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 518701315 259 AGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLV 301
Cdd:cd06306 227 RGKILAAPSDQPVLQGRIAVDQAVRALEGKPVPKHVGPPILVV 269
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
28-302 |
1.37e-21 |
|
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: 91.87 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 28 AKFDDN-FLTVLRNGMIAQAKGMsGVELQVEDAQN-DVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPL 105
Cdd:cd06314 6 PKGLNNpFWDLAEAGAEKAAKEL-GVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 106 VYVNrepvnvNSLPDN--QAFVASNEADSGtletKEVCRLFKEAGKKEANVYVIMGELSNQAAVQRTKDIEEVIAtpDCS 183
Cdd:cd06314 85 ITFD------SDAPDSkrLAYIGTDNYEAG----REAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALK--GSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 184 FIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIdMKSVVVGGVDATQDALAAMQAGDLD 263
Cdd:cd06314 153 GIEIVDPLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGK-VGKVKIVGFDTLPETLQGIKDGVIA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 518701315 264 ATVFQDAAGQGAGALDAALKLSKGEK-VEHKVYVPFQLVT 302
Cdd:cd06314 232 ATVGQRPYEMGYLSVKLLYKLLKGGKpVPDVIDTGVDVVT 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
44-301 |
3.23e-20 |
|
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: 88.19 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 44 AQAKGMSGVELQVEDAQNdVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNREpVNVnslPDNQA 123
Cdd:cd06311 23 KQAKELADLEYKLVTSSN-ANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRG-LNV---LIYDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 124 FVASNEADSGTLETKevcrLFKEAGKKEANVYVIMGELSNQAAVQRTKDIEEVIAT-PDcsfIKIIDKQTSNWNRDEAQN 202
Cdd:cd06311 98 YVAGDNPGMGVVSAE----YIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGnPG---IKILAMQAGDWTREDGLK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 203 LMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGGVdATQDALAAMQAGD--LDATVFQDAAGQGAGALDA 280
Cdd:cd06311 171 VAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIKVMTGGG-GSQEYFKRIMDGDpiWPASATYSPAMIADAIKLA 249
|
250 260
....*....|....*....|.
gi 518701315 281 ALKLSKGEKVEHKVYVPFQLV 301
Cdd:cd06311 250 VLILKGGKTVEKEVIIPSTLV 270
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
22-302 |
4.06e-20 |
|
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: 88.07 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVE--DAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAA 99
Cdd:cd20005 1 YIAVISKGFQHQFWKAVKKGAEQAAKEL-GVKITFEgpDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 100 AAKIPLVYVNRepvNVNS-LPdnQAFVASNEADSGTLETKEVCRLFKEAGKkeanVYVIMGELSNQAAVQRTKDIEEVIA 178
Cdd:cd20005 80 EKGIPVVTFDS---GVPSdLP--LATVATDNYAAGALAADHLAELIGGKGK----VAIVAHDATSETGIDRRDGFKDEIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 179 TpDCSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANiDMKSVVVGGVDATQDALAAMQ 258
Cdd:cd20005 151 E-KYPDIKVVNVQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMG-KLGKIKVVGFDSGEAQIDAIK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 518701315 259 AGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVT 302
Cdd:cd20005 229 NGVIAGSVTQNPYGMGYKTVKAAVKALKGEEVEKLIDTGAKWYD 272
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
22-303 |
1.02e-19 |
|
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: 86.90 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKgmsgvELQVE------DAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMS 95
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQ-----ELGVEiywrgpSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 96 DAAAAAKIPLVYVNRepvnvnSLPDN--QAFVASNEADSGTLETKEVCRLFKEAGKkeanvyVIMGELS--NQAAVQRTK 171
Cdd:cd20004 76 ERARAQGIPVVIIDS------DLGGDavISFVATDNYAAGRLAAKRMAKLLNGKGK------VALLRLAkgSASTTDRER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 172 DIEEVIATpDCSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANiDMKSVVVGGVDATQ 251
Cdd:cd20004 144 GFLEALKK-LAPGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLG-LAGKVKFIGFDASD 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 518701315 252 DALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVTP 303
Cdd:cd20004 222 LLLDALRAGEISALVVQDPYRMGYLGVKTAVAALRGKPVPKRIDTGVVLVTK 273
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
23-301 |
2.27e-19 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 86.79 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDNFLTVLRNGMIAQAKgMSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVnpVDTSATQAMSDAAAAAK 102
Cdd:COG1609 64 IGVVVPDLSNPFFAELLRGIEEAAR-ERGYQLLLANSDEDPEREREALRLLLSRRVDGLIL--AGSRLDDARLERLAEAG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 103 IPLVYVNREPVNVNSlpdnqAFVASNEADSGtletKEVCRLFKEAGKKeaNVYVIMGELSNQAAVQRTKDIEEVIA---- 178
Cdd:COG1609 141 IPVVLIDRPLPDPGV-----PSVGVDNRAGA----RLATEHLIELGHR--RIAFIGGPADSSSARERLAGYREALAeagl 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 179 TPDCSFIkiidkQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANI----DMkSVVvgGVDatQDAL 254
Cdd:COG1609 210 PPDPELV-----VEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLrvpeDV-SVV--GFD--DIPL 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 518701315 255 AAMQAGDLdATVFQDAAGQGAGALDAALKLSKGEKVE-HKVYVPFQLV 301
Cdd:COG1609 280 ARYLTPPL-TTVRQPIEEMGRRAAELLLDRIEGPDAPpERVLLPPELV 326
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
32-302 |
2.24e-18 |
|
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: 83.06 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 32 DNFLTVLRNGMIAQAKGMsGVELQVEDAQN-DVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNr 110
Cdd:cd20007 11 DPFYITMQCGAEAAAKEL-GVELDVQGPPTfDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 111 EPVNVNSLPdnQAFVASNEADSGTLETKEVCRLFKEAGKkeanVYVIMGELSNQAAVQRTKDIEEVI-ATPDcsfIKIID 189
Cdd:cd20007 89 TTLGDPSFV--LSQIASDNVAGGALAAEALAELIGGKGK----VLVINSTPGVSTTDARVKGFAEEMkKYPG---IKVLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 190 KQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGGvDATQDALAAMQAGDLDATVFQD 269
Cdd:cd20007 160 VQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGKVKVVGF-DASPAQVEQLKAGTIDALIAQK 238
|
250 260 270
....*....|....*....|....*....|...
gi 518701315 270 AAGQGAGALDAALKLSKGEKVEHKVYVPFQLVT 302
Cdd:cd20007 239 PAEIGYLAVEQAVAALTGKPVPKDILTPFVVIT 271
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
22-302 |
5.32e-18 |
|
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: 81.96 E-value: 5.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAA 101
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKL-GGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVyvnrePVNVNSLPDNQAFVASNEADSGTLETKEvcrLFKEAGkKEANVYVImgelsNQAAV----QRTKDIEEVI 177
Cdd:cd06305 80 GIPVV-----TFDTDSQVPGVNNITQDDYALGTLSLGQ---LVKDLN-GEGNIAVF-----NVFGVppldKRYDIYKAVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 178 -ATPDCSFIK-IIDKQTSNwNRDEAQNLMTNWLSTGKK--FDGVIANNDESAIGAIQAMKAANIDmkSVVVGGVDATQDA 253
Cdd:cd06305 146 kANPGIKKIVaELGDVTPN-TAADAQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRT--DIKVYGVDISNQD 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 518701315 254 LAAMQAGD--LDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVT 302
Cdd:cd06305 223 LELMADEGspWVATAAQDPALIGTVAVRNVARKLAGEDLPDKYSLVPVLIT 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
22-312 |
1.48e-17 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380652 [Multi-domain] Cd Length: 305 Bit Score: 81.18 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAkFDDNfltVLRNGMI---------AQAKGMSGvELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQ 92
Cdd:cd19997 1 VIALSNS-YAGN---TWRQQMVdafeeaakkAKADGLIA-DYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 93 AMSDAAAAAKIPLVYVNrepvNVNSLPDNQaFVASNEADSGTLETKEVCrlfKEAGKKeANVYVIMGELSNQAAVQRTKD 172
Cdd:cd19997 76 GAIQQACDAGIKVVVFD----SGVTEPCAY-ILNNDFEDYGAASVEYVA---DRLGGK-GNVLEVRGVAGTSPDEEIYAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 173 IEEVIAT-PDcsfIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDeSAIGAIQAMKAANIDMKSVVVGGvdaTQ 251
Cdd:cd19997 147 QVEALKKyPD---LKVVAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGG-DGYGAAQAFEAAGRPLPIIIGGN---RG 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518701315 252 DALA----AMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVTPANIDKFLKK 312
Cdd:cd19997 220 EFLKwwqeEYAKNGYETVSVSTDPGQGSAAFWVALDILNGKDVPKEMILPVVTITEDDLDAWLAV 284
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
1-290 |
4.65e-16 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 77.22 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 1 MKKLLLGVAFAALISSSAF-AAKIGVSMAKFDDNFLTVLRNGMIAQAKGMS-GVELQVEDAQNDVAKQLDQIKNFAASGV 78
Cdd:PRK09701 4 YLKYFSGTLVGLMLSTSAFaAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGvSVDIFASPSEGDFQSQLQLFEDLSNKNY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 79 DAIIVNPVDTSATQAMSDAAAAAKIPLVYVNrEPVNVNSLPDN----QAFVAS-NEADSGTLETKEVCRLFKEAGKkean 153
Cdd:PRK09701 84 KGIAFAPLSSVNLVMPVARAWKKGIYLVNLD-EKIDMDNLKKAggnvEAFVTTdNVAVGAKGASFIIDKLGAEGGE---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 154 VYVIMGELSNQAAVQRTKDIEEVIATPdcSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMK 233
Cdd:PRK09701 159 VAIIEGKAGNASGEARRNGATEAFKKA--SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 518701315 234 AANIDMKSVVVgGVDATQDALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKV 290
Cdd:PRK09701 237 NAGKTGKVLVV-GTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLMVDAEKSGKV 292
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
23-301 |
2.42e-15 |
|
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: 74.48 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDNFLTVLRNGMIAQAKgMSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTsaTQAMSDAAAAAK 102
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAAR-ERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSL--DDELLEELLAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 103 IPLVYVNREPVNVNSlpdnqAFVASNEADSGtletKEVCRLFKEAGKKeaNVYVIMGELSNQAAVQRTKDIEEVIATpdc 182
Cdd:cd06267 79 IPVVLIDRRLDGLGV-----DSVVVDNYAGA----YLATEHLIELGHR--RIAFIGGPLDLSTSRERLEGYRDALAE--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 183 SFIKIIDK--QTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANI----DMkSVVvgGVDATQdaLAA 256
Cdd:cd06267 145 AGLPVDPElvVEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLrvpeDI-SVV--GFDDIP--LAA 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 518701315 257 MQAGDLdATVFQDAAGQGAGALDAALKLSKGEKVE-HKVYVPFQLV 301
Cdd:cd06267 220 LLTPPL-TTVRQPAYEMGRAAAELLLERIEGEEEPpRRIVLPTELV 264
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
52-291 |
8.95e-15 |
|
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: 73.43 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 52 VELQVedAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNREPVNVnslpDNQAFVAS--NE 129
Cdd:cd19994 32 VDLQY--ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYDRLIMNT----DAVDYYVTfdNE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 130 AdSGTLETKE-VCRLFKEAGKKEANVYVIMGELS-------NQAAVQRTKD-IEE---VIATPDCSFIKIIdkqTSNWNR 197
Cdd:cd19994 106 K-VGELQGQYlVDKLGLKDGKGPFNIELFAGSPDdnnaqlfFKGAMEVLQPyIDDgtlVVRSGQTTFEQVA---TPDWDT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 198 DEAQNLMTNWLS----TGKKFDGVIANNDESAIGAIQAMKAANIDMKSV-VVGGVDATQDALAAMQAGDLDATVFQDAAG 272
Cdd:cd19994 182 ETAQARMETLLSayytGGKKLDAVLSPNDGIARGVIEALKAAGYDTGPWpVVTGQDAEDASVKSILDGEQSMTVFKDTRL 261
|
250
....*....|....*....
gi 518701315 273 QGAGALDAALKLSKGEKVE 291
Cdd:cd19994 262 LAKATVELVDALLEGEEVE 280
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
58-301 |
3.01e-14 |
|
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: 71.40 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 58 DAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSatqamSDAAAAAKIPLVYVNREpvnvnsLPDNQAFVASNEADSGTLET 137
Cdd:cd06291 36 NSNEDEEKEKEYLEMLKRNKVDGIILGSHSLD-----IEEYKKLNIPIVSIDRY------LSEGIPSVSSDNYQGGRLAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 138 KEvcrlFKEAGKKeaNVYVIMGELSNQAAVQRTKDIEEVIATPDCSFIkIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGV 217
Cdd:cd06291 105 EH----LIEKGCK--KILHIGGPSNNSPANERYRGFEDALKEAGIEYE-IIEIDENDFSEEDAYELAKELLEKYPDIDGI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 218 IANNDESAIGAIQAMKAANI----DMKsvVVG--GVDATQDALAAMqagdldATVFQDAAGQGAGALDAALKL-SKGEKV 290
Cdd:cd06291 178 FASNDLLAIGVLKALQKLGIrvpeDVQ--IIGfdGIEISELLYPEL------TTIRQPIEEMAKEAVELLLKLiEGEEIE 249
|
250
....*....|.
gi 518701315 291 EHKVYVPFQLV 301
Cdd:cd06291 250 ESRIVLPVELI 260
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
25-274 |
3.34e-13 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380535 [Multi-domain] Cd Length: 272 Bit Score: 68.41 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 25 VSMAKFDDNFLTVLRNGMIAQAKGMsGVELQVEDAQ-NDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKI 103
Cdd:cd06312 5 ISHGSPSDPFWSVVKKGAKDAAKDL-GVTVQYLGPQnNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 104 PLVYVNREPvnVNSLPDNQA--FVASNEADSGTLETKEvcrlFKEAGKKeaNVYVIMGELSNQAAVQRTKDIEEVIATPD 181
Cdd:cd06312 84 PVIAINSGD--DRSKERLGAltYVGQDEYLAGQAAGER----ALEAGPK--NALCVNHEPGNPGLEARCKGFADAFKGAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 182 CSFIKIIDKQTSNwnrdEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKsVVVGGVDATQDALAAMQAGD 261
Cdd:cd06312 156 ILVELLDVGGDPT----EAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGK-VKIGTFDLSPETLEAIKDGK 230
|
250
....*....|...
gi 518701315 262 LDATVFQDAAGQG 274
Cdd:cd06312 231 ILFAIDQQPYLQG 243
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
22-312 |
2.24e-12 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380539 [Multi-domain] Cd Length: 294 Bit Score: 66.11 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMsGVE-LQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAA 100
Cdd:cd06316 1 KVAIAMHTTGSDWSRLQVAGIKDTFEEL-GIEvVAVTDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 101 AKIPLVYVNREPVNVNSLPDNQAFVASNEADSGTLETKEVCRLFKEAGKkeanVYVIMGELSNQAAVQRTKDIEEVIAT- 179
Cdd:cd06316 80 AGIKLVFMDNVPDGLEAGKDYVSVVSSDNRGNGQIAAELLAEAIGGKGK----VGIIYHDADFYATNQRDKAFKDTLKEk 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 180 -PDcsfIKIIDKQ-TSNWNR--DEAQNLMTNWlstgKKFDGVIANNDESAIGAIQAMKAANidMKSVVVGGVD-ATQDAL 254
Cdd:cd06316 156 yPD---IKIVAEQgFADPNDaeEVASAMLTAN----PDIDGIYVSWDTPALGVISALRAAG--RSDIKITTVDlGTEIAL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 518701315 255 AAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVEHKVYVPFQLVTPANIDKFLKK 312
Cdd:cd06316 227 DMAKGGNVKGIGAQRPYDQGVAEALAAALALLGKEVPPFIGVPPLAVTKDNLLEAWKQ 284
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
31-274 |
2.96e-12 |
|
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: 65.81 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 31 DDNFLTVLRNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVN-PVDTSATQAMSDAAAAAKIPLVYVN 109
Cdd:cd19966 11 GDPFWTVVYNGAKDAAADL-GVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMgHPGDGAYTPLIEAAKKAGIIVTSFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 110 repvnvNSLPDNQ------AFVASNEADSGTLETKEvcrLFKEAGKKEANVYVIMGELSNQ-AAVQRTKDIEEVIaTPDC 182
Cdd:cd19966 90 ------TDLPKLEygdcglGYVGADLYAAGYTLAKE---LVKRGGLKTGDRVFVPGLLPGQpYRVLRTKGVIDAL-KEAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 183 SFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGGVDATQDALAAMQAGDL 262
Cdd:cd19966 160 IKVDYLEISLEPNKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKKPGEIPVAGFDLSPATVQAIKSGYV 239
|
250
....*....|..
gi 518701315 263 DATVFQDAAGQG 274
Cdd:cd19966 240 NATIDQQPYLQG 251
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
34-274 |
8.91e-12 |
|
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: 64.22 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 34 FLTVLRNGMIAQAKGMsGVELQVEDAQN-DVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNrep 112
Cdd:cd19965 13 FFQPVKKGMDDACELL-GAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAFN--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 113 VNVNSLPDN-QAFVASNEADSGTLETKEVCRLFKeagKKEANVYVIMGELSNQAAVQRTKDIEEVIAtpDCSFIKIIDKQ 191
Cdd:cd19965 89 VDAPGGENArLAFVGQDLYPAGYVLGKRIAEKFK---PGGGHVLLGISTPGQSALEQRLDGIKQALK--EYGRGITYDVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 192 TSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDmKSVVVGGVDATQDALAAMQAGDLDATVFQDAA 271
Cdd:cd19965 164 DTGTDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLK-GKVLVGGFDLVPEVLQGIKAGYIDFTIDQQPY 242
|
...
gi 518701315 272 GQG 274
Cdd:cd19965 243 LQG 245
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
42-307 |
9.00e-12 |
|
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: 64.28 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 42 MIAQAKGMSGVELQVE-DAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNREPVNVNSLpd 120
Cdd:cd19969 20 GFEDAGAELGVKTEYTgPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSDAPESKRI-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 121 nqAFVASNEADSGTLETKEVCRLFKEAGKkeanVYVIMGELSNQAAvQRTKDIEEVIA-TPDcsfIKIIDKQTSNWNRDE 199
Cdd:cd19969 98 --SYVGTDNYEAGYAAAEKLAELLGGKGK----VAVLTGPGQPNHE-ERVEGFKEAFAeYPG---IEVVAVGDDNDDPEK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 200 AQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVgGVDATQDALAAMQAGDLDATVFQDAAGQGAGALD 279
Cdd:cd19969 168 AAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTGKVKIV-AFDDDPETLDLIKDGVIDASIAQRPWMMGYWSLQ 246
|
250 260
....*....|....*....|....*...
gi 518701315 280 AALKLSKGEkVEHKVYVPFQLVTPANID 307
Cdd:cd19969 247 FLYDLANGL-VKDAWQTAGVNPLPPYVD 273
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
1-308 |
2.19e-11 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 63.61 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 1 MKKLLLGVAFA-ALISSSAFAAKIGVSMAkFDDNFLTVL---RNGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAAS 76
Cdd:PRK10355 3 IKNILLTLCASlLLTSVAAHAKEVKIGMA-IDDLRLERWqkdRDIFVKKAESL-GAKVFVQSANGNEETQMSQIENMINR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 77 GVDAIIVNPVDTsatQAMSDAAAAAK---IPLVYVNREPVNVnslpDNQAFVASNEADSGTLETKEVCRlfkeagKKEAN 153
Cdd:PRK10355 81 GVDVLVIIPYNG---QVLSNVIKEAKqegIKVLAYDRMINNA----DIDFYISFDNEKVGELQAKALVD------KVPQG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 154 VYVIMG--ELSNQAAVQRTKDIEEVIATPDCSFIKII-DKQTSNWNRDEAQNLMTNWLSTGK-KFDGVIANNDESAIGAI 229
Cdd:PRK10355 148 NYFLMGgsPVDNNAKLFRAGQMKVLKPYIDSGKIKVVgDQWVDGWLPENALKIMENALTANNnKIDAVVASNDATAGGAI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 230 QAMKAANIDMKsVVVGGVDATQDALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKVEH-------KVYVPFQLVT 302
Cdd:PRK10355 228 QALSAQGLSGK-VAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKAnttlnngLKDVPSRLLT 306
|
....*.
gi 518701315 303 PANIDK 308
Cdd:PRK10355 307 PIDVNK 312
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
44-305 |
3.67e-11 |
|
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: 62.69 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 44 AQAKGMS-GVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNREPVNVNSLpDNQ 122
Cdd:cd01540 21 AKKAAKElGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAGIPVIAVDDQLVDADPM-KIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 123 AFVASNEADSGTLETKEVCRLFKEAGKKEANVY----VIMGELSnqAAVQRTKDIEEVIATPDCSFIKIIDKQTSNWNRD 198
Cdd:cd01540 100 PFVGIDAYKIGEAVGEWLAKEMKKRGWDDVKEVgvlaITMDTLS--VCVDRTDGAKDALKAAGFPEDQIFQAPYKGTDTE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 199 EAQNLM----------TNWLstgkkfdgVIANNDESAIGAIQAMKAANIDMKSVVVGGVDATQ--DALAAMQAGDLDATV 266
Cdd:cd01540 178 GAFNAAnavitahpevKHWL--------VVGCNDEGVLGAVRALEQAGFDAEDIIGVGIGGYLaaDEEFKKQPTGFKASL 249
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 518701315 267 FQDAAGQGAGALDAALK-LSKGEKVEHKVYVPFQLVTPAN 305
Cdd:cd01540 250 YISPDKHGYIAAEELYNwITDGKPPPAETLTDGVIVTRDN 289
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
51-243 |
8.54e-10 |
|
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: 58.33 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 51 GVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNpvdTSATQAMSDAAAAAKIPLVYVNREPVNvNSLPdnqAFVAsNEA 130
Cdd:cd06288 30 GYLLLLANTGGDPELEAEAIRELLSRRVDGIIYA---SMHHREVTLPPELTDIPLVLLNCFDDD-PSLP---SVVP-DDE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 131 DSGTLETkevcRLFKEAGKKeaNVYVIMGELSNQAAVQRTKDIEEVIA----TPDCSFIKIidkqtSNWNRDEAQNLMTN 206
Cdd:cd06288 102 QGGYLAT----RHLIEAGHR--RIAFIGGPEDSLATRLRLAGYRAALAeagiPYDPSLVVH-----GDWGRESGYEAAKR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518701315 207 WLSTGKKFDGVIANNDESAIGAIQAMKAANI----DMkSVV 243
Cdd:cd06288 171 LLSAPDRPTAIFCGNDRMAMGVYQAAAELGLrvpeDL-SVV 210
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
33-288 |
9.67e-10 |
|
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: 58.41 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 33 NFLTVLRNGMIAQAKGMsGVEL-QVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPlVYVNRE 111
Cdd:cd06302 12 PYFDAAEEGAKKAAKEL-GVEVvYTGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIK-VITWDS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 112 PVNVNSlpdNQAFVasNEADSGTLETKEVCRLFKEAGKKeANVYVIMGELSNQAAVQRTKDIEEVIATpDCSFIKIIDKQ 191
Cdd:cd06302 90 DAPPSA---RDYFV--NQADDEGLGEALVDSLAKEIGGK-GKVAILSGSLTATNLNAWIKAMKEYLKS-KYPDIELVDTY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 192 TSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKsVVVGGVDATQDALAAMQAGDLDATVFQDAA 271
Cdd:cd06302 163 YTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGK-VAVTGIGLPNTARPYLKDGSVKEGVLWDPA 241
|
250
....*....|....*..
gi 518701315 272 GQGAGALDAALKLSKGE 288
Cdd:cd06302 242 KLGYLTVYAAYQLLKGK 258
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
22-303 |
2.11e-09 |
|
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.
Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 57.19 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGMSGVELQV------EDAQNDVAKQLDQIknfaASGVDAIIVNPVDTSATQAMS 95
Cdd:cd06307 1 RFGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLrihfvdSLDPEALAAALRRL----AAGCDGVALVAPDHPLVRAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 96 DAAAAAKIPLVYVnrepvnVNSLPDN--QAFVASNEADSGtletkevcR-----LFKEAGKKEANVYVIMGELSNQAAVQ 168
Cdd:cd06307 77 DELAARGIPVVTL------VSDLPGSrrLAYVGIDNRAAG--------RtaawlMGRFLGRRPGKVLVILGSHRFRGHEE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 169 RTKDIEEVIAT--PDCsfiKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAiGAIQAMKAANIDMKSVVVGG 246
Cdd:cd06307 143 REAGFRSVLRErfPDL---TVLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNE-GIARALREAGRARRVVFIGH 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 518701315 247 vDATQDALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKG-EKVEHKVYVPFQLVTP 303
Cdd:cd06307 219 -ELTPETRRLLRDGTIDAVIDQDPELQARRAIEVLLAHLGGkGPAPPQPPIPIEIITR 275
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
23-301 |
3.22e-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: 380508 [Multi-domain] Cd Length: 269 Bit Score: 53.77 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDNFLTVLRNGMIAQAKGmSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVdtSATQAMSDAAAAAK 102
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARE-RGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPA--RDDAPDLQELAARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 103 IPLVYVNRepvnvnSLPDNQA--FVASNEADsGTLETKEVCRLfkeaGKKEanVYVIMGELSNQAAVQRT----KDIEEV 176
Cdd:cd06285 79 VPVVLVDR------RIGDTALpsVTVDNELG-GRLATRHLLEL----GHRR--IAVVAGPLNASTGRDRLrgyrRALAEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 177 -IATPDCSFIKiidkqtSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANI----DMkSVVvgGVDATQ 251
Cdd:cd06285 146 gLPVPDERIVP------GGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLrvpeDL-SVV--GFDDIP 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 518701315 252 daLAAMQAGDLdATVFQDAAGQGAGALDAALKL--SKGEKVEHKVYVPfQLV 301
Cdd:cd06285 217 --LAAFLPPPL-TTVRQPKYEMGRRAAELLLQLieGGGRPPRSITLPP-ELV 264
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
51-291 |
3.54e-08 |
|
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: 53.81 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 51 GVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVdTSATQAMSDAAAAAKIPLVYVNR--EPVNVNSLPDNQAFVASN 128
Cdd:cd01391 32 GASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGS-SSVAIVIQNLAQLFDIPQLALDAtsQDLSDKTLYKYFLSVVFS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 129 EADSGTLETKEVCRLFKEAgkkeanVYVIMGELSNQAAVQRTKDIEEVIATPDCsfikIIDKQTSNWNRDE-AQNLMTNW 207
Cdd:cd01391 111 DTLGARLGLDIVKRKNWTY------VAAIHGEGLNSGELRMAGFKELAKQEGIC----IVASDKADWNAGEkGFDRALRK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 208 LSTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVgGVDATQDA--LAAMQAGDLDATVFQDAAGQGAGALDAALKLS 285
Cdd:cd01391 181 LREGLKARVIVCANDMTARGVLSAMRRLGLVGDVSVI-GSDGWADRdeVGYEVEANGLTTIKQQKMGFGITAIKAMADGS 259
|
....*.
gi 518701315 286 KGEKVE 291
Cdd:cd01391 260 QNMHEE 265
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
23-248 |
4.52e-08 |
|
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: 53.29 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDNFLtvlrnGMIaqakgMSGVELQVEDAQ---------NDVAKQLDQIKNFAASGVDAIIVNPVDTSATQA 93
Cdd:cd06270 2 IGLVVPDLSGPFF-----GSL-----LKGAERVARAHGkqllitsghHDAEEEREAIEFLLDRRCDAIILHSRALSDEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 94 MsdAAAAAKIPLVYVNRepvNVNSLPDnQAFVASNEAdSGTLETKEvcrLFkEAGKKeaNVYVIMGELSNQAAVQRTKDI 173
Cdd:cd06270 72 I--LIAEKIPPLVVINR---YIPGLAD-RCVWLDNEQ-GGRLAAEH---LL-DLGHR--RIACITGPLDIPDARERLAGY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 174 EEVIA----TPDCSFIKiidkqTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANI----DMkSVVvg 245
Cdd:cd06270 139 RDALAeagiPLDPSLII-----EGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIkvpeDV-SVI-- 210
|
...
gi 518701315 246 GVD 248
Cdd:cd06270 211 GFD 213
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
22-248 |
4.12e-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: 380513 [Multi-domain] Cd Length: 267 Bit Score: 50.31 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGMIAQAKGmSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVnpVDTSATQAMSDaAAAA 101
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAE-SGYTLIVSTSHWNADRELEILRLLLARKVDGIIV--VGGFGDEELLK-LLAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNREP-------VNVNSLpdNQAFVASN-------------EADSGTLETKE----VCRLFKEAGKKEANVYVI 157
Cdd:cd06290 77 GIPVVLVDRELeglnlpvVNVDNE--QGGYNATNhlidlghrrivhiSGPEDHPDAQEryagYRRALEDAGLEVDPRLIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 158 MGELSNQAAVQRTKdieeviatpdcsfiKIIDKqtsnwnrdeaqnlmtnwlstGKKFDGVIANNDESAIGAIQAMKAANI 237
Cdd:cd06290 155 EGDFTEESGYEAMK--------------KLLKR--------------------GGPFTAIFAANDLMALGAMKALREAGI 200
|
250
....*....|..
gi 518701315 238 DMKS-VVVGGVD 248
Cdd:cd06290 201 RVPDdVSVIGFD 212
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
34-301 |
2.82e-06 |
|
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: 47.92 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 34 FLTVLRnGMIAQAKGMsGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVnpVDTSATQAMSDAAAAaKIPLVYVNrEPV 113
Cdd:cd06284 14 YSEILR-GIEDAAAEA-GYDVLLGDTDSDPEREDDLLDMLRSRRVDGVIL--LSGRLDAELLSELSK-RYPIVQCC-EYI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 114 NVNSLPdnqaFVASNEADSGTLETKEVCRLfkeaGKKeaNVYVIMGELSNQAAVQRTK------------DIEEVIATPD 181
Cdd:cd06284 88 PDSGVP----SVSIDNEAAAYDATEYLISL----GHR--RIAHINGPLDNVYARERLEgyrralaeaglpVDEDLIIEGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 182 CSFikiidkqtsnwnrDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANI----DMkSVVvgGVDATqdALAAM 257
Cdd:cd06284 158 FSF-------------EAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLrvpeDV-SVI--GFDDI--EFAEM 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 518701315 258 QAGDLdATVFQDAAGQGAGALDAAL-KLSKGEKVEHKVYVPFQLV 301
Cdd:cd06284 220 FSPSL-TTIRQPRYEIGETAAELLLeKIEGEGVPPEHIILPHELI 263
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
23-301 |
3.71e-06 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 47.53 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDNFLTVLRNGMIA--QAKGMsGVELQVEDAQNDVAKQLDQIKNFaasGVDAIIVnpvdTSAT--QAMSDAA 98
Cdd:cd06278 2 VGVVVGDLSNPFYAELLEELSRalQARGL-RPLLFNVDDEDDVDDALRQLLQY---RVDGVIV----TSATlsSELAEEC 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 99 AAAKIPLVYVNR--EPVNVNSlpdnqafVASNEADSGtletKEVCRLFKEAGKKeaNVYVIMGELSNQAAVQRTKDIEEV 176
Cdd:cd06278 74 ARRGIPVVLFNRvvEDPGVDS-------VSCDNRAGG----RLAADLLLAAGHR--RIAFLGGPEGTSTSRERERGFRAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 177 IATPDCSFIKIIDKQTSnwnRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANI-----DMkSVVvgGVDATq 251
Cdd:cd06278 141 LAELGLPPPAVEAGDYS---YEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGlvvpeDI-SVV--GFDDI- 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 518701315 252 dALAAMQAGDLdATVFQDAAGQGAGALDAALKLSKGEKVEH-KVYVPFQLV 301
Cdd:cd06278 214 -PMAAWPSYDL-TTVRQPIEEMAEAAVDLLLERIENPETPPeRRVLPGELV 262
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
55-291 |
6.41e-06 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380656 Cd Length: 296 Bit Score: 46.89 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 55 QVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIplVYVNREPVNV-NSLPDNQAFvasNEADSG 133
Cdd:cd20001 34 QIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDAGI--VVITHEASNLkNVDYDVEAF---DNAAYG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 134 TLetkeVCRLFKEAGKKEANVYVIMGELSN-------QAAVQRTK----DIEEViatpdcsfikiIDKQTSNWNRDEAQN 202
Cdd:cd20001 109 AF----IMDKLAEAMGGKGKYVTFVGSLTStshmewaNAAVAYQKanypDMLLV-----------TDRVETNDDSETAYE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 203 LMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGG--VDATQDALAamqAGDLDATVFQDAAGQGAGALDA 280
Cdd:cd20001 174 KAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGKIAVVGTglPSVAGEYLE---DGTIDYIQFWDPADAGYAMNAL 250
|
250
....*....|.
gi 518701315 281 ALKLSKGEKVE 291
Cdd:cd20001 251 AVMVLEGEKIT 261
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
61-243 |
7.21e-06 |
|
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: 46.48 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 61 NDVAKQLDQIKNFAASGVDAIIVNPVdTSATQAMSDaAAAAKIPLVYVNREpvnvnsLPDNQAFVASneADSGTLETKEV 140
Cdd:cd06280 39 EDPEKEKRYLDSLLSKQVDGIILAPS-AGPSRELKR-LLKHGIPIVLIDRE------VEGLELDLVA--GDNREGAYKAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 141 CRLFkEAGKKEanVYVIMGELSNQAAVQRTKDIEEVIA----TPDCSFIKiidkqTSNWNRDEAQNLMTNWLSTGKKFDG 216
Cdd:cd06280 109 KHLI-ELGHRR--IGLITGPLEISTTRERLAGYREALAeagiPVDESLIF-----EGDSTIEGGYEAVKALLDLPPRPTA 180
|
170 180 190
....*....|....*....|....*....|
gi 518701315 217 VIANNDESAIGAIQAMKAANIDMK---SVV 243
Cdd:cd06280 181 IFATNNLMAVGALRALRERGLEIPqdiSVV 210
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
23-239 |
7.90e-06 |
|
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: 46.39 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDNFLTVLRNGM--IAQAKGMSGVelqVEDAQNDVAKQLDQIKNFAASGVDAIIVNPvdTSATQAMSDAAAA 100
Cdd:cd06283 2 IGVIVADITNPFSSLLLKGIedVCREAGYQLL---ICNSNNDPEKERDYIESLLSQRVDGLILQP--TGNNNDAYLELAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 101 AKIPLVYVNREpvnvnSLPDNQAFVASNEADSgtleTKEVCRLFKEAGKKeaNVYVIMGELSN------------QAAVQ 168
Cdd:cd06283 77 KGLPVVLVDRQ-----IEPLNWDTVVTDNYDA----TYEATEHLKEQGYE--RIVFVTEPIKGistrrerlqgflDALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518701315 169 RTKDIEEViatpdcsfikIIDKQTSNWNRDEAQNLMTNwlSTGKKFdGVIANNDESAIGAIQAMKAANIDM 239
Cdd:cd06283 146 YNIEGDVY----------VIEIEDTEDLQQALAAFLSQ--HDGGKT-AIFAANGVVLLRVLRALKALGIRI 203
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
22-263 |
1.30e-05 |
|
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: 45.96 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 22 KIGVSMAKFDDNFLTVLRNGM--IAQAKGMSGVELQVEDAQNDVAKQLDQIKnfaASGVDAIIVNPVDTS--ATQAMSDA 97
Cdd:pfam00532 3 KLGALVPQLDEPFFQDLVKGItkAAKDHGFDVFLLAVGDGEDTLTNAIDLLL---ASGADGIIITTPAPSgdDITAKAEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 98 AAaakIPLVYVNREPVNVNSLPdnQAFVASNEAdsGTLETKEvcrLFKEAGKKEanVYVIMGELSNQAAVQRTKDIEEVI 177
Cdd:pfam00532 80 YG---IPVIAADDAFDNPDGVP--CVMPDDTQA--GYESTQY---LIAEGHKRP--IAVMAGPASALTARERVQGFMAAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 178 AtpDCSF-IKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAAN-IDMKSVVVGGVDATQ--DA 253
Cdd:pfam00532 148 A--AAGReVKIYHVATGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIVGIGINSVVgfDG 225
|
250
....*....|
gi 518701315 254 LAAMQAGDLD 263
Cdd:pfam00532 226 LSKAQDTGLY 235
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
60-301 |
1.82e-05 |
|
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: 45.18 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 60 QNDVAKQLDQIKNFAASGVDAIIVNPvdTSATQAMSDAAAAAKIPLVYVNREPVNVNSL--PDNQAfvasneadsgtleT 137
Cdd:cd01542 38 NLDEEREIEYLETLARQKVDGIILFA--TEITDEHRKALKKLKIPVVVLGQEHEGFSCVyhDDYGA-------------G 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 138 KEVCRLFKEAGKKEAnVYVIMGELSNQAAVQRTKDIEEVIATpdcSFIKIIDKQTSNWNRDEAQNLMTNWLSTgKKFDGV 217
Cdd:cd01542 103 KLLGEYLLKKGHKNI-AYIGVDEEDIAVGVARKQGYLDALKE---HGIDEVEIVETDFSMESGYEAAKELLKE-NKPDAI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 218 IANNDESAIGAIQAMKAANIDM-KSVVVGGVDATQdaLAAMQAGDLdATV--FQDAAGQGAGALdaALKLSKGEKVEHKV 294
Cdd:cd01542 178 ICATDNIALGAIKALRELGIKIpEDISVAGFGGYD--LSEFVSPSL-TTVkfDYEEAGEKAAEL--LLDMIEGEKVPKKQ 252
|
....*..
gi 518701315 295 YVPFQLV 301
Cdd:cd01542 253 KLPYELI 259
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
196-301 |
1.92e-05 |
|
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: 45.23 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 196 NRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMKS--VVVGgvdatQDALAAMQAGDLdATVFQDAAGQ 273
Cdd:cd06286 160 TIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEdlAVIG-----FDNQPISELLNL-TTIDQPLEEM 233
|
90 100
....*....|....*....|....*...
gi 518701315 274 GAGALDAALKLSKGEKVEHKVYvPFQLV 301
Cdd:cd06286 234 GKEAFELLLSQLESKEPTKKEL-PSKLI 260
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
29-286 |
4.37e-05 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380628 [Multi-domain] Cd Length: 285 Bit Score: 44.38 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 29 KFDDN-FLTVLRNGMIAQAKGMsGVELQVEDAQ--NDVAKQLDQIKNFAASGVDAIIVNPVDTsatQAMSDAAAAAKIPL 105
Cdd:cd19973 7 KTDTNpFFVKMKEGAQKAAKAL-GIKLMTAAGKidGDNATQVTAIENMIAAGAKGILITPSDT---KAIVPAVKKARDAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 106 VYVnrepVNVNSLPDNQ----AFVASNEADSGTLetkeVCRLFKEA-GKKEANVYVIMGELSNQAAVQRTK--------D 172
Cdd:cd19973 83 VLV----IALDTPTDPIdaadATFATDNFKAGVL----IGEWAKAAlGAKDAKIATLDLTPGHTVGVLRHQgflkgfgiD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 173 IEEVIATPDCSFIKIIDKQTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDmKSVVVGGVDATQD 252
Cdd:cd19973 155 EKDPESNEDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKE-KGVLIVSVDGGCP 233
|
250 260 270
....*....|....*....|....*....|....
gi 518701315 253 ALAAMQAGDLDATVFQDAAGQGAGALDAALKLSK 286
Cdd:cd19973 234 GVKDVKDGIIGATSQQYPLRMAALGVEAIAAFAK 267
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
194-237 |
4.70e-05 |
|
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: 44.05 E-value: 4.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 518701315 194 NWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANI 237
Cdd:cd01544 159 EFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGI 202
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
23-302 |
5.84e-05 |
|
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: 43.80 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDN-FLTVLRnGMIAQAKGmSGVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDtsATQAMSDAAAAA 101
Cdd:cd06296 2 IDLVLPQLDSPyALEVLR-GVERAAAA-AGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSD--PTSRQLRLLRSA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 102 KIPLVYVNrePVNvnSLPDNQAFVASNEADSGTLETKEVCRLfkeaGKKeaNVYVIMGELSNQAAVQRTKD----IEEVI 177
Cdd:cd06296 78 GIPFVLID--PVG--EPDPDLPSVGATNWAGGRLATEHLLDL----GHR--RIAVITGPPRSVSGRARLAGyraaLAEAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 178 ATPDCSFIKIIDkqtsnWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANI----DMkSVVvgGVDatqDA 253
Cdd:cd06296 148 IAVDPDLVREGD-----FTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLrvpdDL-SVI--GFD---DT 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 518701315 254 LAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGEKV-EHKVYVPFQLVT 302
Cdd:cd06296 217 PPARWTSPPLTTVHQPLREMGAVAVRLLLRLLEGGPPdARRIELATELVV 266
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
23-301 |
1.33e-04 |
|
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: 42.93 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 23 IGVSMAKFDDNFLTVLRNGM--IAQAKGMSgveLQVEDAQNDVAKQLDQIKNFAASGVDAIIVnpvdTSA--TQAMSDAA 98
Cdd:cd19975 2 IGVIIPDISNSFFAEILKGIedEARENGYS---VILCNTGSDEEREKKYLQLLKEKRVDGIIF----ASGtlTEENKQLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 99 AAAKIPLVYVNREpVNVNSLPdnqaFVASNEADSGtletKEVCRLFKEAGKKeaNVYVIMGELSN-QAAVQRTKDIEEVI 177
Cdd:cd19975 75 KNMNIPVVLVSTE-SEDPDIP----SVKIDDYQAA----YDATNYLIKKGHR--KIAMISGPLDDpNAGYPRYEGYKKAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 178 ATPDcsfIKIIDK--QTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDM-KSVVVGGVDATQdaL 254
Cdd:cd19975 144 KDAG---LPIKENliVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVpEDISVIGFDNTE--I 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 518701315 255 AAMQAGDLdATVFQDAAGQGAGALDAALKLSKGEKVEHK-VYVPFQLV 301
Cdd:cd19975 219 AEMSIPPL-TTVSQPFYEMGKKAVELLLDLIKNEKKEEKsIVLPHQII 265
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
214-301 |
2.36e-04 |
|
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: 41.80 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 214 FDGVIANNDESAIGAIQAMKAANI----DMkSVVvgGVDATQDalAAMQAGDLDaTVFQDAAGQGAGALDAALKLSKGEK 289
Cdd:cd01574 175 VTAVFAANDQMALGALRALHERGLrvpeDV-SVV--GFDDIPE--AAYFVPPLT-TVRQDFAELGRRAVELLLALIEGPA 248
|
90
....*....|...
gi 518701315 290 -VEHKVYVPFQLV 301
Cdd:cd01574 249 pPPESVLLPPELV 261
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
62-253 |
3.00e-04 |
|
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: 41.78 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 62 DVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMsDAAAAAKIPLVYVNREpvnvnsLPDNQA-FVASNEADSGTLETKev 140
Cdd:cd06289 40 DPERQRRFLRRMLEQGVDGLILSPAAGTTAELL-RRLKAWGIPVVLALRD------VPGSDLdYVGIDNRLGAQLATE-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 141 cRLFKEAGKKEAnvyVIMGELSNQAAVQRTKDIEEVIATPDCSFI--KIIDKQTSNWN-RDEAQNLMTNwlstGKKFDGV 217
Cdd:cd06289 111 -HLIALGHRRIA---FLGGLSDSSTRRERLAGFRAALAEAGLPLDesLIVPGPATREAgAEAARELLDA----APPPTAV 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 518701315 218 IANNDESAIGAIQAMKAANIDM-KSVVVGGVDATQDA 253
Cdd:cd06289 183 VCFNDLVALGAMLALRRRGLEPgRDIAVVGFDDVPEA 219
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
52-290 |
1.13e-03 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 39.89 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 52 VELQVEDAQNDVAKQLDQIKNFAASGVDAIIVnpVDTSATQAMsdAAAAAKIPLVY--VNRepvnvnslPDNQAFVASNE 129
Cdd:COG2984 36 LKLDYQNAQGDQATAAQIAAKLVADKPDLIVA--IGTPAAQAA--ANATKDIPVVFtaVTD--------PVGAGLVKSLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 130 AD----SGTLET---KEVCRLFKEAGKKEANVYVIMGElSNQAAVQRTKDIEEVIATPDCSFIKIIDKQTSNWnRDEAQN 202
Cdd:COG2984 104 KPggnvTGVSDLlpiEKQLELIKKLLPDAKRIGVLYNP-SEANSVAQVEELKKAAKKLGLELVEATVTSSNEI-QQALQS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 203 LMtnwlstgKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGGVDatqdalAAMQAGDLdATVFQDAAGQGAGALDAAL 282
Cdd:COG2984 182 LA-------GKVDAIYVPTDNTVVSALEAIAKVAARAKIPVFGGDD------SSVKAGAL-AGYGIDYYELGRQAAEMAL 247
|
....*...
gi 518701315 283 KLSKGEKV 290
Cdd:COG2984 248 RILKGEKP 255
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
41-93 |
1.28e-03 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 39.93 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 518701315 41 GMIAQAKGMsGVELQVEDAQN--DVAKQLDQIKNFAASGVDAIIVNPVDTSATQA 93
Cdd:PRK10936 67 GMVEEAKRL-GVDLKVLEAGGyyNLAKQQQQLEQCVAWGADAILLGAVTPDGLNP 120
|
|
| PBP1_ABC_sugar_binding-like |
cd06315 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
38-302 |
1.97e-03 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380538 Cd Length: 278 Bit Score: 39.25 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 38 LRN-GMIAQAKGMS------GVELQVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIPLVYVNR 110
Cdd:cd06315 10 LRNgGVLGVGRGVKeaaaalGWKVDVLDGGGTVTGRLAALNQALALKPDGIILGGDDAVELQEPLKKAVKAGIPVVGWHA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 111 EPVnvnSLPDNQAFVASNeADSGTLETKEVCRLFKEA-GKKEANVyVIMGELSNQAAVQRTKDIEEVI-ATPDCSFIKII 188
Cdd:cd06315 90 AAS---PGPIPELGLFTN-ITTDPREVAETAAALVIAqSGGKAGV-VIFTDSRYAIATAKANAMKKAIeACSGCKVLEYV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 189 DKQTSnwnrDEAQ---NLMTNWLST-GKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGGVDATQDALAAMQAGDLD- 263
Cdd:cd06315 165 DIPIA----DTAQrmpKLIRSLLQRyGDRWTHTLAINDLYFDFAAPALRAAGVEADPVNISAGDGSPSAYDRIRAGEYQv 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 518701315 264 ATVFQDAAGQGAGALDAALKLSKGEKVEHkvYV-PFQLVT 302
Cdd:cd06315 241 ATVAEPLTLQGWQLVDELNRALAGEPPSG--YVqPVHLVT 278
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
55-291 |
2.05e-03 |
|
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: 39.22 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 55 QVEDAQNDVAKQLDQIKNFAASGVDAIIVNPVDTSATQAMSDAAAAAKIpLVYVNREPVNVNS-----LPDNQAFvasne 129
Cdd:cd20002 34 QVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGI-VVITHESPGQKGAdwdveLIDNEKF----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 130 adsGTLETKEVCRLFKEAGKkeanvYVIM-GELSNQAAVQRTKDIEEVIATPDCSFIKIIDKQTSNWNRDEAQNLMTNWL 208
Cdd:cd20002 108 ---GEAQMELLAKEMGGKGE-----YAIFvGSLTVPLHNLWADAAVEYQKEKYPNMKQVTDRIPGGEDVDVSRQTTLELL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 209 STGKKFDGVIANNDESAIGAIQAMKAANIDMKSVVVGGVDATQdALAAMQAGDLDATVFQDAAGQGAGALDAALKLSKGE 288
Cdd:cd20002 180 KAYPDLKGIISFGSLGPIGAGQALREKGLKGKVAVVGTVIPSQ-AAAYLKEGSITEGYLWDPADAGYAMVYIAKMLLDGK 258
|
...
gi 518701315 289 KVE 291
Cdd:cd20002 259 RKE 261
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
59-237 |
3.50e-03 |
|
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: 38.38 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 59 AQNDVAKQLDQIKNFAASGVDAIIVNPVDTSaTQAMSDAAAAAKIPLVYVNRepvnvNSLPDNQAFVASNEADSGTLETK 138
Cdd:cd19976 37 TYNDFEREKKYIQELKERNVDGIIIASSNIS-DEAIIKLLKEEKIPVVVLDR-----YIEDNDSDSVGVDDYRGGYEATK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 139 evcrLFKEAGKKeaNVYVIMGELSNQAAVQRTKDIEEVIATPDCSFIKIIDKQTSNWNRDEAQnlMTNWLSTGKKFDGVI 218
Cdd:cd19976 111 ----YLIELGHT--RIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGESSLEGGYK--AAEELLKSKNPTAIF 182
|
170
....*....|....*....
gi 518701315 219 ANNDESAIGAIQAMKAANI 237
Cdd:cd19976 183 AGNDLIAMGVYRAALELGL 201
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
195-302 |
4.16e-03 |
|
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: 37.32 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 195 WNRDEAQNLMTNWLS-TGKKFDGVIANNDESAIGAIQAMKAANI----DMKsvVVGGVDatqDALAAMQAGDLDaTVFQD 269
Cdd:pfam13377 49 GDDEAEAAAARERLRwLGALPTAVFVANDEVALGVLQALREAGLrvpeDLS--VIGFDD---SPLAALVSPPLT-TVRVD 122
|
90 100 110
....*....|....*....|....*....|....
gi 518701315 270 AAGQGAGALDAALK-LSKGEKVEHKVYVPFQLVT 302
Cdd:pfam13377 123 AEELGRAAAELLLDlLNGEPAPPERVLLPPELVE 156
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
191-302 |
8.70e-03 |
|
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: 37.19 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518701315 191 QTSNWNRDEAQNLMTNWLSTGKKFDGVIANNDESAIGAIQAMKAANIDMK---SVVvgGVDATQDALAAMQagDLdATVF 267
Cdd:cd06279 173 EAPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPedlSVT--GFDDIPEAAAADP--GL-TTVR 247
|
90 100 110
....*....|....*....|....*....|....*
gi 518701315 268 QDAAGQGAGALDAALKLSKGEKVEHKVYvPFQLVT 302
Cdd:cd06279 248 QPAVEKGRAAARLLLGLLPGAPPRPVIL-PTELVV 281
|
|
| |
