|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
22-292 |
6.93e-134 |
|
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: 380.42 E-value: 6.93e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 22 EKIGVSMAYFDQNFLTIIRQSIEKEAQA-RHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQ 100
Cdd:cd06301 1 IKIGVSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 101 AKMPLVYVNRTPGDKtlPPGVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKV 180
Cdd:cd06301 81 AGIPLVYVNREPDSK--PKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYPGMKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 181 VQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKK--LLIGGIDATPDGLKALASDKIQVTVFQ 258
Cdd:cd06301 159 VAEQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKddILVAGIDATPDALKAMKAGRLDATVFQ 238
|
250 260 270
....*....|....*....|....*....|....
gi 488999782 259 DAVGQGKTALAVALKLIKGEKVESHVWIPFELVT 292
Cdd:cd06301 239 DAAGQGETAVDVAVKAAKGEEVESDIWIPFELVT 272
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
23-296 |
1.03e-80 |
|
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: 246.76 E-value: 1.03e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:COG1879 35 TIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPGDktlPPGVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQ 182
Cdd:COG1879 115 IPVVTVDSDVDG---SDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANERTDGFKEALKEYPGIKVVA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 183 KQPANYSRSEGMDLMQNW-TGNGEaIDIVAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVTVFQD 259
Cdd:COG1879 192 EQYADWDREKALEVMEDLlQAHPD-IDGIFAANDGMALGAAQALKAAgrKGDVKVVGFDGSPEALQAIKDGTIDATVAQD 270
|
250 260 270
....*....|....*....|....*....|....*..
gi 488999782 260 AVGQGKTALAVALKLIKGEKVESHVWIPFELVTKENM 296
Cdd:COG1879 271 PYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
23-290 |
3.09e-76 |
|
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: 234.00 E-value: 3.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPGDKtlPPGVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQ 182
Cdd:cd01536 81 IPVVAVDTDIDGG--GDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYPDIEIVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 183 KQPANYSRSEGMDLMQNW-TGNGEaIDIVAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVTVFQD 259
Cdd:cd01536 159 EQPANWDRAKALTVTENLlQANPD-IDAVFAANDDMALGAAEALKAAgrTGDIKIVGVDGTPEALKAIKDGELDATVAQD 237
|
250 260 270
....*....|....*....|....*....|.
gi 488999782 260 AVGQGKTALAVALKLIKGEKVESHVWIPFEL 290
Cdd:cd01536 238 PYLQGYLAVEAAVKLLNGEKVPKEILTPVTL 268
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
23-300 |
6.90e-74 |
|
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: 228.31 E-value: 6.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPGDKTLppgVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQ 182
Cdd:cd06313 81 IPLVGVNALIENEDL---TAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYPDIKVLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 183 KQPANYSRSEGMDLMQNW-TGNGEAIDIVAANNDEMAIGAAMALEKS-QKKLLIGGIDATPDGLKALASDKIQVTVFQDA 260
Cdd:cd06313 158 EQTANWSRDEAMSLMENWlQAYGDEIDGIIAQNDDMALGALQAVKAAgRDDIPVVGIDGIEDALQAVKSGELIATVLQDA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488999782 261 VGQGKTALAVALKLIKGEKVESHVWIPFELVTKENMQTYV 300
Cdd:cd06313 238 EAQGKGAVEVAVDAVKGEGVEKKYYIPFVLVTKDNVDDYL 277
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
23-291 |
1.37e-57 |
|
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: 186.21 E-value: 1.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAqARH--VDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQ 100
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEA-AKYpnVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 101 AKMPLVYVNR-TPGDKTLppgvVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMK 179
Cdd:cd06308 80 AGIPVIVLDRkVSGDDYT----AFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYPGIK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVTVF 257
Cdd:cd06308 156 IVASQDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAgrEKEIKIIGVDGLPEAGEKAVKDGILAATF 235
|
250 260 270
....*....|....*....|....*....|....
gi 488999782 258 QDAVGqGKTALAVALKLIKGEKVESHVWIPFELV 291
Cdd:cd06308 236 LYPTG-GKEAIEAALKILNGEKVPKEIVLPTPLI 268
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
23-302 |
2.18e-57 |
|
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: 186.27 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRT--PGDKTLPpgVVFVGSDERESGTLQMEALAK-LANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMK 179
Cdd:cd06309 81 IPVILVDRTidGEDGSLY--VTFIGSDFVEEGRRAAEWLVKnYKGGKGNVVELQGTAGSSVAIDRSKGFREVIKKHPNIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQKQPANYSRSEGMDLMQNW-TGNGEAIDIVAANNDEMAIGAAMALE----KSQKKLLIGGIDATPDGLKALASDKIQV 254
Cdd:cd06309 159 IVASQSGNFTREKGQKVMENLlQAGPGDIDVIYAHNDDMALGAIQALKeaglKPGKDVLVVGIDGQKDALEAIKAGELNA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 488999782 255 TVfQDAVGQGKTALAVALKLIKGEKVESHVWIPFELVTKENMQTYVEK 302
Cdd:cd06309 239 TV-ECNPLFGPTAFDTIAKLLAGEKVPKLIIVEERLFDKDNAAEELEP 285
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
23-289 |
8.26e-57 |
|
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: 185.10 E-value: 8.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARH-VDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQA 101
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGkIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 102 KMPLVYVNRTPGDKTLP--PGVVFVGSDERESGTLQMEALAKLANYKGNVA---------IMI-GNLTDAGALQRTKDVE 169
Cdd:cd01539 82 NIPVIFFNREPSREDLKsyDKAYYVGTDAEESGIMQGEIIADYWKANPEIDkngdgkiqyVMLkGEPGHQDAIARTKYSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 170 QVVAKY-PAMKVVQKQPANYSRSEGMDLMQNW-TGNGEAIDIVAANNDEMAIGAAMALEK-------SQKKLLIGGIDAT 240
Cdd:cd01539 162 KTLNDAgIKTEQLAEDTANWDRAQAKDKMDAWlSKYGDKIELVIANNDDMALGAIEALKAagyntgdGDKYIPVFGVDAT 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 488999782 241 PDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGE---------KVESH-VWIPFE 289
Cdd:cd01539 242 PEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKepletgykfLVEGKyVRIPYK 300
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
23-292 |
1.23e-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: 170.94 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNR-TPGDKTlppgVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVV 181
Cdd:cd06323 81 IPVITVDRsVTGGKV----VSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAKYPKINVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 182 QKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALE-KSQKKLLIGGIDATPDGLKALASDKIQVTVFQDA 260
Cdd:cd06323 157 ASQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKaAGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQP 236
|
250 260 270
....*....|....*....|....*....|..
gi 488999782 261 VGQGKTALAVALKLIKGEKVESHVWIPFELVT 292
Cdd:cd06323 237 EEMGAKAVETADKYLKGEKVPKKIPVPLKLVT 268
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
24-279 |
7.62e-50 |
|
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: 165.95 E-value: 7.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFE-DARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVgPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPGDktlPPGVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAK-YPAMKVV 181
Cdd:pfam13407 81 IPVVTFDSDAPS---SPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEkYPGIKVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 182 QK-QPANYSRSEGMDLMQNW-TGNGEAIDIVAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVTVF 257
Cdd:pfam13407 158 AEvEGTNWDPEKAQQQMEALlTAYPNPLDGIISPNDGMAGGAAQALEAAglAGKVVVTGFDATPEALEAIKDGTIDATVL 237
|
250 260
....*....|....*....|..
gi 488999782 258 QDAVGQGKTALAVALKLIKGEK 279
Cdd:pfam13407 238 QDPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
24-292 |
1.87e-46 |
|
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: 157.44 E-value: 1.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKM 103
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 104 PLVYVN-RTPGDKTlppgVVFVGSDERESGTLQMEALAK-LANYKGNVAImIGNLTDAGALQRTKDVEQVVAKYPAMKVV 181
Cdd:cd06322 82 PVFTVDvKADGAKV----VTHVGTDNYAGGKLAGEYALKaLLGGGGKIAI-IDYPEVESVVLRVNGFKEAIKKYPNIEIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 182 QKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEK--SQKKLLIGGIDATPDGLKALASD-KIQVTVFQ 258
Cdd:cd06322 157 AEQPGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESagKEDKIKVIGFDGNPEAIKAIAKGgKIKADIAQ 236
|
250 260 270
....*....|....*....|....*....|....
gi 488999782 259 DAVGQGKTALAVALKLIKGEKVESHVWIPFELVT 292
Cdd:cd06322 237 QPDKIGQETVEAIVKYLAGETVEKEILIPPKLYT 270
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
23-292 |
1.14e-45 |
|
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: 155.29 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPGDKtlpPGVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQ 182
Cdd:cd19972 81 IPVIAVDRNPEDA---PGDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAEAPGIKVVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 183 KQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALE--KSQKKLLIGGIDATPDGLKALASDKIQVTVFQDA 260
Cdd:cd19972 158 EQTADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKvaGLDHKIWVVGFDGDVAGLKAVKDGVLDATMTQQT 237
|
250 260 270
....*....|....*....|....*....|..
gi 488999782 261 VGQGKTALAVALKLIKGEKVESHVWIPFELVT 292
Cdd:cd19972 238 QKMGRLAVDSAIDLLNGKAVPKEQLQDAVLTT 269
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
23-292 |
4.44e-45 |
|
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: 154.08 E-value: 4.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPGDKTLppgVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQ 182
Cdd:cd19968 81 IPVVTVDRRAEGAAP---VPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAAGPKIKVVF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 183 KQPANYSRSEGMDLMQN-WTGNGEAIDIVAANNDEMAIGAAMALEKS---QKKLLIGGIDATPDGLKALASDKIQVTVFQ 258
Cdd:cd19968 158 EQTGNFERDEGLTVMENiLTSLPGPPDAIICANDDMALGAIEAMRAAgldLKKVKVIGFDAVPDALQAIKDGELYATVEQ 237
|
250 260 270
....*....|....*....|....*....|....
gi 488999782 259 DAVGQGKTALAVALKLIKGEKVESHVWIPFELVT 292
Cdd:cd19968 238 PPGGQARTALRILVDYLKDKKAPKKVNLKPKLIT 271
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
23-290 |
1.10e-44 |
|
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: 152.74 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSmaYFDQN--FLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQ 100
Cdd:cd19971 1 KFGFS--YMTMNnpFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 101 AKMPLVYVNRTPGDKTLppgVV-FVGSDERESGTLQMEALAKLANYKGNVAImIGNLTDAGALQRTKDVEQVVAKYPAMK 179
Cdd:cd19971 79 AGIPVINVDTPVKDTDL---VDsTIASDNYNAGKLCGEDMVKKLPEGAKIAV-LDHPTAESCVDRIDGFLDAIKKNPKFE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQK--KLLIGGIDATPDGLKALASDKIQVTVF 257
Cdd:cd19971 155 VVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKlgDILVYGVDGSPDAKAAIKDGKMTATAA 234
|
250 260 270
....*....|....*....|....*....|...
gi 488999782 258 QDAVGQGKTALAVALKLIKGEKVESHVWIPFEL 290
Cdd:cd19971 235 QSPIEIGKKAVETAYKILNGEKVEKEIVVPTFL 267
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
23-281 |
6.68e-44 |
|
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: 151.20 E-value: 6.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd19992 1 KIGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPGDKTLPpgvVFVGSDERESGTLQMEALAKlANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPA---MK 179
Cdd:cd19992 81 VPVISYDRLILNADVD---LYVGRDNYKVGQLQAEYALE-AVPKGNYVILSGDPGDNNAQLITAGAMDVLQPAIDsgdIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQKQPA-NYSRSEGMDLMQNW-TGNGEAIDIVAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVT 255
Cdd:cd19992 157 IVLDQYVkGWSPDEAMKLVENAlTANNNNIDAVLAPNDGMAGGAIQALKAQglAGKVFVTGQDAELAALKRIVEGTQTMT 236
|
250 260
....*....|....*....|....*.
gi 488999782 256 VFQDAVGQGKTALAVALKLIKGEKVE 281
Cdd:cd19992 237 VWKDLKELARAAADAAVKLAKGEKPQ 262
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
23-296 |
2.98e-41 |
|
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: 144.33 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHV--DVQFEDARGDTGRQADQVQSFIASGVDAIIVDPV-DSASTPQLTKmAQ 99
Cdd:cd06320 1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVkvDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPIsDTNLIPPIEK-AN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 100 QAKMPLVYVNRTPGDKTLP----PGVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKY 175
Cdd:cd06320 80 KKGIPVINLDDAVDADALKkaggKVTSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 176 PAMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQ 253
Cdd:cd06320 160 PGLKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAgkTGKVLVVGTDGIPEAKKSIKAGELT 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 488999782 254 VTVFQDAVGQGKTALAVALKLIKGEKVESHVWIPFELVTKENM 296
Cdd:cd06320 240 ATVAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKDNV 282
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
23-295 |
6.60e-35 |
|
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: 127.53 E-value: 6.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPgdKTLPPGVVFVGSDERESGTLQ-MEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPA---- 177
Cdd:cd06318 81 IPVITVDSAL--DPSANVATQVGRDNKQNGVLVgKEAAKALGGDPGKIIELSGDKGNEVSRDRRDGFLAGVNEYQLrkyg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 178 ---MKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALE--KSQKKLLIGGIDATPDGLKALASDKI 252
Cdd:cd06318 159 ksnIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKaaGMLDKVKVAGADGQKEALKLIKDGKY 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488999782 253 QVTVFQDAVGQGKTALAVALKLIKGE-KVESHVWIPFELVTKEN 295
Cdd:cd06318 239 VATGLNDPDLLGKTAVDTAAKVVKGEeSFPEFTYTPTALITKDN 282
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
23-292 |
9.48e-35 |
|
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: 127.02 E-value: 9.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARH--VDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQ 100
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINpgAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 101 AKMPLVYVNrTPGDktlpPGVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAgALQRTKDVEQVVAKYPAMKV 180
Cdd:cd06321 81 AGIIVVAVD-VAAE----GADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPPVSA-VIDRVNGCKEALAEYPGIKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 181 VQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKK-LLIGGIDATPDGLKALASDK--IQVTVF 257
Cdd:cd06321 155 VDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDdIVITSVDGSPEAVAALKREGspFIATAA 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 488999782 258 QDAVGQGKTALAVALKLIKGEKV-ESHVWIPFELVT 292
Cdd:cd06321 235 QDPYDMARKAVELALKILNGQEPaPELVLIPSTLVT 270
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
42-292 |
4.19e-34 |
|
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: 125.13 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 42 SIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTLppGV 121
Cdd:cd19967 20 GAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLIDREINAEGV--AV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 122 VFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQKQPANYSRSEGMDLMQNWT 201
Cdd:cd19967 98 AQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQYPELKMVAQQSADWDRTEAFEKMESIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 202 GNGEAIDIVAANNDEMAIGAAMALEKSQK--KLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGEK 279
Cdd:cd19967 178 QANPDIKGVICGNDEMALGAIAALKAAGRagDVIIVGFDGSNDVRDAIKEGKISATVLQPAKLIARLAVEQADQYLKGGS 257
|
250
....*....|....*
gi 488999782 280 --VESHVWIPFELVT 292
Cdd:cd19967 258 tgKEEKQLFDCVLIT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
23-295 |
1.60e-33 |
|
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: 124.01 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVY--VNRTPGDKtlppgVVFVGSDERESGTLQMEALAKLANYKG----NVAIMIGNLTDAGALQRTKDVEQVVAKYP 176
Cdd:cd06319 81 IPVVIadIGTGGGDY-----VSYIISDNYDGGYQAGEYLAEALKENGwgggSVGIIAIPQSRVNGQARTAGFEDALEEAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 177 AMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQK--KLLIGGIDATPDGLKALASDKIQV 254
Cdd:cd06319 156 VEEVALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRtgDILVVGFDGDPEALDLIKDGKLDG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488999782 255 TVFQDAVGQGKTALAVALKLIKGEK-VESHVWIPFELVTKEN 295
Cdd:cd06319 236 TVAQQPFGMGARAVELAIQALNGDNtVEKEIYLPVLLVTSEN 277
|
|
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
23-296 |
3.63e-33 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 124.07 E-value: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEA-QARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQA 101
Cdd:PRK15395 26 RIGVTIYKYDDNFMSVVRKAIEKDAkAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAPTVIEKARGQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 102 KMPLVYVNRTPGDKTLPP--GVVFVGSDERESGTLQMEALAKlaNYKGNVAImigNLTDAGALQ---------------R 164
Cdd:PRK15395 106 DVPVVFFNKEPSRKALDSydKAYYVGTDSKESGIIQGDLIAK--HWKANPAW---DLNKDGKIQyvllkgepghpdaeaR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 165 TKDV-EQVVAKYPAMKVVQKQPANYSRSEGMDLMQNW--TGNGEAIDIVAANNDEMAIGAAMALEKSQK-KLLIGGIDAT 240
Cdd:PRK15395 181 TTYViKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWlsGPNANKIEVVIANNDAMAMGAVEALKAHNKsSIPVFGVDAL 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488999782 241 PDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGE--------KVESH-VWIPFELVTKENM 296
Cdd:PRK15395 261 PEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKgaaegtnwKIENKvVRVPYVGVDKDNL 325
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
62-290 |
8.24e-32 |
|
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: 119.28 E-value: 8.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 62 DTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTLPPG---VVFVGSDERESGTLQMEA 138
Cdd:cd19970 43 DIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNRLDADALKEGginVPFVGPDNRQGAYLAGDY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 139 LAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPaMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMA 218
Cdd:cd19970 123 LAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAG-MKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMA 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488999782 219 IGAAMALEKSQK--KLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGEKVESHVWIPFEL 290
Cdd:cd19970 202 LGAIKAVDAAGKagKVLVVGFDNIPAVRPLLKDGKMLATIDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPVEL 275
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
23-300 |
1.11e-31 |
|
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: 119.65 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAqARH----VDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDS-ASTPQLTKm 97
Cdd:cd19996 1 TIGFSNAGLGNSWRVQMIAEFEAEA-AKLkkliKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPtALLPAIEK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 98 AQQAKMPLVYVNRTPGDKTLppgVVFVGSDERESGTLQMEALAKLANYKGNVaIMIGNLtdAG---ALQRTKDVEQVVAK 174
Cdd:cd19996 79 AAAAGIPVVLFDSGVGSDKY---TAFVGVDDAAFGRVGAEWLVKQLGGKGNI-IALRGI--AGvsvSEDRWAGAKEVFKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 175 YPAMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKKL-LIGGiDATPDGLKAL-ASDKI 252
Cdd:cd19996 153 YPGIKIVGEVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLvPMTG-EDNNGFLKAWkELPGF 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 488999782 253 QVTVFQDAVGQGKTALAVALKLIKGEKVESHVWIPFELVTKENMQTYV 300
Cdd:cd19996 232 KSIAPSYPPWLGATALDAALAALEGEPVPKYVYIPLPVITDENLDQYV 279
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
23-292 |
1.04e-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: 113.59 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGR--QADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQ 100
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPESEEDVagQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 101 AKMPLVYVN-RTPGDKTLPpgvvFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPA-M 178
Cdd:cd06310 81 KGIPVIVIDsGIKGDAYLS----YIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGgI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 179 KVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALE--KSQKKLLIGGIDATPDGLKALASDKIQVTV 256
Cdd:cd06310 157 KVLASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKsrKLSGQIKIVGFDSQEELLDALKNGKIDALV 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 488999782 257 FQDAVGQGKTALAVALKLIKGEKVESHVWIPFELVT 292
Cdd:cd06310 237 VQNPYEIGYEGIKLALKLLKGEEVPKNIDTGAELIT 272
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
22-293 |
1.63e-29 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 113.65 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 22 EKIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQA 101
Cdd:PRK10653 27 DTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 102 KMPLVYVNRTPGDKTLppgVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYpAMKVV 181
Cdd:PRK10653 107 NIPVITLDRGATKGEV---VSHIASDNVAGGKMAGDFIAKKLGEGAKVIQLEGIAGTSAARERGEGFKQAVAAH-KFNVL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 182 QKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQK-KLLIGGIDATPDGLKALASDKIQVTVFQDA 260
Cdd:PRK10653 183 ASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKsDVMVVGFDGTPDGIKAVNRGKLAATIAQQP 262
|
250 260 270
....*....|....*....|....*....|...
gi 488999782 261 VGQGKTALAVALKLIKGEKVESHVWIPFELVTK 293
Cdd:PRK10653 263 DQIGAIGVETADKVLKGEKVEAKIPVDLKLVTK 295
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
52-294 |
8.82e-27 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 105.79 E-value: 8.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 52 VDVQFE--DARGDTGRQADQVQSFIASGVDAIIVDPVDS-ASTPQLTKmAQQAKMPLVYVnrtpgDKTLPPGVV--FVGS 126
Cdd:cd20005 30 VKITFEgpDTESDVDKQIEMLDNAIAKKPDAIALAALDTnALLPQLEK-AKEKGIPVVTF-----DSGVPSDLPlaTVAT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 127 DERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKD-VEQVVAKYPAMKVVQKQPANYSRSEGMDLMQNWTGNGE 205
Cdd:cd20005 104 DNYAAGALAADHLAELIGGKGKVAIVAHDATSETGIDRRDGfKDEIKEKYPDIKVVNVQYGVGDHAKAADIAKAILQANP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 206 AIDIVAANNDEMAIGAAMALE--KSQKKLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGEKVESH 283
Cdd:cd20005 184 DLKGIYATNEGAAIGVANALKemGKLGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAAVKALKGEEVEKL 263
|
250
....*....|.
gi 488999782 284 VWIPFELVTKE 294
Cdd:cd20005 264 IDTGAKWYDKD 274
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
46-299 |
1.79e-26 |
|
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: 106.15 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 46 EAQARHVDVQFE--DARGDTGRQADQVQSFIAS--GVDAIIVDPVDSaSTPQLTKMAQQAKMPLVYVNRTPGD----KTL 117
Cdd:cd06324 23 QAAAKDLGIELEvlYANRNRFKMLELAEELLARppKPDYLILVNEKG-VAPELLELAEQAKIPVFLINNDLTDeeraLLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 118 PPGVVF---VGS---DERESGTLQMEALAKLANYKGN------VAIMiGNLTDAGALQRTKDVEQVVAKYPAMKVVQKQP 185
Cdd:cd06324 102 KPREKFkywLGSivpDNEQAGYLLAKALIKAARKKSDdgkirvLAIS-GDKSTPASILREQGLRDALAEHPDVTLLQIVY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 186 ANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKK----LLIGGIDATPDGLKALASDKIQVTvfqdaV 261
Cdd:cd06324 181 ANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKpgkdVLVGGIDWSPEALQAVKDGELTAS-----V 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 488999782 262 GQGKTALAVALKLI----------KGEKVESHvwiPFELVTKENMQTY 299
Cdd:cd06324 256 GGHFLEGAWALVLLydyhhgidfaAGTSVQLK---PMLAITRDNVAQY 300
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
23-287 |
2.09e-26 |
|
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: 105.85 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQA-----RHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKM 97
Cdd:cd19999 1 VIGVSNGYVGNEWRAQMIADFEEVAAEykeegVISDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 98 AQQAKMpLVYVNRTPGDKtlpPGVVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPA 177
Cdd:cd19999 81 AQAAGI-LVVSFDQPVSS---PDAINVVIDQYKWAAIQAQWLAEQLGGKGNIVAINGVAGNPANEARVKAADDVFAKYPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 178 MKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVaANNDEMAIGAAMALEKSQKKLLIGGIDATPDGL---KALASDKIQV 254
Cdd:cd19999 157 IKVLASVPGGWDQATAQQVMATLLATYPDIDGV-LTQDGMAEGVLRAFQAAGKDPPVMTGDYRKGFLrkwKELDLPDFES 235
|
250 260 270
....*....|....*....|....*....|...
gi 488999782 255 TVFQDAVGQGKTALAVALKLIKGEKVESHVWIP 287
Cdd:cd19999 236 IGVVNPPGIGATALRIAVRLLQGKELKEDALNP 268
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
23-303 |
2.73e-26 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 105.22 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFD-QNFLTIiRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDS-ASTPQLTKmAQQ 100
Cdd:COG4213 4 KIGVSLPTKTsERWIRD-GDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGtALAAVLEK-AKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 101 AKMPLV-Y---VNRTPGDktlppgvVFVGSDERESGTLQMEALAKL--ANYKGNVAIMIGNLTDAGALQRTKDVEQVVAK 174
Cdd:COG4213 82 AGIPVIaYdrlILNSDVD-------YYVSFDNVKVGELQGQYLVDGlpLKGKGNIELFGGSPTDNNATLFFEGAMSVLQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 175 YPA---MKVVQKQPA-NYSRSEGMDLMQN-WTGNGEAIDIVAANNDEMAIGAAMALeKSQK---KLLIGGIDATPDGLKA 246
Cdd:COG4213 155 YIDsgkLVVVSGQWTlGWDPETAQKRMENlLTANGNKVDAVLAPNDGLAGGIIQAL-KAQGlagKVVVTGQDAELAAVQR 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488999782 247 LASDKIQVTVFQDAVGQGKTALAVALKLIKGEKVESH------------VWIPFELVTKENMQTYVEKS 303
Cdd:COG4213 234 ILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPEVNgtydngkkdvpsYLLEPVAVTKDNVKETLIDS 302
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
35-292 |
4.76e-26 |
|
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: 103.82 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 35 FLTIIRQSIEKEAQARHVDVQFEDAR-GDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVnrtpg 113
Cdd:cd06314 13 FWDLAEAGAEKAAKELGVNVEFVGPQkSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 114 DKTLPPG--VVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQKQPANYSRS 191
Cdd:cd06314 88 DSDAPDSkrLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKGSPGIEIVDPLSDNDDIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 192 EGMDLMQNWTGNGEAID-IVAANN-DEMAIGAAMALEKSQKKLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALA 269
Cdd:cd06314 168 KAVQNVEDILKANPDLDaIFGVGAyNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVIAATVGQRPYEMGYLSVK 247
|
250 260
....*....|....*....|....
gi 488999782 270 VALKLIKGEKVESHVWI-PFELVT 292
Cdd:cd06314 248 LLYKLLKGGKPVPDVIDtGVDVVT 271
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
23-284 |
3.67e-25 |
|
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: 101.78 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDS-ASTPQLTKmAQQA 101
Cdd:cd19993 1 VVGVSWSNFQEERWKTDEAAMKKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGdAILPAVEK-AAAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 102 KMPLVYVNRTPGDktlpPGVVFVGSDERESGTLQMEALAKLANyKGNVAIMIGNLTDAGA---LQRTKDVEQVVAKYPAM 178
Cdd:cd19993 80 GIPVIAYDRLIEN----PIAFYISFDNVEVGRMQARGVLKAKP-EGNYVFIKGSPTDPNAdflRAGQMEVLQPAIDSGKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 179 KVVQKQ------PANYSRsegmdLMQN-WTGNGEAIDIVAANNDEMAIGAAMALeKSQK---KLLIGGIDATPDGLKALA 248
Cdd:cd19993 155 KIVGEQytdgwkPANAQK-----NMEQiLTANNNKVDAVVASNDGTAGGAVAAL-AAQGlagKVPVSGQDADKAALNRIA 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 488999782 249 SDKIQVTVFQDAVGQGKTALAVALKLIKGEKVESHV 284
Cdd:cd19993 229 LGTQTVTVWKDARELGKEAAEIAVELAKGTKIEAIK 264
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
52-282 |
4.23e-25 |
|
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: 101.60 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 52 VDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLV-YVNRTPGDKTlppgVVFVGSDERE 130
Cdd:cd19995 33 CKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIaYDRLILGGPA----DYYVSFDNVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 131 SGTLQMEALAKLANYKG----NVAIMIGNLTDAGALQRTKDVEQVVAK---YPAMKVVQKQPA-NYSRSEGMDLM-QNWT 201
Cdd:cd19995 109 VGEAQAQSLVDHLKAIGkkgvNIVMINGSPTDNNAGLFKKGAHEVLDPlgdSGELKLVCEYDTpDWDPANAQTAMeQALT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 202 GNGEAIDIVAANNDEMAiGAAMALEKSQK---KLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGE 278
Cdd:cd19995 189 KLGNNIDGVLSANDGLA-GGAIAALKAQGlagKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGE 267
|
....
gi 488999782 279 KVES 282
Cdd:cd19995 268 TPPS 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
30-299 |
8.86e-25 |
|
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: 100.53 E-value: 8.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 30 YFDQN--FLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVY 107
Cdd:cd06317 6 QINQQaqFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 108 VNrTPGDKtlPPGVVFVGSDERESGTLQMEALAKL--ANYKGNVAI-MIGNLTDAGALQRTKDVEQVVAKYPAMKVVQKQ 184
Cdd:cd06317 86 YD-AVIPS--DFQAAQVGVDNLEGGKEIGKYAADYikAELGGQAKIgVVGALSSLIQNQRQKGFEEALKANPGVEIVATV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 185 PA----NYSRSEGMDLMqnwTGNGEaIDIVAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKI-QVTVF 257
Cdd:cd06317 163 DGqnvqEKALSAAENLL---TANPD-LDAIYATGEPALLGAVAAVRSQgrQGKIKVFGWDLTKQAIFLGIDEGVlQAVVQ 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488999782 258 QDAVGQGKTALAVALKLIKGEKVESHVWIPFELVTKENMQTY 299
Cdd:cd06317 239 QDPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTKENVDQF 280
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
24-284 |
1.26e-23 |
|
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: 97.32 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSAStPQLTKMAQQAKM 103
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAA-AGVAEKARGQNV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 104 PLVYVNRTPGDKTLppgVVFVGSDERESGTLQMEALAKLANYKgnVAIMIGNLTDAGALQRT----KDVEQVVAKYPAMK 179
Cdd:cd01537 81 PVVFFDKEPSRYDK---AYYVITDSKEGGIIQGDLLAKHGHIQ--IVLLKGPLGHPDAEARLagviKELNDKGIKTEQLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQkqpANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKKLL----IGGIDATPDGLKALAsdkIQVT 255
Cdd:cd01537 156 LDT---GDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPsdisVFGYDALPEALKSGP---LLTT 229
|
250 260
....*....|....*....|....*....
gi 488999782 256 VFQDAVGQGKTALAVALKLIKGEKVESHV 284
Cdd:cd01537 230 ILQDANNLGKTTFDLLLNLADNWKIDNKV 258
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
23-293 |
3.64e-23 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 96.15 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQ--VQSFIASGVDAIIVDPVDS-ASTPQLTKmAQ 99
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPSREDDVEAQIqiIEYFIDQGVDGIVLAPLDRkALVAPVER-AR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 100 QAKMPLVYVNR-TPGDKTLPpgvvFVGSDERESGTLQMEALAKLANYKGNVAIMignLTDAGA---LQRTKDVEQVVAK- 174
Cdd:cd20004 80 AQGIPVVIIDSdLGGDAVIS----FVATDNYAAGRLAAKRMAKLLNGKGKVALL---RLAKGSastTDRERGFLEALKKl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 175 YPAMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALE---KSQKKLLIGgIDATPDGLKALASDK 251
Cdd:cd20004 153 APGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRrlgLAGKVKFIG-FDASDLLLDALRAGE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488999782 252 IQVTVFQDAVGQGKTALAVALKLIKGEKVESHVWIPFELVTK 293
Cdd:cd20004 232 ISALVVQDPYRMGYLGVKTAVAALRGKPVPKRIDTGVVLVTK 273
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
24-294 |
4.71e-23 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 96.81 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVdpVDSASTPQLTKMAQQAKM 103
Cdd:COG1609 64 IGVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLIL--AGSRLDDARLERLAEAGI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 104 PLVYVNRTPGDktlpPGVVFVGSDERESGTLQMEALAKLaNYKgNVAIMIGNLTDAGALQRTKDVEQVVAK----YPAMK 179
Cdd:COG1609 142 PVVLIDRPLPD----PGVPSVGVDNRAGARLATEHLIEL-GHR-RIAFIGGPADSSSARERLAGYREALAEaglpPDPEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVqkqPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKK----LLIGGID-------ATPdglkALA 248
Cdd:COG1609 216 VV---EGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRvpedVSVVGFDdiplaryLTP----PLT 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488999782 249 sdkiqvTVFQDAVGQGKTALAVALKLIKGEKVES-HVWIPFELVTKE 294
Cdd:COG1609 289 ------TVRQPIEEMGRRAAELLLDRIEGPDAPPeRVLLPPELVVRE 329
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
43-292 |
8.66e-23 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380662 [Multi-domain] Cd Length: 271 Bit Score: 95.00 E-value: 8.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 43 IEKEAQARHVDVQFEDARG-DTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTLPpgV 121
Cdd:cd20007 21 AEAAAKELGVELDVQGPPTfDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVDTTLGDPSFV--L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 122 VFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQKQPANYSRSEGMDLMQN-W 200
Cdd:cd20007 99 SQIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMKKYPGIKVLGVQYSENDPAKAASIVAAaL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 201 TGNGEAIDIVAANNDEmAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGE 278
Cdd:cd20007 179 QANPDLAGIFGTNTFS-AEGAAAALRNAgkTGKVKVVGFDASPAQVEQLKAGTIDALIAQKPAEIGYLAVEQAVAALTGK 257
|
250
....*....|....
gi 488999782 279 KVESHVWIPFELVT 292
Cdd:cd20007 258 PVPKDILTPFVVIT 271
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
23-283 |
1.32e-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: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd19991 1 KIGFSMDSLRVERWQRDRDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNR----TPGDktlppgvVFVGSDERESGTLQMEALAKLANyKGNVAIMIGNLTDAGALQRTKDVEQVVAKY--- 175
Cdd:cd19991 81 VPVLAYDRlilnADVD-------LYVSFDNEKVGELQAEALVKAKP-KGNYVLLGGSPTDNNAKLFREGQMKVLQPLids 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 176 PAMKVVQKQ-PANYSRSEGMDLMQNW-TGNGEAIDIVAANNDEMAIGAAMALEKSQ--KKLLIGGIDATPDGLKALASDK 251
Cdd:cd19991 153 GDIKVVGDQwVDDWDPEEALKIMENAlTANNNKIDAVIASNDGTAGGAIQALAEQGlaGKVAVSGQDADLAACQRIVEGT 232
|
250 260 270
....*....|....*....|....*....|..
gi 488999782 252 IQVTVFQDAVGQGKTALAVALKLIKGEKVESH 283
Cdd:cd19991 233 QTMTIYKPIKELAEKAAELAVALAKGEKNEAN 264
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
52-293 |
2.35e-22 |
|
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: 93.82 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 52 VDVQFE--DARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNrTPGDKTLPPGvvFVGSDER 129
Cdd:cd20006 32 VDLEFLgpESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITID-SPVNSKKADS--FVATDNY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 130 ESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDI 209
Cdd:cd20006 109 EAGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQALAEYPNIKIVETEYCDSDEEKAYEITKELLSKYPDING 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 210 VAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGEKVESHVWIP 287
Cdd:cd20006 189 IVALNEQSTLGAARALKELglGGKVKVVGFDSSVEEIQLLEEGIIDALVVQNPFNMGYLSVQAAVDLLNGKKIPKRIDTG 268
|
....*.
gi 488999782 288 FELVTK 293
Cdd:cd20006 269 SVVITK 274
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
24-291 |
5.35e-22 |
|
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: 92.58 E-value: 5.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVdpVDSASTPQLTKMAQQAKM 103
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIIL--APSSLDDELLEELLAAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 104 PLVYVNRTPGDKTLPpgvvFVGSDERESGTLQMEALAKLaNYKgNVAIMIGNLTDAGALQRTKDVEQVVAKY----PAMK 179
Cdd:cd06267 80 PVVLIDRRLDGLGVD----SVVVDNYAGAYLATEHLIEL-GHR-RIAFIGGPLDLSTSRERLEGYRDALAEAglpvDPEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQkqpANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKK----LLIGGIDATPdglkalASDKIQV- 254
Cdd:cd06267 154 VVE---GDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRvpedISVVGFDDIP------LAALLTPp 224
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488999782 255 --TVFQDAVGQGKTALAVALKLIKGEKVES-HVWIPFELV 291
Cdd:cd06267 225 ltTVRQPAYEMGRAAAELLLERIEGEEEPPrRIVLPTELV 264
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
23-285 |
2.22e-20 |
|
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: 88.63 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPGDKTLPpgvVFVGSDERESGTLQMEALAKlANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKY---PAMK 179
Cdd:cd01538 81 IKVIAYDRLILNADVD---YYISFDNEKVGELQAQALLD-AKPEGNYVLIGGSPTDNNAKLFRDGQMKVLQPAidsGKIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQKQPA-NYSRSEGMDLMQNW-TGNGEAIDIVAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVT 255
Cdd:cd01538 157 VVGDQWVdDWLPANAQQIMENAlTANGNNVDAVVASNDGTAGGAIAALKAQglSGGVPVSGQDADLAAIKRILAGTQTMT 236
|
250 260 270
....*....|....*....|....*....|
gi 488999782 256 VFQDAVGQGKTALAVALKLIKGEKVESHVW 285
Cdd:cd01538 237 VYKDIRLLADAAAEVAVALMRGEKPPINGT 266
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
23-292 |
4.54e-20 |
|
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: 87.74 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAK 102
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPGDktlpPGVVFVGSDERESGTLQMEALAKLANYKGNVA-IMIGNLTDAGalQRTKDVEQVVAKYPAMKVV 181
Cdd:cd06305 81 IPVVTFDTDSQV----PGVNNITQDDYALGTLSLGQLVKDLNGEGNIAvFNVFGVPPLD--KRYDIYKAVLKANPGIKKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 182 QKQPANYS-------RSEGMDLMQNWTGNGeaIDIVAANNDEMAIGAAMALEKSQK-KLLIGGIDATPDGLKALA--SDK 251
Cdd:cd06305 155 VAELGDVTpntaadaQTQVEALLKKYPEGG--IDAIWAAWDEPAKGAVQALEEAGRtDIKVYGVDISNQDLELMAdeGSP 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 488999782 252 IQVTVFQDAVGQGKTALAVALKLIKGEKVESHVWIPFELVT 292
Cdd:cd06305 233 WVATAAQDPALIGTVAVRNVARKLAGEDLPDKYSLVPVLIT 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
23-301 |
2.61e-19 |
|
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: 86.19 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAY----FDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMA 98
Cdd:cd19998 1 KIALSNSYsgndWRQEMINIAKAAAKQPPYADKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 99 QQAKMPLVyvnrtPGDKTLP-PGVVFVGSDERESGTLQMEALAKLANYKGNVaIMI----GNLTDAgalQRTKDVEQVVA 173
Cdd:cd19998 81 CDAGIVVV-----AFDNVVDePCAYNVNTDQAKAGEQTAQWLVDKLGGKGNI-LMVrgvpGTSVDR---DRYEGAKEVFK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 174 KYPAMKVVQKQPANYSRSegmdlmqnwTGNGEAIDIVAANNDEMAI-------GAAMALEKSQKKLLIGGIDATPDGLKA 246
Cdd:cd19998 152 KYPDIKVVAEYYGNWDDG---------TAQKAVADALAAHPDVDGVwtqggetGVIKALQAAGHPLVPVGGEAENGFRKA 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488999782 247 LAS---DKIQVTVFQDAVGQGKTALAVALKLIKGEKVESHVWIPFELVTKENMQTYVE 301
Cdd:cd19998 223 MLEplaNGLPGISAGSPPALSAVALKLAVAVLEGEKEPKTIELPLPWVTTDDVKLCQG 280
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
23-303 |
6.11e-19 |
|
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: 85.03 E-value: 6.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQA-----RHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKM 97
Cdd:cd19997 1 VIALSNSYAGNTWRQQMVDAFEEAAKKakadgLIADYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 98 AQQAKMPLVYVNRTPGDktlpPGVVFVGSDERESGTLQMEALAKLANYKGNVAI---MIGNLTDAGALQRTKDveqVVAK 174
Cdd:cd19997 81 ACDAGIKVVVFDSGVTE----PCAYILNNDFEDYGAASVEYVADRLGGKGNVLEvrgVAGTSPDEEIYAGQVE---ALKK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 175 YPAMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEmAIGAAMALEKSQKKLLIGGIDATPDGLKALASDKIQ- 253
Cdd:cd19997 154 YPDLKVVAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGD-GYGAAQAFEAAGRPLPIIIGGNRGEFLKWWQEEYAKn 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 488999782 254 ----VTVFQDAvGQGKTALAVALKLIKGEKVESHVWIPFELVTKENMQTYVEKS 303
Cdd:cd19997 233 gyetVSVSTDP-GQGSAAFWVALDILNGKDVPKEMILPVVTITEDDLDAWLAVT 285
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
23-291 |
2.92e-18 |
|
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: 82.63 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDT--GRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQ 100
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGGYTnlSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 101 AKMPLV-YVNRTPGDKtlppgVVF-VGSDERESGTLQMEALAK-LANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKyPA 177
Cdd:cd06306 81 AGIPVIdLVNGIDSPK-----VAArVLVDFYDMGYLAGEYLVEhHPGKPVKVAWFPGPAGAGWAEDREKGFKEALAG-SN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 178 MKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAAnNDEMAIGAAMALEKSQK--KLLIGGIDATPDGLKALASDKIQVT 255
Cdd:cd06306 155 VEIVATKYGDTGKAVQLNLVEDALQAHPDIDYIVG-NAVAAEAAVGALREAGLtgKVKVVSTYLTPGVYRGIKRGKILAA 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 488999782 256 VFQDAVGQGKTALAVALKLIKGEKVESHVWIPFELV 291
Cdd:cd06306 234 PSDQPVLQGRIAVDQAVRALEGKPVPKHVGPPILVV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
61-291 |
2.37e-17 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 80.10 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 61 GDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTlppGVVFVGSDERESGTLQMEALA 140
Cdd:cd06311 39 SNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLI---YDLYVAGDNPGMGVVSAEYIG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 141 KLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIG 220
Cdd:cd06311 116 KKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNPGIKILAMQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 221 AAMALEKSQK---KLLIGG------IDATPDGLKALASDkiqVTVFQDAVgqgKTALAVALKLIKG-EKVESHVWIPFEL 290
Cdd:cd06311 196 VLQAIKEAGRtdiKVMTGGggsqeyFKRIMDGDPIWPAS---ATYSPAMI---ADAIKLAVLILKGgKTVEKEVIIPSTL 269
|
.
gi 488999782 291 V 291
Cdd:cd06311 270 V 270
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
62-293 |
1.21e-16 |
|
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: 78.04 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 62 DTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQqAKMPLVYVNRTPgdkTLPPGVVFVGSDERESGTLQMEALAK 141
Cdd:cd20008 42 DIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD-AGIPVVLVDSGA---NTDDYDAFLATDNVAAGALAADELAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 142 L----ANYKGNVAIMIGNLTDAGALQRTKD-VEQVVAKYPAMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDE 216
Cdd:cd20008 118 LlkasGGGKGKVAIISFQAGSQTLVDREEGfRDYIKEKYPDIEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 217 MAIGAAMALEKSQK--KLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGEK-VESHVWIPFELVTK 293
Cdd:cd20008 198 SAVGVAQALAEAGKagKIVLVGFDSSPDEVALLKSGVIKALVVQDPYQMGYEGVKTAVKALKGEEiVEKNVDTGVTVVTK 277
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
23-281 |
1.72e-16 |
|
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: 78.06 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAyfDQNFLTIIR--QSIEKEAQAR--HVDVQFedARGDTGRQADQVQSFIASGVDAIIVDPVD-SASTPQLTKm 97
Cdd:cd19994 1 KIGISLP--TKSEERWIKdgENLKSELEEAgyTVDLQY--ADDDVATQNSQIENMINKGAKVLVIAPVDgSALGDVLEE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 98 AQQAKMPLVYVNRTPGDKtlpPGV-VFVGSDERESGTLQMEALAK---LANYKGNVAIMI--GNLTDAGALqrtkdveqv 171
Cdd:cd19994 76 AKDAGIPVIAYDRLIMNT---DAVdYYVTFDNEKVGELQGQYLVDklgLKDGKGPFNIELfaGSPDDNNAQ--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 172 vAKYP-AMKVVQ---KQPANYSRSEGMDLMQ----NWTGN----------------GEAIDIVAANNDEMAIGAAMALEK 227
Cdd:cd19994 144 -LFFKgAMEVLQpyiDDGTLVVRSGQTTFEQvatpDWDTEtaqarmetllsayytgGKKLDAVLSPNDGIARGVIEALKA 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488999782 228 SQKKL----LIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGEKVE 281
Cdd:cd19994 223 AGYDTgpwpVVTGQDAEDASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVE 280
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
53-300 |
7.28e-16 |
|
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: 76.21 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 53 DVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVnrtpGDKTLPPGVVFVGSDERESG 132
Cdd:cd06300 36 ELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAF----DGAVTSPDAYNVSNDQVEWG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 133 TLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAA 212
Cdd:cd06300 112 RLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEALAEYPGIKVVGEVFGGWDEATAQTAMLDFLATHPQVDGVWT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 213 NNDEmAIGAAMALEKSQKKLLIGGIDATPDGLKALASDKIQVtVFQDAV----GQGKTALAVALKLIKGEK-VESHVWIP 287
Cdd:cd06300 192 QGGE-DTGVLQAFQQAGRPPVPIVGGDENGFAKQWWKHPKKG-LTGAAVwpppAIGAAGLEVALRLLEGQGpKPQSVLLP 269
|
250
....*....|...
gi 488999782 288 FELVTKENMQTYV 300
Cdd:cd06300 270 PPLITNDDAKAWY 282
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
43-258 |
1.99e-15 |
|
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 74.68 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 43 IEKEAQARHVDVQFE-DARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVnrtpgDKTLPPG- 120
Cdd:cd19969 21 FEDAGAELGVKTEYTgPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTF-----DSDAPESk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 121 -VVFVGSDERESGTLQMEALAKLANYKGNVAIMIGNLTDAGAlQRTKDVEQVVAKYPAMKVVQKQPANYSRSEGMDLMQN 199
Cdd:cd19969 96 rISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQPNHE-ERVEGFKEAFAEYPGIEVVAVGDDNDDPEKAAQNTSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488999782 200 WTGNGEAIDIVAANNDEMAIGAAMALEKSQK--KLLIGGIDATPDGLKALASDKIQVTVFQ 258
Cdd:cd19969 175 LLQAHPDLVGIFGVDASGGVGAAQAVREAGKtgKVKIVAFDDDPETLDLIKDGVIDASIAQ 235
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
29-282 |
2.17e-14 |
|
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: 71.92 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 29 AYFDQnfltiIRQSIEKEAQARHVDV-QFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAkmplvy 107
Cdd:cd20001 12 AWFDR-----METGVEQFAKDTGVNVyQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 108 vnrtpgdktlppGVVFVGS---------------DERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTK-DVEQV 171
Cdd:cd20001 81 ------------GIVVITHeasnlknvdydveafDNAAYGAFIMDKLAEAMGGKGKYVTFVGSLTSTSHMEWANaAVAYQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 172 VAKYPAMKVVQKQPANYSRSEgmdlmqnwTGNGEAIDIVAANNDEMAI---------GAAMALEKS--QKKLLIGGIDAT 240
Cdd:cd20001 149 KANYPDMLLVTDRVETNDDSE--------TAYEKAKELLKTYPDLKGIvgcsssdvpGAARAVEELglQGKIAVVGTGLP 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488999782 241 PDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGEKVES 282
Cdd:cd20001 221 SVAGEYLEDGTIDYIQFWDPADAGYAMNALAVMVLEGEKITD 262
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
35-280 |
2.62e-14 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 71.83 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 35 FLTIIRQSIEKEAQARHVDVQF--EDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNRTP 112
Cdd:PRK09701 38 FWVDMKKGIEDEAKTLGVSVDIfaSPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 113 GDKTLPP--GVV--FVGSDERESGTLQME-ALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQKQPAN 187
Cdd:PRK09701 118 DMDNLKKagGNVeaFVTTDNVAVGAKGASfIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAFKKASQIKLVASQPAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 188 YSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQK--KLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGK 265
Cdd:PRK09701 198 WDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKtgKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGA 277
|
250
....*....|....*
gi 488999782 266 TALAVALKLIKGEKV 280
Cdd:PRK09701 278 TGLKLMVDAEKSGKV 292
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
58-303 |
1.37e-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: 380539 [Multi-domain] Cd Length: 294 Bit Score: 69.57 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 58 DARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTLPPGVV-FVGSDERESGTLQM 136
Cdd:cd06316 37 DANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKLVFMDNVPDGLEAGKDYVsVVSSDNRGNGQIAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 137 EALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVA-KYPAMKVVQKQP---ANYSRSEGMDLMQNwtgNGEaIDIVAA 212
Cdd:cd06316 117 ELLAEAIGGKGKVGIIYHDADFYATNQRDKAFKDTLKeKYPDIKIVAEQGfadPNDAEEVASAMLTA---NPD-IDGIYV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 213 NNDEMAIGAAMAL-EKSQKKLLIGGIDATPDGLKALASDK-IQVTVFQDAVGQGKT-ALAVALKLIkGEKVESHVWIPFE 289
Cdd:cd06316 193 SWDTPALGVISALrAAGRSDIKITTVDLGTEIALDMAKGGnVKGIGAQRPYDQGVAeALAAALALL-GKEVPPFIGVPPL 271
|
250
....*....|....
gi 488999782 290 LVTKENMQTYVEKS 303
Cdd:cd06316 272 AVTKDNLLEAWKQI 285
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
35-264 |
1.89e-13 |
|
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: 68.84 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 35 FLTIIRQSIEKEAQARHVDVQFE-DARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNrTPG 113
Cdd:cd19965 13 FFQPVKKGMDDACELLGAECQFTgPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAFN-VDA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 114 DKTLPPGVVFVGSDERESGTLQMEALAKLAnYKGNVAIMIGnLTDAGAL---QRTKDVEQVVAKYPAMKVVQKQPANYSR 190
Cdd:cd19965 92 PGGENARLAFVGQDLYPAGYVLGKRIAEKF-KPGGGHVLLG-ISTPGQSaleQRLDGIKQALKEYGRGITYDVIDTGTDL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488999782 191 SEGMDLMQNW-TGNGEAIDIVAANNDEMAiGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVTVFQDAVGQG 264
Cdd:cd19965 170 AEALSRIEAYyTAHPDIKAIFATGAFDTA-GAGQAIKDLglKGKVLVGGFDLVPEVLQGIKAGYIDFTIDQQPYLQG 245
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
62-294 |
2.12e-12 |
|
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: 66.05 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 62 DTGRQADQVQSFIASGVDAIIVDPVdSASTPQLTKMAQQAKMPLVYVNRTPGDKTLPpgvvFVGSDERESGTLQMEALAK 141
Cdd:cd06289 40 DPERQRRFLRRMLEQGVDGLILSPA-AGTTAELLRRLKAWGIPVVLALRDVPGSDLD----YVGIDNRLGAQLATEHLIA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 142 LanykGNVAI-MIGNLTDAGA-LQRTKDVEQVVAKY----PAMKVVqkqPANYSRSEGMDLMQNWTGNGEAIDIVAANND 215
Cdd:cd06289 115 L----GHRRIaFLGGLSDSSTrRERLAGFRAALAEAglplDESLIV---PGPATREAGAEAARELLDAAPPPTAVVCFND 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 216 EMAIGAAMALEKSQKK----LLIGGIDATPDG---LKALASdkiqVTVFQDAVgqGKTALAVALKLIKGE-KVESHVWIP 287
Cdd:cd06289 188 LVALGAMLALRRRGLEpgrdIAVVGFDDVPEAalwTPPLTT----VSVHPREI--GRRAARLLLRRIEGPdTPPERIIIE 261
|
....*..
gi 488999782 288 FELVTKE 294
Cdd:cd06289 262 PRLVVRE 268
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
52-278 |
2.25e-12 |
|
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: 66.11 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 52 VDVQFE-DARGDTGRQADQVQSFIASGVDAIIVDPVDSAS-TPQLTKmAQQAKMPLVyvnrTPGDKTLPPGV-VFV-GSD 127
Cdd:cd06302 30 VEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADAlAPVLKK-AKDAGIKVI----TWDSDAPPSARdYFVnQAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 128 ERESGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVA-KYPAMKVVQKQP----ANYSRSEGMDLMQNwtg 202
Cdd:cd06302 105 DEGLGEALVDSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKsKYPDIELVDTYYtdddQQKAYTQAQNLIQA--- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488999782 203 NGEaIDIVAANNDEMAIGAAMALEKSQK--KLLIGGIdATPDGLKA-LASDKIQVTVFQDAVGQGKTALAVALKLIKGE 278
Cdd:cd06302 182 YPD-LKGIIGVSTTAPPAAAQAVEEAGKtgKVAVTGI-GLPNTARPyLKDGSVKEGVLWDPAKLGYLTVYAAYQLLKGK 258
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
23-294 |
1.69e-11 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380513 [Multi-domain] Cd Length: 267 Bit Score: 63.40 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVdpVDSASTPQLTKMAQQaK 102
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIV--VGGFGDEELLKLLAE-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTPGDktlpPGVVFVGSDERESGTLQMEALAKLanykG--NVAIMIGNLTDAGALQRTKDVEQVVAKYPaMKV 180
Cdd:cd06290 78 IPVVLVDRELEG----LNLPVVNVDNEQGGYNATNHLIDL----GhrRIVHISGPEDHPDAQERYAGYRRALEDAG-LEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 181 VQK--QPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKK----LLIGGIDATPdglkalASDKIQV 254
Cdd:cd06290 149 DPRliVEGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRvpddVSVIGFDDLP------FSKYTTP 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488999782 255 ---TVFQDAVGQGKTALAVALKLIKGEK-VESHVWIPFELVTKE 294
Cdd:cd06290 223 pltTVRQPLYEMGKTAAEILLELIEGKGrPPRRIILPTELVIRE 266
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
24-294 |
2.45e-11 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 63.01 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSAsTPQLTKMAqQAKM 103
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDD-APDLQELA-ARGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 104 PLVYVNRTPGDKTLPpgvvFVGSDERESGTLQMEALAKLanykG--NVAIMIGNLTDAGALQRTKDVEQVVAK----YPA 177
Cdd:cd06285 80 PVVLVDRRIGDTALP----SVTVDNELGGRLATRHLLEL----GhrRIAVVAGPLNASTGRDRLRGYRRALAEaglpVPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 178 MKVVqkqPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALekSQKKLLIG------GIDATPdglkaLASDk 251
Cdd:cd06285 152 ERIV---PGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAA--RDLGLRVPedlsvvGFDDIP-----LAAF- 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 488999782 252 IQV---TVFQDAVGQGKTALAVALKLI--KGEKVESHVwIPFELVTKE 294
Cdd:cd06285 221 LPPpltTVRQPKYEMGRRAAELLLQLIegGGRPPRSIT-LPPELVVRE 267
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
35-272 |
5.98e-11 |
|
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: 61.86 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 35 FLTIIRQSIEKEAQARHVDVQFE-DARGDTGRQADQVQSFIASGVDAIIV-DPVDSASTPQLTKmAQQAKMPLVYVN--R 110
Cdd:cd06312 14 FWSVVKKGAKDAAKDLGVTVQYLgPQNNDIADQARLIEQAIAAKPDGIIVtIPDPDALEPALKR-AVAAGIPVIAINsgD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 111 TPGDKTLpPGVVFVGSDERESGtlqmEALAKLANYKGNVAIMIGNlTDAGAL---QRTKDVEQVVAK----YPAMKVVQK 183
Cdd:cd06312 93 DRSKERL-GALTYVGQDEYLAG----QAAGERALEAGPKNALCVN-HEPGNPgleARCKGFADAFKGagilVELLDVGGD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 184 QPANYSRSEGMdLMQNWTgngeaIDIV--AANNDEMAIGAAMALEKSQKKLLIGGIDATPDGLKALASDKIQVTVFQDAV 261
Cdd:cd06312 167 PTEAQEAIKAY-LQADPD-----TDAVltLGPVGADPALKAVKEAGLKGKVKIGTFDLSPETLEAIKDGKILFAIDQQPY 240
|
250
....*....|.
gi 488999782 262 GQGktALAVAL 272
Cdd:cd06312 241 LQG--YLAVVF 249
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
44-298 |
1.64e-10 |
|
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: 60.77 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 44 EKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTLPPGVVF 123
Cdd:cd01540 22 KKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAGIPVIAVDDQLVDADPMKIVPF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 124 VGSDERESGTLQMEALAKLANYKG-----NVAIM-IGNLTDAGALQRTK-DVEQVVAK-YPAMKVVQKQPANYSRSEGMD 195
Cdd:cd01540 102 VGIDAYKIGEAVGEWLAKEMKKRGwddvkEVGVLaITMDTLSVCVDRTDgAKDALKAAgFPEDQIFQAPYKGTDTEGAFN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 196 LMQ----------NWtgngeaidIVAANNDEMAIGAAMALEKSQKKLL------IGGIDA-------TPDGLKAlasdki 252
Cdd:cd01540 182 AANavitahpevkHW--------LVVGCNDEGVLGAVRALEQAGFDAEdiigvgIGGYLAadeefkkQPTGFKA------ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488999782 253 qvTVFQDAVGQGKTALAVALKLIK-GEKVESHVWIPFELVTKENMQT 298
Cdd:cd01540 248 --SLYISPDKHGYIAAEELYNWITdGKPPPAETLTDGVIVTRDNYKE 292
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
23-289 |
1.86e-10 |
|
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: 60.22 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSaSTPQLTKMAQQAK 102
Cdd:pfam00532 3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAP-SGDDITAKAEGYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 103 MPLVYVNRTpGDktLPPGVVFVGSDERESGTLQMEALAKLAnYKGNVAIMIGNLTDAGALQRTKDVEQVVAKYP-AMKVV 181
Cdd:pfam00532 82 IPVIAADDA-FD--NPDGVPCVMPDDTQAGYESTQYLIAEG-HKRPIAVMAGPASALTARERVQGFMAALAAAGrEVKIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 182 QKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKKLLIGGIDATPDGLKALAS-DKIQVTVFQda 260
Cdd:pfam00532 158 HVATGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRVKIPDIVGIGINSVVGFDGlSKAQDTGLY-- 235
|
250 260 270
....*....|....*....|....*....|.
gi 488999782 261 vgQGKTALAVALKLIKGEKVESHV--WIPFE 289
Cdd:pfam00532 236 --LSPLTVIQLPRQLLGIKASDMVyqWIPKF 264
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
62-282 |
2.09e-10 |
|
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: 60.41 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 62 DTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMpLVYVNRTPGDKTLPPGVVFVGSDerESGTLQMEALAK 141
Cdd:cd20002 41 DPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGI-VVITHESPGQKGADWDVELIDNE--KFGEAQMELLAK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 142 LANYKGNVAIMIGNLTDAGALQRTK-DVEQVVAKYPAMK-VVQKQP----ANYSRSEGMDLMQNWTgngeaiDIVA--AN 213
Cdd:cd20002 118 EMGGKGEYAIFVGSLTVPLHNLWADaAVEYQKEKYPNMKqVTDRIPggedVDVSRQTTLELLKAYP------DLKGiiSF 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488999782 214 NDEMAIGAAMALE--KSQKKLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGEKVES 282
Cdd:cd20002 192 GSLGPIGAGQALRekGLKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDPADAGYAMVYIAKMLLDGKRKEI 262
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
34-264 |
7.11e-10 |
|
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: 58.49 E-value: 7.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 34 NFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIV--DPVDSASTPqLTKMAQQAKMPLVYVNRT 111
Cdd:cd19966 13 PFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAImgHPGDGAYTP-LIEAAKKAGIIVTSFNTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 112 -PGDKTLPPGVVFVGSDERESGTLQMEALAKLANYK-GNVAIMIGNLTDA-GALQRTKDVEQVVAKYPAM-KVVQKQPAN 187
Cdd:cd19966 92 lPKLEYGDCGLGYVGADLYAAGYTLAKELVKRGGLKtGDRVFVPGLLPGQpYRVLRTKGVIDALKEAGIKvDYLEISLEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 188 YSRSEGMDLMQNWtgngeaidiVAANNDEMAIG-------AAM--ALEKSQKK---LLIGGIDATPDGLKALASDKIQVT 255
Cdd:cd19966 172 NKPAEGIPVMTGY---------LAANPDVKAIVgdgggltANVakYLKAAGKKpgeIPVAGFDLSPATVQAIKSGYVNAT 242
|
....*....
gi 488999782 256 VFQDAVGQG 264
Cdd:cd19966 243 IDQQPYLQG 251
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
35-291 |
7.71e-10 |
|
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: 58.32 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 35 FLTIIRqSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDpvdSASTPQLTKMAQQAKMPLVYVNRTPGD 114
Cdd:cd06284 14 YSEILR-GIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILL---SGRLDAELLSELSKRYPIVQCCEYIPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 115 KTLPpgvvFVGSDERESGTLQMEALAKLanykG--NVAIMIGNLTD-------AGALQRTKDVEQVVAKYPamkvvqKQP 185
Cdd:cd06284 90 SGVP----SVSIDNEAAAYDATEYLISL----GhrRIAHINGPLDNvyarerlEGYRRALAEAGLPVDEDL------IIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 186 ANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAamaleksqkklliggidatpdgLKALASDKIQV----------- 254
Cdd:cd06284 156 GDFSFEAGYAAARALLALPERPTAIFCASDELAIGA----------------------IKALRRAGLRVpedvsvigfdd 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488999782 255 ------------TVFQDAVGQGKTALAVALKLIKGEKVES-HVWIPFELV 291
Cdd:cd06284 214 iefaemfspsltTIRQPRYEIGETAAELLLEKIEGEGVPPeHIILPHELI 263
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
70-294 |
9.64e-10 |
|
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: 57.92 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 70 VQSFIASGVDAIIVdpvdSASTPQLTKMaQQAKMPLVYVNRTPGDktlppGVVFVGSDERESGTLQMEALAKlanyKG-- 147
Cdd:cd06291 48 LEMLKRNKVDGIIL----GSHSLDIEEY-KKLNIPIVSIDRYLSE-----GIPSVSSDNYQGGRLAAEHLIE----KGck 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 148 NVAIMIGNLTDAGALQRTKDVEQVVAKYPAMKVVQKQPAN-YSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALE 226
Cdd:cd06291 114 KILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENdFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQ 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488999782 227 KSQKKL-----LIG--GIDATPDGLKALAsdkiqvTVFQDAVGQGKTALAVALKLIKGEKV-ESHVWIPFELVTKE 294
Cdd:cd06291 194 KLGIRVpedvqIIGfdGIEISELLYPELT------TIRQPIEEMAKEAVELLLKLIEGEEIeESRIVLPVELIERE 263
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
45-282 |
4.92e-09 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 56.67 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 45 KEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTLPPGVVFv 124
Cdd:PRK10355 49 KKAESLGAKVFVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDFYISF- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 125 gsDERESGTLQMEALAKlANYKGNVAIMIGNLTDAGA---LQRTKDVEQVVAKYPAMKVVQKQPAN-YSRSEGMDLMQN- 199
Cdd:PRK10355 128 --DNEKVGELQAKALVD-KVPQGNYFLMGGSPVDNNAklfRAGQMKVLKPYIDSGKIKVVGDQWVDgWLPENALKIMENa 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 200 WTGNGEAIDIVAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKG 277
Cdd:PRK10355 205 LTANNNKIDAVVASNDATAGGAIQALSAQglSGKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNG 284
|
....*
gi 488999782 278 EKVES 282
Cdd:PRK10355 285 EEPKA 289
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
39-291 |
5.29e-09 |
|
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: 55.99 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 39 IRQSIEKEAQARHVDVQFEdargdtgRQADQVQSFIASGVDAIIVdpVDSASTPQLTKMAQQAKmPLVYVnrtpGDKTLP 118
Cdd:cd01544 22 IRLGIEKEAKKLGYEIKTI-------FRDDEDLESLLEKVDGIIA--IGKFSKEEIEKLKKLNP-NIVFV----DSNPDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 119 PGVVFVGSDeRESGTLQ-MEALAKLaNYKgNVAIMIGNLTDAGALQRTKDV-EQVVAKYpaMKvvQKQPAN--------Y 188
Cdd:cd01544 88 DGFDSVVPD-FEQAVRQaLDYLIEL-GHR-RIGFIGGKEYTSDDGEEIEDPrLRAFREY--MK--EKGLYNeeyiyigeF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 189 SRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKK----LLIGGID-------ATPdglkALASdkiqVTVF 257
Cdd:cd01544 161 SVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKvpedISIISFNdievakyVTP----PLTT----VHIP 232
|
250 260 270
....*....|....*....|....*....|....*
gi 488999782 258 QDAVgqGKTALAVALKLIKGE-KVESHVWIPFELV 291
Cdd:cd01544 233 TEEM--GRTAVRLLLERINGGrTIPKKVLLPTKLI 265
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
35-282 |
1.32e-08 |
|
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380658 Cd Length: 298 Bit Score: 54.98 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 35 FLTIIRQSIEKEAQARHVDVQFE-DARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLV------- 106
Cdd:cd20003 13 YFTAAGQGAQEAAKELGVDVTYDgPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVtwdsdvn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 107 ------YVNRTPgdktlPPGVvfvgsderesGTLQMEALAKLANYKGNVAIMIGNLTDAGALQRTKDVEQVVA-KYPAMK 179
Cdd:cd20003 93 pdardfFVNQAT-----PEGI----------GKTLVDMVAEQTGEKGKVAIVTSSPTATNQNAWIKAMKAYIAeKYPDMK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQKQPANYSRSEGMDlmqnwtgngEAIDIVAANNDEMAI---------GAAMALEKSQK--KLLIGGIdATPDGLKA-L 247
Cdd:cd20003 158 IVTTQYGQEDPAKSLQ---------VAENILKAYPDLKAIiapdsvalpGAAEAVEQLGRtgKVAVTGL-STPNVMRPyV 227
|
250 260 270
....*....|....*....|....*....|....*
gi 488999782 248 ASDKIQVTVFQDAVGQGKTALAVALKLIKGEKVES 282
Cdd:cd20003 228 KDGTVKSVVLWDVVDLGYLAVYVARALADGTLLKV 262
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
24-291 |
3.21e-08 |
|
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: 53.70 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDpvdSASTPQLTKMAQQAKM 103
Cdd:cd06286 2 IGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIIT---SRENDWEVIEPYAKYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 104 PLVYVNRTpGDKTLPpgVVFVgsdERESGTlqMEALAKLANyKG--NVAIMIGNLTDAGALQ--RTKDVEQVVAKYPamK 179
Cdd:cd06286 79 PIVLCEET-DSPDIP--SVYI---DRYEAY--LEALEYLKE-KGhrKIGYCLGRPESSSASTqaRLKAYQDVLGEHG--L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQKQPANYSRS---EGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKK----LLIGGIDATPdglkalASDKI 252
Cdd:cd06286 148 SLREEWIFTNCHtieDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRvpedLAVIGFDNQP------ISELL 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488999782 253 QV-TVFQDAVGQGKTALAVALKLIKGEKVESHVwIPFELV 291
Cdd:cd06286 222 NLtTIDQPLEEMGKEAFELLLSQLESKEPTKKE-LPSKLI 260
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
23-293 |
1.45e-07 |
|
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: 51.79 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 23 KIGVSMAYFDQNFLTIIRQSIEKEAQA---RHVDVQFED-ARGDTGRQADQVQSfIASGVDAIIVDPVDSASTPQLTKMA 98
Cdd:cd06307 1 RFGFLLPSPENPFYELLRRAIEAAAAAlrdRRVRLRIHFvDSLDPEALAAALRR-LAAGCDGVALVAPDHPLVRAAIDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 99 QQAKMPLVY-VNRTPGDKTLPpgvvFVGSDERESGTLQMEALAK-LANYKGNVAIMIGNLTDAGALQRTKDVEQVVA-KY 175
Cdd:cd06307 80 AARGIPVVTlVSDLPGSRRLA----YVGIDNRAAGRTAAWLMGRfLGRRPGKVLVILGSHRFRGHEEREAGFRSVLReRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 176 PAMKVVqkqpanySRSEGMDLMQnwtGNGEAI-DIVAANNDEMAI--------GAAMALEKSQKKLLIGGI--DATPDGL 244
Cdd:cd06307 156 PDLTVL-------EVLEGLDDDE---LAYELLrELLARHPDLVGIynagggneGIARALREAGRARRVVFIghELTPETR 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488999782 245 KALASDKIQVTVFQDAVGQGKTALAVALKLIKG-EKVESHVWIPFELVTK 293
Cdd:cd06307 226 RLLRDGTIDAVIDQDPELQARRAIEVLLAHLGGkGPAPPQPPIPIEIITR 275
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
24-294 |
2.11e-07 |
|
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: 51.02 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIvdpvdSAS---TPQLTKMAQQ 100
Cdd:cd19975 2 IGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGII-----FASgtlTEENKQLLKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 101 AKMPLVYVNRTPGDKTLPpgvvFVGSDERESGTLQMEALAKLaNYKgNVAIMIGNLTDAGA-LQRTKDVEQVVAKYP-AM 178
Cdd:cd19975 77 MNIPVVLVSTESEDPDIP----SVKIDDYQAAYDATNYLIKK-GHR-KIAMISGPLDDPNAgYPRYEGYKKALKDAGlPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 179 KVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKS----QKKLLIGGIDATPdglkaLASDKIQ- 253
Cdd:cd19975 151 KENLIVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHgirvPEDISVIGFDNTE-----IAEMSIPp 225
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 488999782 254 -VTVFQDAVGQGKTALAVALKLIKGEKV-ESHVWIPFELVTKE 294
Cdd:cd19975 226 lTTVSQPFYEMGKKAVELLLDLIKNEKKeEKSIVLPHQIIERE 268
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
80-294 |
3.01e-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: 380510 [Multi-domain] Cd Length: 268 Bit Score: 50.88 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 80 AIIVDPvdSASTPQLTKMAQqAKMPLVYVNRTPGDKTLPPGVvfvgsDERESGTLQMeALAKL-ANYKGNVAIMIGNLTD 158
Cdd:cd06287 60 AIVVEP--TVEDPILARLRQ-RGVPVVSIGRAPGTDEPVPYV-----DLQSAATARL-LLEHLhGAGARQVALLTGSSRR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 159 AGALQRTKDVEQVVAKYPAMKVVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKKLLIGGID 238
Cdd:cd06287 131 NSSLESEAAYLRFAQEYGTTPVVYKVPESEGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMV 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488999782 239 ATP-DGLKALASDKIQVTVFQDAVGQGKTALAVALKLIKGEKVESHVWIPFELVTKE 294
Cdd:cd06287 211 VTRyDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSVEVGPAPELVVRA 267
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
35-258 |
6.75e-07 |
|
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: 49.77 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 35 FLTIIRQSIEKEAQARHVDVQFEDAR--GDTGRQADQVQSFIASGVDAIIVDPVDS-ASTPQLTKmAQQAKMpLVYVNRT 111
Cdd:cd19973 13 FFVKMKEGAQKAAKALGIKLMTAAGKidGDNATQVTAIENMIAAGAKGILITPSDTkAIVPAVKK-ARDAGV-LVIALDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 112 PGDKTLPPGVVFvGSDERESGTL--------QMEALAKLANYKGNVAIMIGNLTDAGALQ----RTKDVEQVVAKYPAmK 179
Cdd:cd19973 91 PTDPIDAADATF-ATDNFKAGVLigewakaaLGAKDAKIATLDLTPGHTVGVLRHQGFLKgfgiDEKDPESNEDEDDS-Q 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQKQPANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKS--QKKLLIGGIDATPDGLKALASDKIQVTVF 257
Cdd:cd19973 169 VVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAgkEKGVLIVSVDGGCPGVKDVKDGIIGATSQ 248
|
.
gi 488999782 258 Q 258
Cdd:cd19973 249 Q 249
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
35-231 |
7.01e-07 |
|
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: 49.56 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 35 FLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAqqAKMPLVYVNRTPGD 114
Cdd:cd06280 13 FFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLK--HGIPIVLIDREVEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 115 KTLPpgvvFVGSDERESGTLQMEALAKLAnYKgNVAIMIGNLTDAGALQRTKDVEQVVAKYpAMKVVQK--QPANYSRSE 192
Cdd:cd06280 91 LELD----LVAGDNREGAYKAVKHLIELG-HR-RIGLITGPLEISTTRERLAGYREALAEA-GIPVDESliFEGDSTIEG 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 488999782 193 GMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKK 231
Cdd:cd06280 164 GYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLE 202
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
24-225 |
7.78e-07 |
|
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: 49.44 E-value: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPvDSASTPQLTKMAQQaKM 103
Cdd:cd06270 2 IGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHS-RALSDEELILIAEK-IP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 104 PLVYVNRT-PGdktLPPGVVFVgsDERESGTLQMEALAKLanykG--NVAIMIGNLTDAGALQRTKDVEQVVAKY----P 176
Cdd:cd06270 80 PLVVINRYiPG---LADRCVWL--DNEQGGRLAAEHLLDL----GhrRIACITGPLDIPDARERLAGYRDALAEAgiplD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488999782 177 AMKVVQkqpANYSRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMAL 225
Cdd:cd06270 151 PSLIIE---GDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAAL 196
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
41-294 |
1.45e-06 |
|
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: 48.73 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 41 QSIEKEAQARHVDVQFEDARGDTGRQADQ-VQSFIASGVDAIIVDPVDSASTPQLTKMAQQakMPLVYVNRTPGdktlpP 119
Cdd:cd01574 19 AGIERAARERGYSVSIATVDEDDPASVREaLDRLLSQRVDGIIVIAPDEAVLEALRRLPPG--LPVVIVGSGPS-----P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 120 GVVFVGSDERESGTLQMEALAKLanykG--NVAIMIGNLTDAGALQRTKDVEQVVAKYPAmKVVQKQPANYSRSEGMDLM 197
Cdd:cd01574 92 GVPTVSIDQEEGARLATRHLLEL----GhrRIAHIAGPLDWVDARARLRGWREALEEAGL-PPPPVVEGDWSAASGYRAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 198 QNWTGNGEAIDIVAAnNDEMAIGAAMALEKSQKK----LLIGGIDATPDG---LKALAsdkiqvTVFQDAVGQGKTALAV 270
Cdd:cd01574 167 RRLLDDGPVTAVFAA-NDQMALGALRALHERGLRvpedVSVVGFDDIPEAayfVPPLT------TVRQDFAELGRRAVEL 239
|
250 260
....*....|....*....|....*
gi 488999782 271 ALKLIKGEK-VESHVWIPFELVTKE 294
Cdd:cd01574 240 LLALIEGPApPPESVLLPPELVVRE 264
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
35-241 |
1.99e-06 |
|
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380632 [Multi-domain] Cd Length: 264 Bit Score: 48.29 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 35 FLTIIRqSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSaSTPQLTKMaQQAKMPLVYVNRTPGD 114
Cdd:cd19977 14 FTSVVR-GIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGG-NEDLIEKL-VKSGIPVVFVDRYIPG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 115 KTLPpgvvFVGSDERESGTLQMEALAKLaNYKgNVAIMIGNLTDAGALQRTKDVEQVVAKY------PAMKVVQKQpany 188
Cdd:cd19977 91 LDVD----TVVVDNFKGAYQATEHLIEL-GHK-RIAFITYPLELSTRQERLEGYKAALADHglpvdeELIKHVDRQ---- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488999782 189 srSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMALEKSQKK----LLIGGIDATP 241
Cdd:cd19977 161 --DDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRipddIALIGFDDIP 215
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
24-291 |
2.11e-06 |
|
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: 47.87 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVdpvdSAS--TPQLTKMAQQA 101
Cdd:cd01542 2 IGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIIL----FATeiTDEHRKALKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 102 KMPLVYVnrtpGDKTlpPGVVFVGSDERESGTLQMEALAKLaNYKgNVAiMIG-NLTD-AGALQRTKDVEQVVAKYPAMK 179
Cdd:cd01542 78 KIPVVVL----GQEH--EGFSCVYHDDYGAGKLLGEYLLKK-GHK-NIA-YIGvDEEDiAVGVARKQGYLDALKEHGIDE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 180 VVQKQpANYSRSEGMDLMQN-WTGNgeAIDIVAANNDEMAIGAAMALEKSQKK----LLIGGIDATPdgLKALASDKIqV 254
Cdd:cd01542 149 VEIVE-TDFSMESGYEAAKElLKEN--KPDAIICATDNIALGAIKALRELGIKipedISVAGFGGYD--LSEFVSPSL-T 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488999782 255 TV---FQDAvgqGKTALAVALKLIKGEKVESHVWIPFELV 291
Cdd:cd01542 223 TVkfdYEEA---GEKAAELLLDMIEGEKVPKKQKLPYELI 259
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
42-294 |
4.03e-06 |
|
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380522 [Multi-domain] Cd Length: 268 Bit Score: 47.27 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 42 SIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVdSASTPQLTKmAQQAKMPLVYVNRTPGDktlPPGV 121
Cdd:cd06299 20 GIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPT-GENSEGLQA-LIAQGLPVVFVDREVEG---LGGV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 122 VFVGSDERESGTLQMEALAKLANYKgnVAIMIGNLTDAGALQRTKD----VEQVVAKYPAMKVVQKqpaNYSRSEGMDLM 197
Cdd:cd06299 95 PVVTSDNRPGAREAVEYLVSLGHRR--IGYISGPLSTSTGRERLAAfraaLTAAGIPIDEELVAFG---DFRQDSGAAAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 198 QNWTGNGEAIDIVAANNDEMAIGAAMALEksQKKLLIG------GIDATPdgLKALASDKIQVtVFQDAVGQGKTALAVA 271
Cdd:cd06299 170 HRLLSRGDPPTALIAGDSLMALGAIQALR--ELGLRIGddvsliSFDDVP--WFELLSPPLTV-IAQPVERIGRRAVELL 244
|
250 260
....*....|....*....|....
gi 488999782 272 LKLIK-GEKVESHVwIPFELVTKE 294
Cdd:cd06299 245 LALIEnGGRATSIR-VPTELIPRE 267
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
46-202 |
4.59e-06 |
|
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
Pssm-ID: 380498 [Multi-domain] Cd Length: 264 Bit Score: 47.20 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 46 EAQARHVDVQF------EDArgDTGRQAdqVQSFIASGVDAIIVDPvdSASTPQLTKMAQQAKMPLVYVNRtPGDKTLPP 119
Cdd:cd06274 22 ERLARERGLQLliacsdDDP--EQERRL--VENLIARQVDGLIVAP--STPPDDIYYLCQAAGLPVVFLDR-PFSGSDAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 120 GVVfvgSDERESGTLQMEALAKLAnyKGNVAIMIGNLTDAGALQRTKDVEQVVAKY-PAMKVVQKQPANYSRSEGMDLMQ 198
Cdd:cd06274 95 SVV---SDNRAGARALTEKLLAAG--PGEIYFLGGRPELPSTAERIRGFRAALAEAgITEGDDWILAEGYDRESGYQLMA 169
|
....
gi 488999782 199 NWTG 202
Cdd:cd06274 170 ELLA 173
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
38-225 |
8.44e-06 |
|
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: 46.39 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 38 IIRQsIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIvdpVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTL 117
Cdd:cd06288 18 IIRG-AQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGII---YASMHHREVTLPPELTDIPLVLLNCFDDDPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 118 pPGVVFvgsDERESGTLQMEALAKlANYKgNVAIMIGNLTDAGALQRTKDVEQVVAK----YPAMKVVQkqpANYSRSEG 193
Cdd:cd06288 94 -PSVVP---DDEQGGYLATRHLIE-AGHR-RIAFIGGPEDSLATRLRLAGYRAALAEagipYDPSLVVH---GDWGRESG 164
|
170 180 190
....*....|....*....|....*....|..
gi 488999782 194 MDLMQNWTGNGEAIDIVAANNDEMAIGAAMAL 225
Cdd:cd06288 165 YEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAA 196
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
24-131 |
9.14e-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: 46.00 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQNFLTIIRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVdsASTPQLTKMAQQAKM 103
Cdd:cd06283 2 IGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPT--GNNNDAYLELAQKGL 79
|
90 100
....*....|....*....|....*...
gi 488999782 104 PLVYVNRtpgdKTLPPGVVFVGSDERES 131
Cdd:cd06283 80 PVVLVDR----QIEPLNWDTVVTDNYDA 103
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
24-225 |
1.28e-05 |
|
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380489 [Multi-domain] Cd Length: 269 Bit Score: 45.95 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGV---SMAyfDQNFLTIIrQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVdpVDSASTPQLTKMAQQ 100
Cdd:cd01575 2 VAVvvpSLS--NSVFAETL-QGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLIL--TGTEHTPATRKLLRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 101 AKMPLVYVnrtpGDKTLPPGVVFVGSDERESGTLQMEALAKlANYKgNVAImIGNLTDAG--ALQRTKDVEQVVAKY--- 175
Cdd:cd01575 77 AGIPVVET----WDLPDDPIDMAVGFSNFAAGRAMARHLIE-RGYR-RIAF-VGARLDGDsrARQRLEGFRDALAEAglp 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488999782 176 PAMKVVQKQPAnySRSEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAMAL 225
Cdd:cd01575 150 LPLVLLVELPS--SFALGREALAELLARHPDLDAIFCSNDDLALGALFEC 197
|
|
| PBP1_YraM_LppC_lipoprotein-like |
cd06339 |
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup ... |
39-121 |
1.54e-05 |
|
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup includes periplasmic binding component of lipoprotein LppC, an immunodominant antigen, whose molecular function is not characterized. Members of this subgroup are predicted to be involved in transport of lipid compounds, and they are sequence similar to the family of ABC-type hydrophobic amino acid transporters (HAAT).
Pssm-ID: 380562 [Multi-domain] Cd Length: 331 Bit Score: 45.72 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 39 IRQSIE---KEAQARHVDVQFEDARGDTG-RQAdqVQSFIASGVDAIIvDPVDSASTPQLTKMAQQAKMPLVYVNRTPGD 114
Cdd:cd06339 19 IRDGIElalFDAGGSRPELRVYDTGGPEGaAAA--YQQAVAEGADLII-GPLLKSSVAALAAAAQALGVPVLALNNDESA 95
|
....*..
gi 488999782 115 kTLPPGV 121
Cdd:cd06339 96 -TAGPGL 101
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-291 |
6.00e-05 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 43.65 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 62 DTGRQADQVQSFIASGVDAIIVdpVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTLPpgvvFVGSDERESGTLQMEALAK 141
Cdd:cd06273 40 DPARELEQVRALIERGVDGLIL--VGSDHDPELFELLEQRQVPYVLTWSYDEDSPHP----SIGFDNRAAAARAAQHLLD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 142 LanykGNVAI-MIGNLTDAG--ALQRTKDVEQVVAKY----PAMKVVQkqpANYSRSEGMDLMQNWTGNGEAIDIVAANN 214
Cdd:cd06273 114 L----GHRRIaVISGPTAGNdrARARLAGIRDALAERglelPEERVVE---APYSIEEGREALRRLLARPPRPTAIICGN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 215 DEMAIGAAMALEKS----QKKLLIGGIDATPdglkaLASDkIQV---TVFQDAVGQGKTALAVALKLIKGEKVESHVWIP 287
Cdd:cd06273 187 DVLALGALAECRRLgisvPEDLSITGFDDLE-----LAAH-LSPpltTVRVPAREIGELAARYLLALLEGGPPPKSVELE 260
|
....
gi 488999782 288 FELV 291
Cdd:cd06273 261 TELI 264
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
41-278 |
9.31e-05 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 43.04 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 41 QSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLtKMAQQAKMPLVYVNRTPGDKTLPpg 120
Cdd:cd06282 19 QGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSEAL-ELLEEEGVPYVLLFNQTENSSHP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 121 vvFVGSDERESGTLQMEALAKLANYkgNVAIMIGNLTDAG-ALQRTKDVEQVVAK--YPAMKVVQkQPANYSRSEGmDLM 197
Cdd:cd06282 96 --FVSVDNRLASYDVAEYLIALGHR--RIAMVAGDFSASDrARLRYQGYRDALKEagLKPIPIVE-VDFPTNGLEE-ALT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 198 QNWTGNGEAIDIVAAnNDEMAIGAAMALEKSqkklligGIDaTPDGLKALASDKIQV---------TVFQDAVGQGKTAL 268
Cdd:cd06282 170 SLLSGPNPPTALFCS-NDLLALSVISALRRL-------GIR-VPDDVSVIGFDGIAIgelltptlaTVVQPSRDMGRAAA 240
|
250
....*....|
gi 488999782 269 AVALKLIKGE 278
Cdd:cd06282 241 DLLLAEIEGE 250
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
24-112 |
1.43e-04 |
|
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380483 [Multi-domain] Cd Length: 274 Bit Score: 42.54 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 24 IGVSMAYFDQN-FLTIIRQsIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSA----STPQLTKMa 98
Cdd:cd01541 2 IGVITTYIDDYiFPSIIQG-IESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSAlpnpNLDLYEEL- 79
|
90
....*....|....
gi 488999782 99 QQAKMPLVYVNRTP 112
Cdd:cd01541 80 QKKGIPVVFINSYY 93
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
68-225 |
1.49e-04 |
|
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: 42.52 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 68 DQVQSFIASGVDAIIVdpVDSASTPQLTKMAQQAKMPLVYVNRTPGDktlpPGVVFVGSDERESGTLQMEALAKlANYKg 147
Cdd:cd06278 45 DALRQLLQYRVDGVIV--TSATLSSELAEECARRGIPVVLFNRVVED----PGVDSVSCDNRAGGRLAADLLLA-AGHR- 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488999782 148 NVAIMIGNLTDAGALQRTKDVEQVVAKYpAMKVVQKQPANYSRSEGMDLMQNWTGNGEAID-IVAANnDEMAIGAAMAL 225
Cdd:cd06278 117 RIAFLGGPEGTSTSRERERGFRAALAEL-GLPPPAVEAGDYSYEGGYEAARRLLAAPDRPDaIFCAN-DLMALGALDAA 193
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-295 |
5.13e-04 |
|
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: 40.70 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 62 DTGRQADQVQSFIASGVDAIIVDPVdSASTPQLTKMAQQAKMPLVYVNRtpgdKTLPPGVVFVGSDERESGTLQMEALAK 141
Cdd:cd19976 40 DFEREKKYIQELKERNVDGIIIASS-NISDEAIIKLLKEEKIPVVVLDR----YIEDNDSDSVGVDDYRGGYEATKYLIE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 142 LANYKgnVAIMIGNLTDAGALQRTKDVEQV--VAKYPAMKVVQKQpANYSRSEGM----DLMQNwtgngEAIDIVAANND 215
Cdd:cd19976 115 LGHTR--IGCIVGPPSTYNEHERIEGYKNAlqDHNLPIDESWIYS-GESSLEGGYkaaeELLKS-----KNPTAIFAGND 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 216 EMAIGAAMALEKSQKK----LLIGGIDATPdgLKALASDKIqVTVFQDAVGQGKTALAVALKLIKGE--KVESHVwIPFE 289
Cdd:cd19976 187 LIAMGVYRAALELGLKipedLSVIGFDNII--LSEYITPAL-TTIAQPIFEMGQEAAKLLLKIIKNPakKKEEIV-LPPE 262
|
....*.
gi 488999782 290 LVTKEN 295
Cdd:cd19976 263 LIKRDS 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06315 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
41-256 |
6.13e-04 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380538 Cd Length: 278 Bit Score: 40.79 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 41 QSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTLPPG 120
Cdd:cd06315 20 RGVKEAAAALGWKVDVLDGGGTVTGRLAALNQALALKPDGIILGGDDAVELQEPLKKAVKAGIPVVGWHAAASPGPIPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 121 VVF--VGSDERESGTLQmeALAKLANYKGNVAIMIgnLTD---AGALQRTKDVEQVVAKYPAMKVVQKQ--PANYSRSEG 193
Cdd:cd06315 100 GLFtnITTDPREVAETA--AALVIAQSGGKAGVVI--FTDsryAIATAKANAMKKAIEACSGCKVLEYVdiPIADTAQRM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488999782 194 MDLMQNWTGN-GEAIDIVAANNDEMAIGAAMALEKSQKK---LLIGGIDATPDGLKALASDKIQ-VTV 256
Cdd:cd06315 176 PKLIRSLLQRyGDRWTHTLAINDLYFDFAAPALRAAGVEadpVNISAGDGSPSAYDRIRAGEYQvATV 243
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
52-294 |
6.22e-04 |
|
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior.
Pssm-ID: 380526 [Multi-domain] Cd Length: 320 Bit Score: 40.82 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 52 VDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDSASTPQLTKMAQQAKMPLVYVN-RTPGDKTL--PPgVVFVGSDE 128
Cdd:cd06303 63 LDEFFTRPGAEIRLQALQIREMLKSDPDYLIFTLDALRHRRFVEILLDSGKPKLILQNiTTPLRDWDnhQP-LLYVGFDH 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 129 RESGTLQMEALAKLANYKGNVAIMIGnltDAGAL--QRTKDVEQVVAKYPAMKVVQKQPANYSRSEGMDLMQNWTGNGEA 206
Cdd:cd06303 142 AEGSRMLAKHFIKIFPEEGKYAILYL---TEGYVsdQRGDTFIDEVARHSNLELVSAYYTDFDRESAREAARALLARHPD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 207 IDIVAANNDEMAIGAAMALEKSQK--KLLIGGIDATPDGLKALASDKIQVTVFQ--DAVGqgkTALAVALKL-IKGEKVE 281
Cdd:cd06303 219 LDFIYACSTDIALGAIDALQELGRetDIMINGWGGGSAELDALQKGGLDVTVMRmnDDNG---IAMAEAIKLdLEGREVP 295
|
250
....*....|...
gi 488999782 282 SHVWIPFELVTKE 294
Cdd:cd06303 296 TVYAGDFELVTKG 308
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
43-225 |
2.96e-03 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 38.41 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 43 IEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVDPVDsASTPQLTKMAQQAkMPLVYVNRTPGDKTLPPgvv 122
Cdd:cd06293 21 VEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSD-DDLSHLARLRARG-TAVVLLDRPAPGPAGCS--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 123 fVGSDERESGTLQMEALAKLanykGNVAIM-IGNLTD--------AGALQRTKDVEQVvakyPAMKVVQKQPANYSRSEG 193
Cdd:cd06293 96 -VSVDDVQGGALAVDHLLEL----GHRRIAfVSGPLRtrqvaerlAGARAAVAEAGLD----PDEVVRELSAPDANAELG 166
|
170 180 190
....*....|....*....|....*....|..
gi 488999782 194 MDLMQNWTGNGEAIDIVAANNDEMAIGAAMAL 225
Cdd:cd06293 167 RAAAAQLLAMPPRPTAVFAANDLLALGLLAGL 198
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
50-175 |
5.43e-03 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 38.02 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 50 RHVDVQFEDARGDTGRQADQVQSFIAS-GVDAIIvDPVDSASTPQLTKMAQQAKMPLVYVNRTPGDKTlPPGVVFVGSDE 128
Cdd:pfam13458 41 RKIELVVADDQGDPDVAAAAARRLVDQdGVDAIV-GGVSSAVALAVAEVLAKKGVPVIGPAALTGEKC-SPYVFSLGPTY 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488999782 129 RESGTLQMEALAKlaNYKGNVAIMIGNLTDAGALQRtKDVEQVVAKY 175
Cdd:pfam13458 119 SAQATALGRYLAK--ELGGKKVALIGADYAFGRALA-AAAKAAAKAA 162
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
66-227 |
6.28e-03 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 37.70 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 66 QADQVQSFIASGVDAIIVdpVDSASTPQLTKMAQQAKMPLVYVNrtpgDKTLPPGVVFVGSDERESGTlQMEAlAKLANY 145
Cdd:PRK14987 108 EQERLESMLSWNIDGLIL--TERTHTPRTLKMIEVAGIPVVELM----DSQSPCLDIAVGFDNFEAAR-QMTT-AIIARG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 146 KGNVAIMiGNLTDAGALQRTKDVEQVV--AKYPAMKVVQKQPANYSrsEGMDLMQNWTGNGEAIDIVAANNDEMAIGAAM 223
Cdd:PRK14987 180 HRHIAYL-GARLDERTIIKQKGYEQAMldAGLVPYSVMVEQSSSYS--SGIELIRQARREYPQLDGVFCTNDDLAVGAAF 256
|
....
gi 488999782 224 ALEK 227
Cdd:PRK14987 257 ECQR 260
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
39-293 |
7.28e-03 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 37.58 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 39 IRQSIEKEAQARHVDVQFEDARGDTGRQADQVQSFIASGVDAIIVdpvdsASTPQLTKMAQQAK-MPLVY--VNRTPGDK 115
Cdd:COG2984 23 FKDGLAEAGYGKNLKLDYQNAQGDQATAAQIAAKLVADKPDLIVA-----IGTPAAQAAANATKdIPVVFtaVTDPVGAG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 116 TLP----PGVVFVGSDERESGTLQMEALAKLANYKGNVAImIGNLTDAGALQRTKDVEQVVAKYPaMKVVQKQPANYSrs 191
Cdd:COG2984 98 LVKslekPGGNVTGVSDLLPIEKQLELIKKLLPDAKRIGV-LYNPSEANSVAQVEELKKAAKKLG-LELVEATVTSSN-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999782 192 egmDLMQNWTGNGEAIDIVAANNDEM---AIGAAMALEKSQKKLLIGGIDATP-DGlkALASdkiqvtVFQDAVGQGKTA 267
Cdd:COG2984 174 ---EIQQALQSLAGKVDAIYVPTDNTvvsALEAIAKVAARAKIPVFGGDDSSVkAG--ALAG------YGIDYYELGRQA 242
|
250 260
....*....|....*....|....*.
gi 488999782 268 LAVALKLIKGEKVEShvwIPFELVTK 293
Cdd:COG2984 243 AEMALRILKGEKPAD---IPVETPKK 265
|
|
| |
