|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-295 |
0e+00 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 552.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 1 MKLNKLATLFTAFALTATVSVNAMAKESIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTV 80
Cdd:PRK10653 1 MNMKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 81 RGTKLMLINPTDSDAVGNSILMANKAKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGT 160
Cdd:PRK10653 81 RGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIAKKLGEGAKVIQLEGIAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 161 SAARERGEGFNAGAKEHKFNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRDDVLVVGFD 240
Cdd:PRK10653 161 SAARERGEGFKQAVAAHKFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 493711027 241 GTNDGIKAVQGGKLGATIAQRPDQIGIVGVQIADKVLKGEKVEATVPVELELVVK 295
Cdd:PRK10653 241 GTPDGIKAVNRGKLAATIAQQPDQIGAIGVETADKVLKGEKVEAKIPVDLKLVTK 295
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
28-294 |
1.40e-135 |
|
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: 384.34 E-value: 1.40e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGF-NAGAKEHKFNVLASQP 186
Cdd:cd06323 81 IPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFhNAIAKYPKINVVASQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 187 ADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRDDVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQIG 266
Cdd:cd06323 161 ADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQPEEMG 240
|
250 260
....*....|....*....|....*...
gi 493711027 267 IVGVQIADKVLKGEKVEATVPVELELVV 294
Cdd:cd06323 241 AKAVETADKYLKGEKVPKKIPVPLKLVT 268
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
29-292 |
4.66e-91 |
|
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: 271.36 E-value: 4.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd01536 2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAAN-KGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH-KFNVLASQP 186
Cdd:cd01536 82 PVVAVDTDIDgGGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYpDIEIVAEQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 187 ADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQI 265
Cdd:cd01536 162 ANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRtGDIKIVGVDGTPEALKAIKDGELDATVAQDPYLQ 241
|
250 260
....*....|....*....|....*..
gi 493711027 266 GIVGVQIADKVLKGEKVEATVPVELEL 292
Cdd:cd01536 242 GYLAVEAAVKLLNGEKVPKEILTPVTL 268
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
6-295 |
1.45e-90 |
|
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: 271.41 E-value: 1.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 6 LATLFTAFALTATVSVNAMAKE-SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTK 84
Cdd:COG1879 12 LALALAACGSAAAEAAAAAAKGkTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 85 LMLINPTDSDAVGNSILMANKAKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAAR 164
Cdd:COG1879 92 AIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAAN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 165 ERGEGFNAGAKEH-KFNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGT 242
Cdd:COG1879 172 ERTDGFKEALKEYpGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRkGDVKVVGFDGS 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 493711027 243 NDGIKAVQGGKLGATIAQRPDQIGIVGVQIADKVLKGEKVEATVPVELELVVK 295
Cdd:COG1879 252 PEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTK 304
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
29-293 |
6.09e-75 |
|
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: 230.95 E-value: 6.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd06309 2 VGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAAN---KGEVVSHVASDNRMGGKMAADFIAKKTGND-AKVIQLEGISGTSAARERGEGFNAGAKEH-KFNVLA 183
Cdd:cd06309 82 PVILVDRTIDgedGSLYVTFIGSDFVEEGRRAAEWLVKNYKGGkGNVVELQGTAGSSVAIDRSKGFREVIKKHpNIKIVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 184 SQPADFDRTKGLNVMQNLLTAHP-AVQAVFAQNDEMALGALRALQTAGRD---DVLVVGFDGTNDGIKAVQGGKLGATIA 259
Cdd:cd06309 162 SQSGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLKpgkDVLVVGIDGQKDALEAIKAGELNATVE 241
|
250 260 270
....*....|....*....|....*....|....
gi 493711027 260 QRPDQiGIVGVQIADKVLKGEKVEATVPVELELV 293
Cdd:cd06309 242 CNPLF-GPTAFDTIAKLLAGEKVPKLIIVEERLF 274
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
29-283 |
2.93e-73 |
|
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: 226.11 E-value: 2.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd19968 2 IGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAG-AKEHKFNVLASQPA 187
Cdd:cd19968 82 PVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEElAAGPKIKVVFEQTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 188 DFDRTKGLNVMQNLLTAHPA-VQAVFAQNDEMALGALRALQTAGRD--DVLVVGFDGTNDGIKAVQGGKLGATIAQRPD- 263
Cdd:cd19968 162 NFERDEGLTVMENILTSLPGpPDAIICANDDMALGAIEAMRAAGLDlkKVKVIGFDAVPDALQAIKDGELYATVEQPPGg 241
|
250 260
....*....|....*....|
gi 493711027 264 QIGIVGVQIADKVLKGEKVE 283
Cdd:cd19968 242 QARTALRILVDYLKDKKAPK 261
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
29-293 |
7.77e-72 |
|
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: 222.58 E-value: 7.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd19967 2 VAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAAN-KGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH-KFNVLASQP 186
Cdd:cd19967 82 PVFLIDREINaEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQYpELKMVAQQS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 187 ADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQI 265
Cdd:cd19967 162 ADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRaGDVIIVGFDGSNDVRDAIKEGKISATVLQPAKLI 241
|
250 260 270
....*....|....*....|....*....|
gi 493711027 266 GIVGVQIADKVLKGEK--VEATVPVELELV 293
Cdd:cd19967 242 ARLAVEQADQYLKGGStgKEEKQLFDCVLI 271
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
29-293 |
1.52e-71 |
|
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: 221.65 E-value: 1.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADK-LGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd06308 2 IGFSQCSLNDPWRAAMNEEIKAEAAKyPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGF-NAGAKEHKFNVLASQP 186
Cdd:cd06308 82 IPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFlEAIAKYPGIKIVASQD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 187 ADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTND-GIKAVQGGKLGATIaqRPDQ 264
Cdd:cd06308 162 GDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGLPEaGEKAVKDGILAATF--LYPT 239
|
250 260
....*....|....*....|....*....
gi 493711027 265 IGIVGVQIADKVLKGEKVEATVPVELELV 293
Cdd:cd06308 240 GGKEAIEAALKILNGEKVPKEIVLPTPLI 268
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
29-296 |
3.55e-69 |
|
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: 215.97 E-value: 3.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLG--YELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKA 106
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGvkVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLDRA-------ANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKE-HK 178
Cdd:cd06320 82 GIPVINLDDAvdadalkKAGGKVTSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKKaPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 179 FNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGAT 257
Cdd:cd06320 162 LKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKtGKVLVVGTDGIPEAKKSIKAGELTAT 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 493711027 258 IAQRPDQIGIVGVQIADKVLKGEKVEATVPVELELVVKQ 296
Cdd:cd06320 242 VAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKD 280
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
29-294 |
5.00e-69 |
|
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: 215.22 E-value: 5.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH-KFNVLASQPA 187
Cdd:cd06322 82 PVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKALLGGGGKIAIIDYPEVESVVLRVNGFKEAIKKYpNIEIVAEQPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 188 DFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQ-GGKLGATIAQRPDQI 265
Cdd:cd06322 162 DGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKeDKIKVIGFDGNPEAIKAIAkGGKIKADIAQQPDKI 241
|
250 260
....*....|....*....|....*....
gi 493711027 266 GIVGVQIADKVLKGEKVEATVPVELELVV 294
Cdd:cd06322 242 GQETVEAIVKYLAGETVEKEILIPPKLYT 270
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
29-292 |
1.75e-66 |
|
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: 208.59 E-value: 1.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd19971 2 FGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRA-ANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSaARERGEGFNAGAKEH-KFNVLASQP 186
Cdd:cd19971 82 PVINVDTPvKDTDLVDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLDHPTAES-CVDRIDGFLDAIKKNpKFEVVAQQD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 187 ADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQI 265
Cdd:cd19971 161 GKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKlGDILVYGVDGSPDAKAAIKDGKMTATAAQSPIEI 240
|
250 260
....*....|....*....|....*..
gi 493711027 266 GIVGVQIADKVLKGEKVEATVPVELEL 292
Cdd:cd19971 241 GKKAVETAYKILNGEKVEKEIVVPTFL 267
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
27-293 |
1.39e-63 |
|
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: 201.31 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 27 ESIALVISTLNNPFFVTMKDAAQKEADK-LGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANK 105
Cdd:cd06301 1 IKIGVSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRA-ANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH-KFNVLA 183
Cdd:cd06301 81 AGIPLVYVNREpDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYpGMKIVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 184 SQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRP 262
Cdd:cd06301 161 EQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKkDDILVAGIDATPDALKAMKAGRLDATVFQDA 240
|
250 260 270
....*....|....*....|....*....|.
gi 493711027 263 DQIGIVGVQIADKVLKGEKVEATVPVELELV 293
Cdd:cd06301 241 AGQGETAVDVAVKAAKGEEVESDIWIPFELV 271
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
29-296 |
1.24e-62 |
|
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: 199.03 E-value: 1.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd06313 2 IGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGF-NAGAKEHKFNVLASQPA 187
Cdd:cd06313 82 PLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIeNVLKKYPDIKVLAEQTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 188 DFDRTKGLNVMQNLLTAHPA-VQAVFAQNDEMALGALRALQTAGRDDVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQIG 266
Cdd:cd06313 162 NWSRDEAMSLMENWLQAYGDeIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDALQAVKSGELIATVLQDAEAQG 241
|
250 260 270
....*....|....*....|....*....|
gi 493711027 267 IVGVQIADKVLKGEKVEATVPVELELVVKQ 296
Cdd:cd06313 242 KGAVEVAVDAVKGEGVEKKYYIPFVLVTKD 271
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
29-292 |
1.51e-62 |
|
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: 198.63 E-value: 1.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADK-LGYELIV--LDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANK 105
Cdd:cd19970 2 VALVMKSLANEFFIEMEKGARKHAKEaNGYELLVkgIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLD------RAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEHKF 179
Cdd:cd19970 82 AGIAVINIDnrldadALKEGGINVPFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAGM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 180 NVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATI 258
Cdd:cd19970 162 KIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKaGKVLVVGFDNIPAVRPLLKDGKMLATI 241
|
250 260 270
....*....|....*....|....*....|....
gi 493711027 259 AQRPDQIGIVGVQIADKVLKGEKVEATVPVELEL 292
Cdd:cd19970 242 DQHPAKQAVYGIEYALKMLNGEEVPGWVKTPVEL 275
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
29-282 |
3.66e-61 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 195.71 E-value: 3.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd06318 2 IGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAAN-KGEVVSHVASDNRMGGKMAADFIAKKTGNDA-KVIQLEGISGTSAARERGEGFNAGAKEH--------K 178
Cdd:cd06318 82 PVITVDSALDpSANVATQVGRDNKQNGVLVGKEAAKALGGDPgKIIELSGDKGNEVSRDRRDGFLAGVNEYqlrkygksN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 179 FNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRDD-VLVVGFDGTNDGIKAVQGGKLGAT 257
Cdd:cd06318 162 IKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDkVKVAGADGQKEALKLIKDGKYVAT 241
|
250 260
....*....|....*....|....*
gi 493711027 258 IAQRPDQIGIVGVQIADKVLKGEKV 282
Cdd:cd06318 242 GLNDPDLLGKTAVDTAAKVVKGEES 266
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
29-296 |
8.43e-58 |
|
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: 186.80 E-value: 8.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd06319 2 IGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKK------TGNDAKVIQLEgiSGTSAARERGEGFNAGAKEHKFNVL 182
Cdd:cd06319 82 PVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIP--QSRVNGQARTAGFEDALEEAGVEEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 183 A-SQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRD-DVLVVGFDGTNDGIKAVQGGKLGATIAQ 260
Cdd:cd06319 160 AlRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTgDILVVGFDGDPEALDLIKDGKLDGTVAQ 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 493711027 261 RPDQIGIVGVQIADKVLKGEK-VEATVPVELELVVKQ 296
Cdd:cd06319 240 QPFGMGARAVELAIQALNGDNtVEKEIYLPVLLVTSE 276
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-293 |
1.21e-56 |
|
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: 183.64 E-value: 1.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGY--ELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANK 105
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPgaKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRAANKgeVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISgTSAARERGEGFNAGAKEHK-FNVLAS 184
Cdd:cd06321 81 AGIIVVAVDVAAEG--ADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPP-VSAVIDRVNGCKEALAEYPgIKLVDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 185 QPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRDDVLVVGFDGTNDGIKAVQ--GGKLGATIAQRP 262
Cdd:cd06321 158 QNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSVDGSPEAVAALKreGSPFIATAAQDP 237
|
250 260 270
....*....|....*....|....*....|..
gi 493711027 263 DQIGIVGVQIADKVLKGEKV-EATVPVELELV 293
Cdd:cd06321 238 YDMARKAVELALKILNGQEPaPELVLIPSTLV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
29-293 |
3.56e-54 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 177.25 E-value: 3.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd19972 2 IGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH-KFNVLASQPA 187
Cdd:cd19972 82 PVIAVDRNPEDAPGDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAEApGIKVVAEQTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 188 DFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRD-DVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQIG 266
Cdd:cd19972 162 DWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDhKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKMG 241
|
250 260
....*....|....*....|....*..
gi 493711027 267 IVGVQIADKVLKGEKVEATVPVELELV 293
Cdd:cd19972 242 RLAVDSAIDLLNGKAVPKEQLQDAVLT 268
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
29-281 |
5.47e-52 |
|
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: 171.34 E-value: 5.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVL-DSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVgPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH--KFNVLAS- 184
Cdd:pfam13407 81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKypGIKVVAEv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 185 QPADFDRTKGLNVMQNLLTAHP-AVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRP 262
Cdd:pfam13407 161 EGTNWDPEKAQQQMEALLTAYPnPLDGIISPNDGMAGGAAQALEAAGLaGKVVVTGFDATPEALEAIKDGTIDATVLQDP 240
|
250
....*....|....*....
gi 493711027 263 DQIGIVGVQIADKVLKGEK 281
Cdd:pfam13407 241 YGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-293 |
1.18e-51 |
|
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: 170.60 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVL--DSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANK 105
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVgpESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH--KFNVLA 183
Cdd:cd06310 81 KGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHpgGIKVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 184 SQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG-RDDVLVVGFDGTNDGIKAVQGGKLGATIAQRP 262
Cdd:cd06310 161 SQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKlSGQIKIVGFDSQEELLDALKNGKIDALVVQNP 240
|
250 260 270
....*....|....*....|....*....|.
gi 493711027 263 DQIGIVGVQIADKVLKGEKVEATVPVELELV 293
Cdd:cd06310 241 YEIGYEGIKLALKLLKGEEVPKNIDTGAELI 271
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-293 |
5.72e-48 |
|
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: 161.25 E-value: 5.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVL-DSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKA 106
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQgPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLD-RAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAG-AKEHKFNVLAS 184
Cdd:cd20007 81 GIKVVTVDtTLGDPSFVLSQIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEmKKYPGIKVLGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 185 QPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRPD 263
Cdd:cd20007 161 QYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKtGKVKVVGFDASPAQVEQLKAGTIDALIAQKPA 240
|
250 260 270
....*....|....*....|....*....|
gi 493711027 264 QIGIVGVQIADKVLKGEKVEATVPVELELV 293
Cdd:cd20007 241 EIGYLAVEQAVAALTGKPVPKDILTPFVVI 270
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
3-295 |
2.92e-47 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 160.42 E-value: 2.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 3 LNKLATLFTAFALTATVSVNAMAKESIALVISTLNNPFFVTMKDAAQKEADKLG--YELIVLDSQDNPAKELANVQDLTV 80
Cdd:PRK09701 1 MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGvsVDIFASPSEGDFQSQLQLFEDLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 81 RGTKLMLINPTDSDAVGNSILMANKAKIPVITLDRAAN-------KGEVVSHVASDNRMGGKMAADFIAKKTGNDA-KVI 152
Cdd:PRK09701 81 KNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGgEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 153 QLEGISGTSAARERGEGFN-AGAKEHKFNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR 231
Cdd:PRK09701 161 IIEGKAGNASGEARRNGATeAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493711027 232 D-DVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQIGIVGVQI------ADKVLKGEKVEATVPVELELVVK 295
Cdd:PRK09701 241 TgKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLmvdaekSGKVIPLDKAPEFKLVDSILVTQ 311
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
29-283 |
1.21e-45 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 155.47 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVL--DSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVgNSILMANKA 106
Cdd:cd20008 2 IAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLgpATEADIAGQVNLVENAISRKPDAIVLAPNDTAAL-VPAVEAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAK----KTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH--KFN 180
Cdd:cd20008 81 GIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAEllkaSGGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKypDIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 181 VLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIA 259
Cdd:cd20008 161 IVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKaGKIVLVGFDSSPDEVALLKSGVIKALVV 240
|
250 260
....*....|....*....|....
gi 493711027 260 QRPDQIGIVGVQIADKVLKGEKVE 283
Cdd:cd20008 241 QDPYQMGYEGVKTAVKALKGEEIV 264
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-295 |
1.07e-42 |
|
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: 147.38 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVL--DSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANK 105
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRgpSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH--KFNVLA 183
Cdd:cd20004 81 QGIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAKGSASTTDRERGFLEALKKLapGLKVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 184 SQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRP 262
Cdd:cd20004 161 DQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLaGKVKFIGFDASDLLLDALRAGEISALVVQDP 240
|
250 260 270
....*....|....*....|....*....|...
gi 493711027 263 DQIGIVGVQIADKVLKGEKVEATVPVELELVVK 295
Cdd:cd20004 241 YRMGYLGVKTAVAALRGKPVPKRIDTGVVLVTK 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
29-293 |
4.35e-42 |
|
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: 146.62 E-value: 4.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLG---YELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANK 105
Cdd:cd19996 2 IGFSNAGLGNSWRVQMIAEFEAEAAKLKkliKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEHK-FNVLAS 184
Cdd:cd19996 82 AGIPVVLFDSGVGSDKYTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYPgIKIVGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 185 QPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRDDVLVVGfDGTNDGIKAVQ---GGKLGATIAqr 261
Cdd:cd19996 162 VYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTG-EDNNGFLKAWKelpGFKSIAPSY-- 238
|
250 260 270
....*....|....*....|....*....|..
gi 493711027 262 PDQIGIVGVQIADKVLKGEKVEATVPVELELV 293
Cdd:cd19996 239 PPWLGATALDAALAALEGEPVPKYVYIPLPVI 270
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
28-296 |
1.02e-40 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 144.19 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLT---VRGtkLMLINPTDSDAVgnsILMAN 104
Cdd:COG1609 63 TIGVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLsrrVDG--LILAGSRLDDAR---LERLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 105 KAKIPVITLDRAANkGEVVSHVASDNRMGGKMAADFIAKKtGNDaKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLAS 184
Cdd:COG1609 138 EAGIPVVLIDRPLP-DPGVPSVGVDNRAGARLATEHLIEL-GHR-RIAFIGGPADSSSARERLAGYREALAEAGLPPDPE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 185 Q--PADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTNDGikAVQGGKLgATIA 259
Cdd:COG1609 215 LvvEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLrvpEDVSVVGFDDIPLA--RYLTPPL-TTVR 291
|
250 260 270
....*....|....*....|....*....|....*...
gi 493711027 260 QRPDQIGIVGVQIADKVLKGEKVEA-TVPVELELVVKQ 296
Cdd:COG1609 292 QPIEEMGRRAAELLLDRIEGPDAPPeRVLLPPELVVRE 329
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
29-290 |
1.20e-40 |
|
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: 141.89 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLT---VRGtklmLINPTDSDAVGNSIlmanK 105
Cdd:cd06291 2 IGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKrnkVDG----IILGSHSLDIEEYK----K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRAANKGevVSHVASDNRMGGKMAADFIAKKtgNDAKVIQLEGISGTSAARERGEGFNAGAKEH--KFNVLA 183
Cdd:cd06291 74 LNIPIVSIDRYLSEG--IPSVSSDNYQGGRLAAEHLIEK--GCKKILHIGGPSNNSPANERYRGFEDALKEAgiEYEIIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 184 SQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTNDgikavqgGKLG----A 256
Cdd:cd06291 150 IDENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIrvpEDVQIIGFDGIEI-------SELLypelT 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 493711027 257 TIAQRPDQIGIVGVQIADKVLKGEKVEA---TVPVEL 290
Cdd:cd06291 223 TIRQPIEEMAKEAVELLLKLIEGEEIEEsriVLPVEL 259
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
29-290 |
4.19e-40 |
|
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: 140.34 E-value: 4.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAvgNSILMANKAKI 108
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDD--ELLEELLAAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAANkGEVVSHVASDNRMGGKMAAD-----------FIAkktgndakviqleGISGTSAARERGEGFNAGAKEH 177
Cdd:cd06267 80 PVVLIDRRLD-GLGVDSVVVDNYAGAYLATEhlielghrriaFIG-------------GPLDLSTSRERLEGYRDALAEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 178 KFNVLAS--QPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTndgikavqgg 252
Cdd:cd06267 146 GLPVDPElvVEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLrvpEDISVVGFDDI---------- 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 493711027 253 KLGA-------TIAQRPDQIGIVGVQIADKVLKGEKVEA---TVPVEL 290
Cdd:cd06267 216 PLAAlltppltTVRQPAYEMGRAAAELLLERIEGEEEPPrriVLPTEL 263
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
48-290 |
5.30e-40 |
|
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: 140.58 E-value: 5.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 48 AQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKIPVITLDRAANKGEVVSHVA 127
Cdd:cd06311 21 AEKQAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYDLYVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 128 SDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH-KFNVLASQPADFDRTKGLNVMQNLLTAHP 206
Cdd:cd06311 101 GDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNpGIKILAMQAGDWTREDGLKVAQDILTKNK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 207 AVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGK--LGATIAQRPDQIGiVGVQIADKVLKGEK-- 281
Cdd:cd06311 181 KIDAVWAADDDMAIGVLQAIKEAGRtDIKVMTGGGGSQEYFKRIMDGDpiWPASATYSPAMIA-DAIKLAVLILKGGKtv 259
|
250
....*....|
gi 493711027 282 -VEATVPVEL 290
Cdd:cd06311 260 eKEVIIPSTL 269
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
29-286 |
2.26e-38 |
|
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: 136.17 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQD-NPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd06314 2 FALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH-KFNVLASQP 186
Cdd:cd06314 82 IPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKGSpGIEIVDPLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 187 ADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQI 265
Cdd:cd06314 162 DNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKvGKVKIVGFDTLPETLQGIKDGVIAATVGQRPYEM 241
|
250 260
....*....|....*....|.
gi 493711027 266 GIVGVQIADKVLKGEKVEATV 286
Cdd:cd06314 242 GYLSVKLLYKLLKGGKPVPDV 262
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
29-285 |
4.22e-37 |
|
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: 133.09 E-value: 4.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd19992 2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKK--TGNdakVIQLEGISGTSAARERGEGFNAGAKEH----KFNVL 182
Cdd:cd19992 82 PVISYDRLILNADVDLYVGRDNYKVGQLQAEYALEAvpKGN---YVILSGDPGDNNAQLITAGAMDVLQPAidsgDIKIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 183 ASQPAD-FDRTKGLNVMQNLLTA-HPAVQAVFAQNDEMALGALRALQTAGRDD-VLVVGFDGTNDGIKAVQGGKLGATIA 259
Cdd:cd19992 159 LDQYVKgWSPDEAMKLVENALTAnNNNIDAVLAPNDGMAGGAIQALKAQGLAGkVFVTGQDAELAALKRIVEGTQTMTVW 238
|
250 260
....*....|....*....|....*.
gi 493711027 260 QRPDQIGIVGVQIADKVLKGEKVEAT 285
Cdd:cd19992 239 KDLKELARAAADAAVKLAKGEKPQTT 264
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-259 |
3.96e-36 |
|
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: 131.57 E-value: 3.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVI-STLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTK---LMLINptdSDAVGNSIL-M 102
Cdd:cd06324 1 RVVFINpGKEDEPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARPPKpdyLILVN---EKGVAPELLeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 103 ANKAKIPVITLDR---AANKGEV----------VSHVASDNRMGG-KMAADFIA----KKTGNDAKVIQLEGISGTSAAR 164
Cdd:cd06324 78 AEQAKIPVFLINNdltDEERALLgkprekfkywLGSIVPDNEQAGyLLAKALIKaarkKSDDGKIRVLAISGDKSTPASI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 165 ERGEGFNAGAKEH-KFNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRD---DVLVVGFD 240
Cdd:cd06324 158 LREQGLRDALAEHpDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKpgkDVLVGGID 237
|
250
....*....|....*....
gi 493711027 241 GTNDGIKAVQGGKLGATIA 259
Cdd:cd06324 238 WSPEALQAVKDGELTASVG 256
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-295 |
2.32e-35 |
|
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: 128.65 E-value: 2.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVSHVASDN----RMGGKMAADFIAKKTGNDAKvIQLEGISGTSAARERGEGF-NAGAKEHKFNVL 182
Cdd:cd06317 81 IPVIAYDAVIPSDFQAAQVGVDNleggKEIGKYAADYIKAELGGQAK-IGVVGALSSLIQNQRQKGFeEALKANPGVEIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 183 ASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKA-VQGGKLGATIAQ 260
Cdd:cd06317 160 ATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRqGKIKVFGWDLTKQAIFLgIDEGVLQAVVQQ 239
|
250 260 270
....*....|....*....|....*....|....*
gi 493711027 261 RPDQIGIVGVQIADKVLKGEKVEATVPVELELVVK 295
Cdd:cd06317 240 DPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
29-278 |
3.15e-34 |
|
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: 125.66 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQ---DNpAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANK 105
Cdd:cd19973 2 IGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKidgDN-ATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRAANKGEVV-SHVASDNRMGGKMAADFIAKKTG-NDAKVIQLEGISGTSAARERGEGF-----------NA 172
Cdd:cd19973 81 AGVLVIALDTPTDPIDAAdATFATDNFKAGVLIGEWAKAALGaKDAKIATLDLTPGHTVGVLRHQGFlkgfgidekdpES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 173 GAKEHKFNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRD-DVLVVGFDGTNDGIKAVQG 251
Cdd:cd19973 161 NEDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKEkGVLIVSVDGGCPGVKDVKD 240
|
250 260
....*....|....*....|....*..
gi 493711027 252 GKLGATIAQRPDQIGIVGVQIADKVLK 278
Cdd:cd19973 241 GIIGATSQQYPLRMAALGVEAIAAFAK 267
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
29-286 |
4.74e-34 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 125.05 E-value: 4.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVL--DSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKA 106
Cdd:cd20005 2 IAVISKGFQHQFWKAVKKGAEQAAKELGVKITFEgpDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEHKFN--VLAS 184
Cdd:cd20005 82 GIPVVTFDSGVPSDLPLATVATDNYAAGALAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDikVVNV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 185 QPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRPD 263
Cdd:cd20005 162 QYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKlGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNPY 241
|
250 260
....*....|....*....|...
gi 493711027 264 QIGIVGVQIADKVLKGEKVEATV 286
Cdd:cd20005 242 GMGYKTVKAAVKALKGEEVEKLI 264
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
28-286 |
6.00e-34 |
|
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: 124.72 E-value: 6.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVsHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGiSGTSAARERGEGFNAGAKEHK--FNVLASQ 185
Cdd:cd06305 81 IPVVTFDTDSQVPGVN-NITQDDYALGTLSLGQLVKDLNGEGNIAVFNV-FGVPPLDKRYDIYKAVLKANPgiKKIVAEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 186 PADFDRTKG--LNVMQNLLTAHPA--VQAVFAQNDEMALGALRALQTAGRDDVLVVGFDGTNDGIKAVQ--GGKLGATIA 259
Cdd:cd06305 159 GDVTPNTAAdaQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISNQDLELMAdeGSPWVATAA 238
|
250 260
....*....|....*....|....*..
gi 493711027 260 QRPDQIGIVGVQIADKVLKGEKVEATV 286
Cdd:cd06305 239 QDPALIGTVAVRNVARKLAGEDLPDKY 265
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
28-282 |
7.72e-34 |
|
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: 125.00 E-value: 7.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLG-YELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKA 106
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGkIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLDR-----AANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAK-------VIQ---LEGISGTSAARERGEGFN 171
Cdd:cd01539 82 NIPVIFFNRepsreDLKSYDKAYYVGTDAEESGIMQGEIIADYWKANPEidkngdgKIQyvmLKGEPGHQDAIARTKYSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 172 AGAKEH--KFNVLASQPADFDRTKGLNVMQNLLTAHPA-VQAVFAQNDEMALGALRALQTAGRDD------VLVVGFDGT 242
Cdd:cd01539 162 KTLNDAgiKTEQLAEDTANWDRAQAKDKMDAWLSKYGDkIELVIANNDDMALGAIEALKAAGYNTgdgdkyIPVFGVDAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 493711027 243 NDGIKAVQGGKLGATIAQRPDQIGIVGVQIADKVLKGEKV 282
Cdd:cd01539 242 PEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEP 281
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
25-285 |
2.16e-32 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 121.40 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 25 AKESIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMAN 104
Cdd:COG4213 1 GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 105 KAKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAK--VIQLEGISGTSAARErgegFNAGAKE------ 176
Cdd:COG4213 81 AAGIPVIAYDRLILNSDVDYYVSFDNVKVGELQGQYLVDGLPLKGKgnIELFGGSPTDNNATL----FFEGAMSvlqpyi 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 177 --HKFNVLASQPA-DFDRTKGLNVMQNLLTAHPA-VQAVFAQNDEMALGALRALQTAGRD-DVLVVGFDGTNDGIKAVQG 251
Cdd:COG4213 157 dsGKLVVVSGQWTlGWDPETAQKRMENLLTANGNkVDAVLAPNDGLAGGIIQALKAQGLAgKVVVTGQDAELAAVQRILA 236
|
250 260 270
....*....|....*....|....*....|....
gi 493711027 252 GKLGATIAQRPDQIGIVGVQIADKVLKGEKVEAT 285
Cdd:COG4213 237 GTQYMTVYKDTRELAEAAAELAVALAKGEKPEVN 270
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
29-242 |
5.68e-31 |
|
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: 116.48 E-value: 5.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYE--LIVLDSQDNPAKELANVQDLTVRGtkLMLINPTDSDAVgnsILMANKA 106
Cdd:cd06278 2 VGVVVGDLSNPFYAELLEELSRALQARGLRplLFNVDDEDDVDDALRQLLQYRVDG--VIVTSATLSSEL---AEECARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLDRAANkGEVVSHVASDNRMGGKMAADFIAKKTGndAKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLASQP 186
Cdd:cd06278 77 GIPVVLFNRVVE-DPGVDSVSCDNRAGGRLAADLLLAAGH--RRIAFLGGPEGTSTSRERERGFRAALAELGLPPPAVEA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 187 ADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR----DDVLVVGFDGT 242
Cdd:cd06278 154 GDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGlvvpEDISVVGFDDI 213
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
29-295 |
5.97e-31 |
|
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: 116.93 E-value: 5.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVI--STLNNPFFVTMKDAAQKEADKLGYELIVL--DSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMAN 104
Cdd:cd20006 2 IALILksSDPNSDFWQTVKSGAEAAAKEYGVDLEFLgpESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 105 KAKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEHKF-NVLA 183
Cdd:cd20006 82 KAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQALAEYPNiKIVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 184 SQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRP 262
Cdd:cd20006 162 TEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLgGKVKVVGFDSSVEEIQLLEEGIIDALVVQNP 241
|
250 260 270
....*....|....*....|....*....|...
gi 493711027 263 DQIGIVGVQIADKVLKGEKVEATVPVELELVVK 295
Cdd:cd20006 242 FNMGYLSVQAAVDLLNGKKIPKRIDTGSVVITK 274
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
28-293 |
1.42e-30 |
|
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.
Pssm-ID: 380529 [Multi-domain] Cd Length: 269 Bit Score: 115.76 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQ--DNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANK 105
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGgyTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDA-KVIQLEGISGTSAARERGEGFNAGAKEHKFNVLAS 184
Cdd:cd06306 81 AGIPVIDLVNGIDSPKVAARVLVDFYDMGYLAGEYLVEHHPGKPvKVAWFPGPAGAGWAEDREKGFKEALAGSNVEIVAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 185 QPADFDRTKGLNVMQNLLTAHPAVQAVFAqNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRPD 263
Cdd:cd06306 161 KYGDTGKAVQLNLVEDALQAHPDIDYIVG-NAVAAEAAVGALREAGLtGKVKVVSTYLTPGVYRGIKRGKILAAPSDQPV 239
|
250 260 270
....*....|....*....|....*....|
gi 493711027 264 QIGIVGVQIADKVLKGEKVEATVPVELELV 293
Cdd:cd06306 240 LQGRIAVDQAVRALEGKPVPKHVGPPILVV 269
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
28-290 |
3.15e-30 |
|
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: 114.66 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDavGNSILMANKAK 107
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGP--SRELKRLLKHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAAnKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQleGISGTSAARERGEGFNAGAKEHKFNVLAS--Q 185
Cdd:cd06280 79 IPIVLIDREV-EGLELDLVAGDNREGAYKAVKHLIELGHRRIGLIT--GPLEISTTRERLAGYREALAEAGIPVDESliF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 186 PADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG---RDDVLVVGFDgtNDGIKAVQGGKLGAtIAQRP 262
Cdd:cd06280 156 EGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGleiPQDISVVGFD--DSDWFEIVDPPLTV-VAQPA 232
|
250 260 270
....*....|....*....|....*....|.
gi 493711027 263 DQIGIVGVQIADKVLKGEKVEAT---VPVEL 290
Cdd:cd06280 233 YEIGRIAAQLLLERIEGQGEEPRrivLPTEL 263
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
47-282 |
2.03e-28 |
|
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: 110.86 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 47 AAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKIPVITLDRAANKGEVVShV 126
Cdd:cd19999 25 AAEYKEEGVISDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPVSSPDAIN-V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 127 ASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEHK-FNVLASQPADFDRTKGLNVMQNLLTAH 205
Cdd:cd19999 104 VIDQYKWAAIQAQWLAEQLGGKGNIVAINGVAGNPANEARVKAADDVFAKYPgIKVLASVPGGWDQATAQQVMATLLATY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 206 PAVQAVFAQnDEMALGALRALQTAGRDDVLVVGfDGTNDGI---KAVQGGKLGATIAQRPDQIGIVGVQIADKVLKGEKV 282
Cdd:cd19999 184 PDIDGVLTQ-DGMAEGVLRAFQAAGKDPPVMTG-DYRKGFLrkwKELDLPDFESIGVVNPPGIGATALRIAVRLLQGKEL 261
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
44-281 |
4.79e-28 |
|
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: 109.72 E-value: 4.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 44 MKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKIPVITLDRAANKGEVV 123
Cdd:cd06300 22 KADAAQSGQKGLVKELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGAVTSPDAY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 124 sHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAG-AKEHKFNVLASQPADFDRTKGLNVMQNLL 202
Cdd:cd06300 102 -NVSNDQVEWGRLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEAlAEYPGIKVVGEVFGGWDEATAQTAMLDFL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 203 TAHPAVQAVFAQNDEmALGALRALQTAGRDDVLVVGFDGTNDGIKAVQGGKLGATIAQ--RPDQIGIVGVQIADKVLKGE 280
Cdd:cd06300 181 ATHPQVDGVWTQGGE-DTGVLQAFQQAGRPPVPIVGGDENGFAKQWWKHPKKGLTGAAvwPPPAIGAAGLEVALRLLEGQ 259
|
.
gi 493711027 281 K 281
Cdd:cd06300 260 G 260
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-296 |
1.49e-27 |
|
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: 107.70 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDavgNSILMANKAK 107
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGD---EELLKLLAEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVShVASDNRMGGKMAADFIAKKtGNdAKVIQLEGISGTSAARERGEGF-----NAGAKEHKFNVL 182
Cdd:cd06290 78 IPVVLVDRELEGLNLPV-VNVDNEQGGYNATNHLIDL-GH-RRIVHISGPEDHPDAQERYAGYrraleDAGLEVDPRLIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 183 asqPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTndgikavqggkLGA--- 256
Cdd:cd06290 155 ---EGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIrvpDDVSVIGFDDL-----------PFSkyt 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 493711027 257 -----TIAQRPDQIGIVGVQIADKVLKGEKVEATVPV-ELELVVKQ 296
Cdd:cd06290 221 tppltTVRQPLYEMGKTAAEILLELIEGKGRPPRRIIlPTELVIRE 266
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
28-296 |
5.89e-27 |
|
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: 106.07 E-value: 5.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINP---TDSDAvgnsILMAN 104
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSralSDEEL----ILIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 105 KaKIPVITLDRAANKgevVSH--VASDNRMGGKMAADFIAKKTGNDAKVIQleGISGTSAARERGEGFNAGAKEH--KFN 180
Cdd:cd06270 77 K-IPPLVVINRYIPG---LADrcVWLDNEQGGRLAAEHLLDLGHRRIACIT--GPLDIPDARERLAGYRDALAEAgiPLD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 181 VLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDgtNDGIKAVQGGKLgAT 257
Cdd:cd06270 151 PSLIIEGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIkvpEDVSVIGFD--DVPLARYLSPKL-TT 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 493711027 258 IAQRPDQIGIVGVQIADKVLKGEKVEATVPVELELVVKQ 296
Cdd:cd06270 228 VHYPIEEMAQAAAELALNLAYGEPLPISHEFTPTLIERD 266
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
28-296 |
8.36e-27 |
|
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380499 [Multi-domain] Cd Length: 269 Bit Score: 105.80 E-value: 8.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLT---VRGTKLMLINPTDSDAVgnsiLMAN 104
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAekrVDGLLLMCSEMTDDDAE----LLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 105 KAKIPVITLDRAANKGEVVShVASDNRMGGKMAADFIAKKTGNDAKVIQleGISGTSAARERGEGFNAGAKEHKFNVLAS 184
Cdd:cd06275 77 LRSIPVVVLDREIAGDNADA-VLDDSFQGGYLATRHLIELGHRRIGCIT--GPLEHSVSRERLAGFRRALAEAGIEVPPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 185 --QPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG-R--DDVLVVGFDGTNdgIKAVQGGKLgATIA 259
Cdd:cd06275 154 wiVEGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGlRvpQDISIIGYDDIE--LARYFSPAL-TTIH 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 493711027 260 QRPDQIGIVGVQ-IADKVLKGEKVEATVPVELELVVKQ 296
Cdd:cd06275 231 QPKDELGELAVElLLDRIENKREEPQSIVLEPELIERE 268
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-243 |
3.82e-25 |
|
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: 101.15 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMAnkAK 107
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAA--RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVShVASDNRMGGKMAADFIAKKtGNdAKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLASQ-- 185
Cdd:cd06285 79 VPVVLVDRRIGDTALPS-VTVDNELGGRLATRHLLEL-GH-RRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERiv 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493711027 186 PADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTN 243
Cdd:cd06285 156 PGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLrvpEDLSVVGFDDIP 216
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
29-242 |
9.57e-25 |
|
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: 99.92 E-value: 9.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKE---LANVQDLTVRGtkLMLINPTDSDAvgnsILMANK 105
Cdd:cd06284 2 ILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREddlLDMLRSRRVDG--VILLSGRLDAE----LLSELS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIP-VITLDRAANKGevVSHVASDNRMGGKMAADFIAKkTGNdaKVIQLegISGTSA---ARERGEGFNAGAKEHK--F 179
Cdd:cd06284 76 KRYPiVQCCEYIPDSG--VPSVSIDNEAAAYDATEYLIS-LGH--RRIAH--INGPLDnvyARERLEGYRRALAEAGlpV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493711027 180 NVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGT 242
Cdd:cd06284 149 DEDLIIEGDFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLrvpEDVSVIGFDDI 214
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
30-295 |
1.35e-24 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380539 [Multi-domain] Cd Length: 294 Bit Score: 100.39 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 30 ALVISTLNNPFFVTMKDAAQKEADKLGYELI-VLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd06316 3 AIAMHTTGSDWSRLQVAGIKDTFEELGIEVVaVTDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAAN----KGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH--KFNVL 182
Cdd:cd06316 83 KLVFMDNVPDgleaGKDYVSVVSSDNRGNGQIAAELLAEAIGGKGKVGIIYHDADFYATNQRDKAFKDTLKEKypDIKIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 183 ASQPADfDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRDDVLVVGFD-GTNDGIKAVQGGKLGATIAQR 261
Cdd:cd06316 163 AEQGFA-DPNDAEEVASAMLTANPDIDGIYVSWDTPALGVISALRAAGRSDIKITTVDlGTEIALDMAKGGNVKGIGAQR 241
|
250 260 270
....*....|....*....|....*....|....
gi 493711027 262 PDQIGIVGVQIADKVLKGEKVEATVPVELELVVK 295
Cdd:cd06316 242 PYDQGVAEALAAALALLGKEVPPFIGVPPLAVTK 275
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
29-240 |
1.67e-24 |
|
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: 99.56 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINP---TDSDAVgnsiLMANK 105
Cdd:cd06289 2 VGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPaagTTAELL----RRLKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRAAnKGEVVSHVASDNRMGGKMAADFIAKKtGNDaKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLASQ 185
Cdd:cd06289 78 WGIPVVLALRDV-PGSDLDYVGIDNRLGAQLATEHLIAL-GHR-RIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 186 --PADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRD---DVLVVGFD 240
Cdd:cd06289 155 ivPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEpgrDIAVVGFD 214
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
43-291 |
2.73e-24 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 99.47 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 43 TMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKIPVITLDRAAnKGEV 122
Cdd:cd19993 16 TDEAAMKKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDRLI-ENPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 123 VSHVASDNRMGGKMAADFI--AKKTGNdakVIQLEGISGTSAA----RERGEGFNAGAKEHKFNVLASQPAD-FDRTKGL 195
Cdd:cd19993 95 AFYISFDNVEVGRMQARGVlkAKPEGN---YVFIKGSPTDPNAdflrAGQMEVLQPAIDSGKIKIVGEQYTDgWKPANAQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 196 NVMQNLLTAHP-AVQAVFAQNDEMALGALRALQTAG-RDDVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQIGIVGVQIA 273
Cdd:cd19993 172 KNMEQILTANNnKVDAVVASNDGTAGGAVAALAAQGlAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIA 251
|
250
....*....|....*...
gi 493711027 274 DKVLKGEKVEATVPVELE 291
Cdd:cd19993 252 VELAKGTKIEAIKGAALT 269
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-296 |
3.21e-24 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 98.88 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAvgnSILMANKAK 107
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDL---SHLARLRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 -IPVITLDRAAnKGEVVSHVASDNRMGGKMAADFIAKKTGNdaKVIQLEGISGTSAARERGEGFNAGAKEHKFN----VL 182
Cdd:cd06293 78 gTAVVLLDRPA-PGPAGCSVSVDDVQGGALAVDHLLELGHR--RIAFVSGPLRTRQVAERLAGARAAVAEAGLDpdevVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 183 ASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG-R--DDVLVVGFDGTNdgikavqggkLGA--- 256
Cdd:cd06293 155 ELSAPDANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGlRvpDDVSVVGYDDLP----------FAAaan 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 493711027 257 ----TIAQRPDQIGivgvQIADKVLKGEKVEATVPVEL-----ELVVKQ 296
Cdd:cd06293 225 ppltTVRQPSYELG----RAAADLLLDEIEGPGHPHEHvvfqpELVVRS 269
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
28-285 |
1.05e-23 |
|
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: 97.49 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIqlegISGtSAARERGEGFNAGAKE--------HKF 179
Cdd:cd01538 81 IKVIAYDRLILNADVDYYISFDNEKVGELQAQALLDAKPEGNYVL----IGG-SPTDNNAKLFRDGQMKvlqpaidsGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 180 NVLASQPAD-FDRTKGLNVMQNLLTAHPA-VQAVFAQNDEMALGALRALQTAGRDD-VLVVGFDGTNDGIKAVQGGKLGA 256
Cdd:cd01538 156 KVVGDQWVDdWLPANAQQIMENALTANGNnVDAVVASNDGTAGGAIAALKAQGLSGgVPVSGQDADLAAIKRILAGTQTM 235
|
250 260
....*....|....*....|....*....
gi 493711027 257 TIAQRPDQIGIVGVQIADKVLKGEKVEAT 285
Cdd:cd01538 236 TVYKDIRLLADAAAEVAVALMRGEKPPIN 264
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
28-243 |
1.15e-23 |
|
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: 97.32 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTD-SDAVGNSILmaNKA 106
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNiSDEAIIKLL--KEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLDRAANKGEVVShVASDNRMGGKMAADFIAKKtGNDaKVIQLEGISGTSAARERGEGFNAGAKEHKFNvlasqp 186
Cdd:cd19976 79 KIPVVVLDRYIEDNDSDS-VGVDDYRGGYEATKYLIEL-GHT-RIGCIVGPPSTYNEHERIEGYKNALQDHNLP------ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493711027 187 adFDRTKGLNVMQNLLTAHPAVQ---------AVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTN 243
Cdd:cd19976 150 --IDESWIYSGESSLEGGYKAAEellksknptAIFAGNDLIAMGVYRAALELGLkipEDLSVIGFDNII 216
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
29-288 |
6.02e-23 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 95.41 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLN---NPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILmANK 105
Cdd:cd01391 2 IGVVTSSLHqirEQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNL-AQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLD------RAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGisgTSAARERGEGFNAGAKEHKF 179
Cdd:cd01391 81 FDIPQLALDatsqdlSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEG---LNSGELRMAGFKELAKQEGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 180 NVLASQPADFDR-TKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG-RDDVLVVGFDGT--NDGIKAVQGGKLG 255
Cdd:cd01391 158 CIVASDKADWNAgEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGlVGDVSVIGSDGWadRDEVGYEVEANGL 237
|
250 260 270
....*....|....*....|....*....|...
gi 493711027 256 ATIAQRPDQIGIVGVQIADKVLKGEKVEATVPV 288
Cdd:cd01391 238 TTIKQQKMGFGITAIKAMADGSQNMHEEVWFDE 270
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
29-296 |
7.91e-23 |
|
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: 95.44 E-value: 7.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTD---SDAVGNSilmANK 105
Cdd:cd01540 2 IGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDqklGPAIAAK---AKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRA---ANKGEVVSHVASD-NRMG---GKMAADFIAKK---TGNDAKVIQLEgISGTSAARERGEGFNAGAK 175
Cdd:cd01540 79 AGIPVIAVDDQlvdADPMKIVPFVGIDaYKIGeavGEWLAKEMKKRgwdDVKEVGVLAIT-MDTLSVCVDRTDGAKDALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 176 EHKF---NVLASQPADFDRTKGLNVMQNLLTAHPAVQ--AVFAQNDEMALGALRALQTAG--RDDVLVVGFDGTN--DGI 246
Cdd:cd01540 158 AAGFpedQIFQAPYKGTDTEGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAGfdAEDIIGVGIGGYLaaDEE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 493711027 247 KAVQGGKLGATIAQRPDQIGIVGVQ-IADKVLKGEKVEATVPVELELVVKQ 296
Cdd:cd01540 238 FKKQPTGFKASLYISPDKHGYIAAEeLYNWITDGKPPPAETLTDGVIVTRD 288
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
28-285 |
1.69e-22 |
|
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: 94.62 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd19994 1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVSHVAS-DNRMGGKMAADFIAKKTG--NDAKVIQLEGISGtSAARERGEGFNAGAKEhkfnVLas 184
Cdd:cd19994 81 IPVIAYDRLIMNTDAVDYYVTfDNEKVGELQGQYLVDKLGlkDGKGPFNIELFAG-SPDDNNAQLFFKGAME----VL-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 185 QP---------------------ADFDRTKGLNVMQNLLTAHPA----VQAVFAQNDEMALGALRALQTAGRDD---VLV 236
Cdd:cd19994 154 QPyiddgtlvvrsgqttfeqvatPDWDTETAQARMETLLSAYYTggkkLDAVLSPNDGIARGVIEALKAAGYDTgpwPVV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 493711027 237 VGFDGTNDGIKAVQGGKLGATIAQRPDQIGIVGVQIADKVLKGEKVEAT 285
Cdd:cd19994 234 TGQDAEDASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVEVN 282
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
28-266 |
7.52e-22 |
|
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: 92.31 E-value: 7.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGnSILMANKAK 107
Cdd:cd01537 1 RIGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAG-VAEKARGQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKtgNDAKVIQLEGISGTSAARERGEGFNAGAKEHKFNV--LASQ 185
Cdd:cd01537 80 VPVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKH--GHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTeqLQLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 186 PADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRD---DVLVVGFDGTNDGIKAvqgGKLGATIAQRP 262
Cdd:cd01537 158 TGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRvpsDISVFGYDALPEALKS---GPLLTTILQDA 234
|
....
gi 493711027 263 DQIG 266
Cdd:cd01537 235 NNLG 238
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
28-240 |
1.04e-21 |
|
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: 91.96 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAvgNSILMANKAK 107
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENS--EGLQALIAQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQleGISGTSAARERGEGFNAGAKEHKFNV--LASQ 185
Cdd:cd06299 79 LPVVFVDREVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYIS--GPLSTSTGRERLAAFRAALTAAGIPIdeELVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493711027 186 PADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG---RDDVLVVGFD 240
Cdd:cd06299 157 FGDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGlriGDDVSLISFD 214
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-296 |
1.19e-20 |
|
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: 89.11 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTK-LMLINPTDSDAVgnsILMANKA 106
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDgLILVGSDHDPEL---FELLEQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLDrAANKGEVVSHVASDNRMGGKMAADFiakktgndakVIQLeG------ISGTSA----ARERGEGFNAGAKE 176
Cdd:cd06273 78 QVPYVLTW-SYDEDSPHPSIGFDNRAAAARAAQH----------LLDL-GhrriavISGPTAgndrARARLAGIRDALAE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 177 HKFNV----LASQPADFDRTKGLnvMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRD---DVLVVGFDGTNdgikav 249
Cdd:cd06273 146 RGLELpeerVVEAPYSIEEGREA--LRRLLARPPRPTAIICGNDVLALGALAECRRLGISvpeDLSITGFDDLE------ 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 493711027 250 qggkLGA-------TIAQRPDQIGIVGvqiADKV---LKGEKVEATVPVELELVVKQ 296
Cdd:cd06273 218 ----LAAhlsppltTVRVPAREIGELA---ARYLlalLEGGPPPKSVELETELIVRE 267
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
29-280 |
1.30e-20 |
|
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: 88.88 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDavGNSIL-MANKAK 107
Cdd:cd06282 2 IGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQ--GSEALeLLEEEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGEvVSHVASDNRMGGKMAADFIAKK--------TGNdakviqlegISGTSAARERGEGFNAGAKEHKF 179
Cdd:cd06282 80 VPYVLLFNQTENSS-HPFVSVDNRLASYDVAEYLIALghrriamvAGD---------FSASDRARLRYQGYRDALKEAGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 180 NVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGtndgikaVQGGKLG- 255
Cdd:cd06282 150 KPIPIVEVDFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIrvpDDVSVIGFDG-------IAIGELLt 222
|
250 260
....*....|....*....|....*...
gi 493711027 256 ---ATIAQRPDQIGIVGVQIADKVLKGE 280
Cdd:cd06282 223 ptlATVVQPSRDMGRAAADLLLAEIEGE 250
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
58-285 |
2.85e-20 |
|
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: 88.50 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 58 ELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKIPVITLDRAANKGEVVSHVASDNRMGGKMA 137
Cdd:cd19995 34 KVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPADYYVSFDNVAVGEAQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 138 ADFIAK----KTGNDAKVIQLEGISGTSAARERGEGFNAGAK----EHKFNVLASQPA-DFDRTKGLNVMQNLLTAHP-A 207
Cdd:cd19995 114 AQSLVDhlkaIGKKGVNIVMINGSPTDNNAGLFKKGAHEVLDplgdSGELKLVCEYDTpDWDPANAQTAMEQALTKLGnN 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493711027 208 VQAVFAQNDEMALGALRALQTAGRDDVLVV-GFDGTNDGIKAVQGGKLGATIAQRPDQIGIVGVQIADKVLKGEKVEAT 285
Cdd:cd19995 194 IDGVLSANDGLAGGAIAALKAQGLAGKVPVtGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGETPPSD 272
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
87-271 |
3.14e-20 |
|
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: 88.16 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 87 LINPTDSDAVGNSILMANKAKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAArER 166
Cdd:cd19969 61 AVSAIDPEALTPTINKAVDAGIPVVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQPNHE-ER 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 167 GEGFNAGAKEHK-FNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTND 244
Cdd:cd19969 140 VEGFKEAFAEYPgIEVVAVGDDNDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKtGKVKIVAFDDDPE 219
|
170 180
....*....|....*....|....*..
gi 493711027 245 GIKAVQGGKLGATIAQRPDQIGIVGVQ 271
Cdd:cd19969 220 TLDLIKDGVIDASIAQRPWMMGYWSLQ 246
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
29-240 |
3.33e-20 |
|
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: 87.59 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAvgNSILMANKAKI 108
Cdd:cd19977 2 IGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNE--DLIEKLVKSGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAANKGEvVSHVASDNRMGGKMAADFIAKKtGndAKVIQLEGIS-GTSAARERGEGFNAGAKEHKFNVLASQPA 187
Cdd:cd19977 80 PVVFVDRYIPGLD-VDTVVVDNFKGAYQATEHLIEL-G--HKRIAFITYPlELSTRQERLEGYKAALADHGLPVDEELIK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493711027 188 DFDRTKGLNV-MQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFD 240
Cdd:cd19977 156 HVDRQDDVRKaISELLKLEKPPDAIFAANNLITLEVLKAIKELGLripDDIALIGFD 212
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
28-287 |
3.36e-20 |
|
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: 87.95 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLInpTDSDAVGNSIL-MANKA 106
Cdd:pfam00532 3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIII--TTPAPSGDDITaKAEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIaKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLASQP 186
Cdd:pfam00532 81 GIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYL-IAEGHKRPIAVMAGPASALTARERVQGFMAALAAAGREVKIYHV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 187 A--DFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR----DDVL-----VVGFDG-TNDGIKAVQGGKL 254
Cdd:pfam00532 160 AtgDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRvkipDIVGiginsVVGFDGlSKAQDTGLYLSPL 239
|
250 260 270
....*....|....*....|....*....|...
gi 493711027 255 gaTIAQRPDQigIVGVQIADKVLKGEKVEATVP 287
Cdd:pfam00532 240 --TVIQLPRQ--LLGIKASDMVYQWIPKFREHP 268
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
29-283 |
4.09e-20 |
|
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: 87.61 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLT---VRGtkLMLINPTDSDAVGNsilMANK 105
Cdd:cd19975 2 IGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKekrVDG--IIFASGTLTEENKQ---LLKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLDRAANKGEVVShVASDNRMGGKMAADFIAKKtgnDAKVIQLegISG----TSAARERGEGFNAGAKEH--KF 179
Cdd:cd19975 77 MNIPVVLVSTESEDPDIPS-VKIDDYQAAYDATNYLIKK---GHRKIAM--ISGplddPNAGYPRYEGYKKALKDAglPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 180 NVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG---RDDVLVVGFDGTNdgIKAVQGGKLgA 256
Cdd:cd19975 151 KENLIVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGirvPEDISVIGFDNTE--IAEMSIPPL-T 227
|
250 260
....*....|....*....|....*..
gi 493711027 257 TIAQRPDQIGIVGVQIADKVLKGEKVE 283
Cdd:cd19975 228 TVSQPFYEMGKKAVELLLDLIKNEKKE 254
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
28-240 |
6.12e-20 |
|
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: 86.83 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLN-NPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLT---VRGtkLMLINPTDSDAVgnsiLMA 103
Cdd:cd06288 1 TIGLITDDIAtTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLsrrVDG--IIYASMHHREVT----LPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 104 NKAKIPVITLDRAANKGEVVSHVAsDNRMGGKMAADFIAKKtgNDAKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLA 183
Cdd:cd06288 75 ELTDIPLVLLNCFDDDPSLPSVVP-DDEQGGYLATRHLIEA--GHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493711027 184 S--QPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFD 240
Cdd:cd06288 152 SlvVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLrvpEDLSVVGFD 213
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
37-262 |
3.61e-19 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380535 [Multi-domain] Cd Length: 272 Bit Score: 84.98 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 37 NNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELA-NVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKIPVITL-- 113
Cdd:cd06312 11 SDPFWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQArLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAIns 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 114 --DRAANKGEVVSHVASDNRMGGKMAAD-FIAKKTGNDAKVIQLEGISGTSAareRGEGFNAGAKEHKFNVLASQPADfD 190
Cdd:cd06312 91 gdDRSKERLGALTYVGQDEYLAGQAAGErALEAGPKNALCVNHEPGNPGLEA---RCKGFADAFKGAGILVELLDVGG-D 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493711027 191 RTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRDD-VLVVGFDGTNDGIKAVQGGKLGATIAQRP 262
Cdd:cd06312 167 PTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGkVKIGTFDLSPETLEAIKDGKILFAIDQQP 239
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
29-285 |
1.15e-18 |
|
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: 83.82 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd19991 2 IGFSMDSLRVERWQRDRDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIqlegISGtSAARERGEGFNAGAKE--------HKFN 180
Cdd:cd19991 82 PVLAYDRLILNADVDLYVSFDNEKVGELQAEALVKAKPKGNYVL----LGG-SPTDNNAKLFREGQMKvlqplidsGDIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 181 VLASQ-PADFDRTKGLNVMQNLLTAHPA-VQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGAT 257
Cdd:cd19991 157 VVGDQwVDDWDPEEALKIMENALTANNNkIDAVIASNDGTAGGAIQALAEQGLaGKVAVSGQDADLAACQRIVEGTQTMT 236
|
250 260
....*....|....*....|....*...
gi 493711027 258 IAQRPDQIGIVGVQIADKVLKGEKVEAT 285
Cdd:cd19991 237 IYKPIKELAEKAAELAVALAKGEKNEAN 264
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-242 |
1.65e-18 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 83.06 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTK-LMLINPTDSDAVGNSILmaNKA 106
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDgLILTPGDEDDPELAAAL--ARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLDRAAnkGEVVSHVASDNRMGGKMAADF--------IAKKTGNdakviqlegiSGTSAARERGEGFNAGAKEHK 178
Cdd:cd06281 79 DIPVVLIDRDL--PGDIDSVLVDHRSGVRQATEYllslghrrIALLTGG----------PDIRPGRERIAGFKAAFAAAG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493711027 179 FNV--LASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGT 242
Cdd:cd06281 147 LPPdpDLVRLGSFSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLripGDLSVVSIGDS 215
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
29-280 |
1.74e-18 |
|
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: 83.45 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVL-DSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd06302 2 IAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKG--EVVSHVASDNRMGGKMAaDFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH--KFNVLA 183
Cdd:cd06302 82 IKVITWDSDAPPSarDYFVNQADDEGLGEALV-DSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKypDIELVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 184 SQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRP 262
Cdd:cd06302 161 TYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKtGKVAVTGIGLPNTARPYLKDGSVKEGVLWDP 240
|
250
....*....|....*...
gi 493711027 263 DQIGIVGVQIADKVLKGE 280
Cdd:cd06302 241 AKLGYLTVYAAYQLLKGK 258
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
28-240 |
1.80e-18 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 83.98 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSIlMANKAK 107
Cdd:PRK10423 58 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREI-MQRYPS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGevVSHVASDNRM-GGKMAADFIAKKtgNDAKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLASQP 186
Cdd:PRK10423 137 VPTVMMDWAPFDG--DSDLIQDNSLlGGDLATQYLIDK--GYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYE 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493711027 187 --ADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFD 240
Cdd:PRK10423 213 vtGDFEFNGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLsvpQDIAVIGYD 271
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
29-290 |
1.99e-18 |
|
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: 82.60 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAvgNSILMANKAKI 108
Cdd:cd06283 2 IGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNN--DAYLELAQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAANkGEVVSHVASDNRMGGKMAADFIAKKtGNDAKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLASQpad 188
Cdd:cd06283 80 PVVLVDRQIE-PLNWDTVVTDNYDATYEATEHLKEQ-GYERIVFVTEPIKGISTRRERLQGFLDALARYNIEGDVYV--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 189 FDRTKGLNVMQNLLTAHPAVQ----AVFAQNDEMALGALRALQTAG---RDDVLVVGFDGTN------DGIkavqggklg 255
Cdd:cd06283 155 IEIEDTEDLQQALAAFLSQHDggktAIFAANGVVLLRVLRALKALGiriPDDVGLCGFDDWDwadligPGI--------- 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 493711027 256 ATIAQRPDQIGIVGVQIADKVLKGEKVEA---TVPVEL 290
Cdd:cd06283 226 TTIRQPTYEIGKAAAEILLERIEGDSGEPkeiELPSEL 263
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
47-296 |
7.42e-18 |
|
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: 81.09 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 47 AAQKEADKLGYELIVLD-SQDNPAKELANVQDLT---VRGtkLMLINPTDSDAVGNSILMANkakIPVITLDraANKGEV 122
Cdd:cd01574 20 GIERAARERGYSVSIATvDEDDPASVREALDRLLsqrVDG--IIVIAPDEAVLEALRRLPPG---LPVVIVG--SGPSPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 123 VSHVASDNRMGGKMAADFIakktgndakvIQLeG------ISGTS---AARERGEGFNAGAKEHKFNVLASQPADFDRTK 193
Cdd:cd01574 93 VPTVSIDQEEGARLATRHL----------LEL-GhrriahIAGPLdwvDARARLRGWREALEEAGLPPPPVVEGDWSAAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 194 GLNVMQNLLtAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTNDGikAVQGGKLgATIAQRPDQIGIVGV 270
Cdd:cd01574 162 GYRAGRRLL-DDGPVTAVFAANDQMALGALRALHERGLrvpEDVSVVGFDDIPEA--AYFVPPL-TTVRQDFAELGRRAV 237
|
250 260
....*....|....*....|....*..
gi 493711027 271 QIADKVLKGEKVEAT-VPVELELVVKQ 296
Cdd:cd01574 238 ELLLALIEGPAPPPEsVLLPPELVVRE 264
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
29-288 |
1.77e-17 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380652 [Multi-domain] Cd Length: 305 Bit Score: 80.80 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEA-----DKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMA 103
Cdd:cd19997 2 IALSNSYAGNTWRQQMVDAFEEAAkkakaDGLIADYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 104 NKAKIPVITLDRAANKgEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEH-KFNVL 182
Cdd:cd19997 82 CDAGIKVVVFDSGVTE-PCAYILNNDFEDYGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKKYpDLKVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 183 ASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEmALGALRALQTAGRdDVLVVGFDGTNDGIK--AVQGGKLG-ATIA 259
Cdd:cd19997 161 AEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGD-GYGAAQAFEAAGR-PLPIIIGGNRGEFLKwwQEEYAKNGyETVS 238
|
250 260 270
....*....|....*....|....*....|..
gi 493711027 260 QRPDQ-IGIVGVQIADKVLKGEKV--EATVPV 288
Cdd:cd19997 239 VSTDPgQGSAAFWVALDILNGKDVpkEMILPV 270
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
29-242 |
5.02e-17 |
|
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380487 [Multi-domain] Cd Length: 270 Bit Score: 79.14 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIV--LDSQDNPAKE--LANVQDLTVRGtkLMLINPTDSDAVGNSILMAn 104
Cdd:cd01545 2 IGLLYDNPSASYVSALQVGALRACREAGYHLVVepCDSDDEDLADrlRRFLSRSRPDG--VILTPPLSDDPALLDALDE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 105 kAKIPVITLDRAANKGEVVShVASDNRMGGKMAAD-----------FIAkktgndakviqleGISGTSAARERGEGFNAG 173
Cdd:cd01545 79 -LGIPYVRIAPGTDDDRSPS-VRIDDRAAAREMTRhlialghrrigFIA-------------GPPDHGASAERLEGFRDA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493711027 174 AKEH--KFNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG---RDDVLVVGFDGT 242
Cdd:cd01545 144 LAEAglPLDPDLVVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGlrvPDDLSVAGFDDS 217
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
38-290 |
7.07e-17 |
|
ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which 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: 380517 [Multi-domain] Cd Length: 269 Bit Score: 78.39 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 38 NPFFVTMKDAAQKEADKLGYeLIVLDSQDNPAKELANVQDLtVRGTK---LMLINPTDSDAVgnsILMANKAKIPVITLD 114
Cdd:cd06294 16 NPFFSEVLRGISQVANENGY-SLLLATGNTEEELLEEVKRM-VRGRRvdgFILLYSKEDDPL---IEYLKEEGFPFVVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 115 RAANKGEVvSHVASDNRMGGKMAADFIAKKtgNDAKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLASQ--PADFDRT 192
Cdd:cd06294 91 KPLDDNDV-LYVDNDNVQAGYEATEYLIDK--GHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDDYilLLDFSEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 193 KGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFdgtNDGIKAVQGGKLGATIAQRPDQIGIVG 269
Cdd:cd06294 168 DGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLrvpEDVSIISF---NNSPLAELASPPLTSVDINPYELGREA 244
|
250 260
....*....|....*....|....
gi 493711027 270 VQIADKVLKGEKVEAT---VPVEL 290
Cdd:cd06294 245 AKLLINLLEGPESLPKnviVPHEL 268
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
28-296 |
7.49e-17 |
|
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators; This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380518 [Multi-domain] Cd Length: 273 Bit Score: 78.45 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVI-------STLNNPFFVTMKDAAQKEADKLGYELIV--LDSQDNPAKELANVQdltvRGTKLMLINPTDSDAVGN 98
Cdd:cd06295 5 TIAVVVpmdphgdQSITDPFFLELLGGISEALTDRGYDMLLstQDEDANQLARLLDSG----RADGLIVLGQGLDHDALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 99 SILMANkakIPVITLDRAANKGEVVShVASDNRMGGKMAAD-FIAkkTGndAKVIQLEGISGTSAARERGEGFNAGAKEH 177
Cdd:cd06295 81 ELAQQG---LPMVVWGAPEDGQSYCS-VGSDNVKGGALATEhLIE--IG--RRRIAFLGDPPHPEVADRLQGYRDALAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 178 KFNVLASQ--PADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDG------TNDGI 246
Cdd:cd06295 153 GLEADPSLllSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGIsvpGDVAVVGYDDiplaayFRPPL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 493711027 247 KAV-QGGKLGatiaqrpdqigivGVQIADKVLK---GEKVEaTVPVELELVVKQ 296
Cdd:cd06295 233 TTVrQDLALA-------------GRLLVEKLLAliaGEPVT-SSMLPVELVVRE 272
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
29-284 |
9.29e-17 |
|
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: 78.47 E-value: 9.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLD-SQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd20003 2 IAMIPKLVGVPYFTAAGQGAQEAAKELGVDVTYDGpTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKG--EVVSHVASDNRMGgKMAADFIAKKTGNDAKV----------IQLEGISgtsAARERGEgfnagAK 175
Cdd:cd20003 82 IKVVTWDSDVNPDarDFFVNQATPEGIG-KTLVDMVAEQTGEKGKVaivtssptatNQNAWIK---AMKAYIA-----EK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 176 EHKFNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQnDEMAL-GALRALQTAGRD-DVLVVGFDGTNDGIKAVQGGK 253
Cdd:cd20003 153 YPDMKIVTTQYGQEDPAKSLQVAENILKAYPDLKAIIAP-DSVALpGAAEAVEQLGRTgKVAVTGLSTPNVMRPYVKDGT 231
|
250 260 270
....*....|....*....|....*....|.
gi 493711027 254 LGATIAQRPDQIGIVGVQIADKVLKGEKVEA 284
Cdd:cd20003 232 VKSVVLWDVVDLGYLAVYVARALADGTLLKV 262
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
29-294 |
1.17e-16 |
|
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: 77.92 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDL---TVRGtkLMLINPTDSDAVGNsilMANK 105
Cdd:cd01575 2 VAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALlsrRPAG--LILTGTEHTPATRK---LLRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVI-TLDRAANKGEVVshVASDNRMGGKMAADFIAKK--------TGNDakviqlegiSGTSAARERGEGFNAGAKE 176
Cdd:cd01575 77 AGIPVVeTWDLPDDPIDMA--VGFSNFAAGRAMARHLIERgyrriafvGARL---------DGDSRARQRLEGFRDALAE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 177 HKFN----VLASQPADFDRtkGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTNdgIKAV 249
Cdd:cd01575 146 AGLPlplvLLVELPSSFAL--GREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIrvpGDIAIAGFGDLD--IAAA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 493711027 250 QGGKLgATIAQRPDQIgivGVQIADKVL---KGEKVEAT-VPVELELVV 294
Cdd:cd01575 222 LPPAL-TTVRVPRYEI---GRKAAELLLarlEGEEPEPRvVDLGFELVR 266
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
29-293 |
1.18e-16 |
|
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: 77.54 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLT---VRGTKLMLINPTDSDavgnsILMANK 105
Cdd:cd01542 2 IGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLArqkVDGIILFATEITDEH-----RKALKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 AKIPVITLdraANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIqleGISGT--SAARERGEGFNAGAKEHKFNVLA 183
Cdd:cd01542 77 LKIPVVVL---GQEHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYI---GVDEEdiAVGVARKQGYLDALKEHGIDEVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 184 SQPADFDRTKGLNVMQNLLTAHPAvQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTndgikavqggKLGA---- 256
Cdd:cd01542 151 IVETDFSMESGYEAAKELLKENKP-DAIICATDNIALGAIKALRELGIkipEDISVAGFGGY----------DLSEfvsp 219
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 493711027 257 ---TIAQRPDQIGIVGVQIADKVLKGEKVEATVPVELELV 293
Cdd:cd01542 220 sltTVKFDYEEAGEKAAELLLDMIEGEKVPKKQKLPYELI 259
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
29-293 |
1.18e-16 |
|
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: 78.48 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTM----KDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMAN 104
Cdd:cd19998 2 IALSNSYSGNDWRQEMiniaKAAAKQPPYADKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 105 KAKIPVITLDRAANkGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNA-GAKEHKFNVLA 183
Cdd:cd19998 82 DAGIVVVAFDNVVD-EPCAYNVNTDQAKAGEQTAQWLVDKLGGKGNILMVRGVPGTSVDRDRYEGAKEvFKKYPDIKVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 184 SQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMalGALRALQTAGRdDVLVVGFDGTNDGIKAVQ---GGKLGATIAQ 260
Cdd:cd19998 161 EYYGNWDDGTAQKAVADALAAHPDVDGVWTQGGET--GVIKALQAAGH-PLVPVGGEAENGFRKAMLeplANGLPGISAG 237
|
250 260 270
....*....|....*....|....*....|...
gi 493711027 261 RPDQIGIVGVQIADKVLKGEKVEATVPVELELV 293
Cdd:cd19998 238 SPPALSAVALKLAVAVLEGEKEPKTIELPLPWV 270
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
29-296 |
3.78e-16 |
|
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380515 [Multi-domain] Cd Length: 273 Bit Score: 76.54 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLN----NPFFVTMKDAAQKEADKLGYeLIVLDSQDNPAKELANVQDLT----VRGTKLMLINPTDSDAvgnSI 100
Cdd:cd06292 2 IGYVVPELPggfsDPFFDEFLAALGHAAAARGY-DVLLFTASGDEDEIDYYRDLVrsrrVDGFVLASTRHDDPRV---RY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 101 LMAnkAKIPVITLDRAANKGEVvSHVASDNRMGGKMAADFIAKKtgNDAKVIQLEGISGTSAARERGEGFNAGAKEHKfn 180
Cdd:cd06292 78 LHE--AGVPFVAFGRANPDLDF-PWVDVDGAAGMRQAVRHLIAL--GHRRIGLIGGPEGSVPSDDRLAGYRAALEEAG-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 181 vLASQPA-----DFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTNdgikavqgg 252
Cdd:cd06292 151 -LPFDPGlvvegENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLrvgRDVSVVGFDDSP--------- 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 493711027 253 kLGA-------TIAQRPDQIGIVGVQIADKVLKGEKVE-ATVPVELELVVKQ 296
Cdd:cd06292 221 -LAAfthppltTVRQPIDEIGRAVVDLLLAAIEGNPSEpREILLQPELVVRE 271
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
125-296 |
6.44e-16 |
|
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: 76.64 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 125 HVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTsAARERGEGFNAGAKEH-KFNVLASQPADFDRTKGLNVMQNLLT 203
Cdd:cd06303 136 YVGFDHAEGSRMLAKHFIKIFPEEGKYAILYLTEGY-VSDQRGDTFIDEVARHsNLELVSAYYTDFDRESAREAARALLA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 204 AHPAVQAVFAQNDEMALGALRALQTAGRD-DVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQIGIVgvqIADKV---LKG 279
Cdd:cd06303 215 RHPDLDFIYACSTDIALGAIDALQELGREtDIMINGWGGGSAELDALQKGGLDVTVMRMNDDNGIA---MAEAIkldLEG 291
|
170
....*....|....*..
gi 493711027 280 EKVEATVPVELELVVKQ 296
Cdd:cd06303 292 REVPTVYAGDFELVTKG 308
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
39-262 |
2.24e-15 |
|
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: 74.28 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 39 PFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVR---GTKLMLINPTDSDAvgNSILMANKAKIPVITLDR 115
Cdd:cd19966 13 PFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAkpdGIAIMGHPGDGAYT--PLIEAAKKAGIIVTSFNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 116 AANKGEVVS----HVASDNRMGGKMAADFIAKKTG--NDAKVIQLEGISGTSAARERGEGFNAGAKEH--KFNVLASQPA 187
Cdd:cd19966 91 DLPKLEYGDcglgYVGADLYAAGYTLAKELVKRGGlkTGDRVFVPGLLPGQPYRVLRTKGVIDALKEAgiKVDYLEISLE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493711027 188 DFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR--DDVLVVGFDGTNDGIKAVQGGKLGATIAQRP 262
Cdd:cd19966 171 PNKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKkpGEIPVAGFDLSPATVQAIKSGYVNATIDQQP 247
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
29-262 |
2.73e-15 |
|
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: 74.23 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQD-NPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd19965 2 FVFVTHVTTNPFFQPVKKGMDDACELLGAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITLDRAANKGE--VVSHVASDNRMGGKMAADFIAKKTGND-AKVIQLEGISGTSAARERGEGFNAGAKEHK----FN 180
Cdd:cd19965 82 IPVVAFNVDAPGGEnaRLAFVGQDLYPAGYVLGKRIAEKFKPGgGHVLLGISTPGQSALEQRLDGIKQALKEYGrgitYD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 181 VLASQPadfDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRDD-VLVVGFDGTNDGIKAVQGGKLGATIA 259
Cdd:cd19965 162 VIDTGT---DLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGkVLVGGFDLVPEVLQGIKAGYIDFTID 238
|
...
gi 493711027 260 QRP 262
Cdd:cd19965 239 QQP 241
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
29-294 |
5.54e-15 |
|
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation; This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380519 [Multi-domain] Cd Length: 270 Bit Score: 73.08 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMAnkAKI 108
Cdd:cd06296 2 IDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRS--AGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLD-RAANKGEVVShVASDNRMGGKMAADFIAKKTGNDAKVIQleGISGTSAARERGEGFNAGAKEH-----KFNVL 182
Cdd:cd06296 80 PFVLIDpVGEPDPDLPS-VGATNWAGGRLATEHLLDLGHRRIAVIT--GPPRSVSGRARLAGYRAALAEAgiavdPDLVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 183 ASqpaDFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTndgikaVQGGKLG---A 256
Cdd:cd06296 157 EG---DFTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLrvpDDLSVIGFDDT------PPARWTSpplT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 493711027 257 TIAQRPDQIGIVGVQIADKVLKGEKVEAtVPVEL--ELVV 294
Cdd:cd06296 228 TVHQPLREMGAVAVRLLLRLLEGGPPDA-RRIELatELVV 266
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
29-295 |
1.50e-14 |
|
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: 72.21 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLD----SQDNPAKELANVQDLTvRGTKLMLINPTDSDAVGNSILMAN 104
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRihfvDSLDPEALAAALRRLA-AGCDGVALVAPDHPLVRAAIDELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 105 KAKIPVITL-------DRAAnkgevvsHVASDNRMGGKMAADFIAKKTGND-AKVIQLEGISGTSAARERGEGFNAGAKE 176
Cdd:cd06307 81 ARGIPVVTLvsdlpgsRRLA-------YVGIDNRAAGRTAAWLMGRFLGRRpGKVLVILGSHRFRGHEEREAGFRSVLRE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 177 H--KFNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVF---AQNDemalGALRALQTAGRD-DVLVVGFDGTNDGIKAVQ 250
Cdd:cd06307 154 RfpDLTVLEVLEGLDDDELAYELLRELLARHPDLVGIYnagGGNE----GIARALREAGRArRVVFIGHELTPETRRLLR 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 493711027 251 GGKLGATIAQRPDQIGIVGVQ-IADKVLKGEKVEATVPVELELVVK 295
Cdd:cd06307 230 DGTIDAVIDQDPELQARRAIEvLLAHLGGKGPAPPQPPIPIEIITR 275
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
28-241 |
3.52e-14 |
|
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380665 [Multi-domain] Cd Length: 269 Bit Score: 71.04 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVIST----LNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAkELANVQDLtVRGTK---LMLINPTDSDAvgnSI 100
Cdd:cd20010 1 AIGLVLPLdpgdLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGED-ELATYRRL-VERGRvdgFILARTRVNDP---RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 101 LMANKAKIPVITLDRAANKGEVvSHVASDNRMGGKMAADF--------IAKKTGNDakviqlegisGTSAARERGEGFNA 172
Cdd:cd20010 76 AYLLERGIPFVVHGRSESGAPY-AWVDIDNEGAFRRATRRllalghrrIALLNGPE----------ELNFAHQRRDGYRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493711027 173 GAKEHKFNVLAS--QPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDG 241
Cdd:cd20010 145 ALAEAGLPVDPAlvREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLspgKDVSVIGHDD 218
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
44-286 |
3.71e-14 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 71.52 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 44 MKDA--------AQKEADKLGYELIVLD--SQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKaKIPVITL 113
Cdd:PRK10936 56 LKDSywlsvnygMVEEAKRLGVDLKVLEagGYYNLAKQQQQLEQCVAWGADAILLGAVTPDGLNPDLELQAA-NIPVIAL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 114 DRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQL------EGISGTSAARErgeGFNAGAKEHKFNVLASQPA 187
Cdd:PRK10936 135 VNGIDSPQVTTRVGVSWYQMGYQAGRYLAQWHPKGSKPLNVallpgpEGAGGSKAVEQ---GFRAAIAGSDVRIVDIAYG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 188 DFDRTKGLNVMQNLLTAHPAVQ-----AVFAqndEMALGALRALQTagRDDVLVVGFDGTNDGIKAVQGGKLGATIAQRP 262
Cdd:PRK10936 212 DNDKELQRNLLQELLERHPDIDyiagsAVAA---EAAIGELRGRNL--TDKIKLVSFYLSHQVYRGLKRGKVLAAPSDQM 286
|
250 260
....*....|....*....|....
gi 493711027 263 DQIGIVGVQIADKVLKGEKVEATV 286
Cdd:PRK10936 287 VLQGRLAIDQAVRQLEGAPVPGDV 310
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
28-240 |
6.26e-14 |
|
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: 70.31 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLI----NPTDSDAVGnsilma 103
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVapstPPDDIYYLC------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 104 NKAKIPVITLDRAANKGEVVShVASDNRMGgkmAADFIAKKTGNDAK-VIQLEGISGTSAARERGEGFNAGAKEHKF--- 179
Cdd:cd06274 75 QAAGLPVVFLDRPFSGSDAPS-VVSDNRAG---ARALTEKLLAAGPGeIYFLGGRPELPSTAERIRGFRAALAEAGIteg 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493711027 180 --NVLASqpaDFDRTKGLNVMQNLLTAH-PAVQAVFAQ---NDEMALGALRALQTAGRDDVLVVGFD 240
Cdd:cd06274 151 ddWILAE---GYDRESGYQLMAELLARLgGLPQALFTSsltLLEGVLRFLRERLGAIPSDLVLGTFD 214
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
29-295 |
9.78e-14 |
|
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: 69.50 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTvrgTKLM--LI-----NPTDsdavgnsIL 101
Cdd:cd06286 2 IGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLK---TKQIdgLIitsreNDWE-------VI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 102 MANKAKIPVITLDRAANKGevVSHVASDNRMGGKMAADFIAKK--------TGNDAkviqlegiSGTSAARERGEGFNAG 173
Cdd:cd06286 72 EPYAKYGPIVLCEETDSPD--IPSVYIDRYEAYLEALEYLKEKghrkigycLGRPE--------SSSASTQARLKAYQDV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 174 AKEHKfnvLASQPAD-----FDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDgtNDG 245
Cdd:cd06286 142 LGEHG---LSLREEWiftncHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIrvpEDLAVIGFD--NQP 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 493711027 246 IkavqGGKLG-ATIAQRPDQIGIVGVQIADKVLKGEKVEaTVPVELELVVK 295
Cdd:cd06286 217 I----SELLNlTTIDQPLEEMGKEAFELLLSQLESKEPT-KKELPSKLIER 262
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
28-240 |
3.06e-13 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 68.98 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLT---VRGTKLMLINPTDsdavgNSI-LMA 103
Cdd:PRK10703 61 SIGLLATSSEAPYFAEIIEAVEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAqkrVDGLLVMCSEYPE-----PLLaMLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 104 NKAKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIqlEGISGTSAARERGEGFNAGAKEHKFNVLA 183
Cdd:PRK10703 136 EYRHIPMVVMDWGEAKADFTDAIIDNAFEGGYLAGRYLIERGHRDIGVI--PGPLERNTGAGRLAGFMKAMEEANIKVPE 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493711027 184 S--QPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG---RDDVLVVGFD 240
Cdd:PRK10703 214 EwiVQGDFEPESGYEAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGlrvPQDISVIGYD 275
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
109-241 |
3.06e-12 |
|
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380520 [Multi-domain] Cd Length: 268 Bit Score: 65.18 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDrAANKGevVSHVASDNRMGGKMAADFIAKKTGND--AKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLASQP 186
Cdd:cd06297 80 PVVLID-ANSMG--YDCVYVDNVKGGFMATEYLAGLGEREyvFFGIEEDTVFTETVFREREQGFLEALNKAGRPISSSRM 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 187 --ADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDG 241
Cdd:cd06297 157 frIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLrvgEDVAVIGFDG 216
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
37-240 |
4.87e-12 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 64.95 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 37 NNPFFVTMKDAAQKEADKLGYELI--VLDSQDNPAKELANVQDLTVRGtklMLINPTDSDAVgnSILMANKAKIPVITLD 114
Cdd:cd06277 17 ETPFFSELIDGIEREARKYGYNLLisSVDIGDDFDEILKELTDDQSSG---IILLGTELEEK--QIKLFQDVSIPVVVVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 115 RAAnkgEVVS--HVASDNRMGGKMAADFIAKKtgNDAKVIQLEGISGTSAARERGEGFNAGAKEHKfnvLASQPAD---- 188
Cdd:cd06277 92 NYF---EDLNfdCVVIDNEDGAYEAVKYLVEL--GHTRIGYLASSYRIKNFEERRRGFRKAMRELG---LSEDPEPefvv 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493711027 189 --------FDRTKGLNVMQNLLTAhpavqaVFAQNDEMALGALRALQTAGR---DDVLVVGFD 240
Cdd:cd06277 164 svgpegayKDMKALLDTGPKLPTA------FFAENDIIALGCIKALQEAGIrvpEDVSVIGFD 220
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
1-284 |
7.98e-12 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 64.76 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 1 MKLNKLatLFTAFALTATVSVNAMAKE-SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLT 79
Cdd:PRK10355 1 MKIKNI--LLTLCASLLLTSVAAHAKEvKIGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQMSQIENMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 80 VRGTKLMLINPTDSDAVGNSILMANKAKIPVITLDRAANKGEVVSHVASDNRMGGKMAADFIAKK--TGNdakviqlEGI 157
Cdd:PRK10355 79 NRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDFYISFDNEKVGELQAKALVDKvpQGN-------YFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 158 SGTSAARERGEGFNAGA--------KEHKFNVLASQPAD-FDRTKGLNVMQNLLTAHP-AVQAVFAQNDEMALGALRALQ 227
Cdd:PRK10355 152 MGGSPVDNNAKLFRAGQmkvlkpyiDSGKIKVVGDQWVDgWLPENALKIMENALTANNnKIDAVVASNDATAGGAIQALS 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 493711027 228 TAG-RDDVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQIGIVGVQIADKVLKGEKVEA 284
Cdd:PRK10355 232 AQGlSGKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKA 289
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
76-242 |
1.04e-11 |
|
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380502 [Multi-domain] Cd Length: 284 Bit Score: 64.15 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 76 QDLTVRGTKLMLINPTDSDAVGNSILMAN--------------------KAKIPVITLDRAANKGevVSHVASDNRMGGK 135
Cdd:cd06279 28 EVCEEEGLGLLLLPATDEGSAAAAVRNAAvdgfivyglsdddpavaalrRRGLPLVVVDGPAPPG--IPSVGIDDRAAAR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 136 MAADF-----------IAKKTGNDAKVIQLEGI----SGTSAARERGEGFNAGAKEHKFNVLASQP---ADFDRTKGLNV 197
Cdd:cd06279 106 AAARHlldlghrriaiLSLRLDRGRERGPVSAErlaaATNSVARERLAGYRDALEEAGLDLDDVPVveaPGNTEEAGRAA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493711027 198 MQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGT 242
Cdd:cd06279 186 ARALLALDPRPTAILCMSDVLALGALRAARERGLrvpEDLSVTGFDDI 233
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
29-240 |
2.60e-11 |
|
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: 62.58 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKE---LANVQDLTVRGtklMLINPTDSdAVGNS------ 99
Cdd:cd01541 2 IGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEreiLESLLDQNVDG---LIIEPTKS-ALPNPnldlye 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 100 ILMANKakIPVITLDRAANKGEVvSHVASDNRMGGKMAADFIA----KKTGNDAKVIQLEGIsgtsaarERGEGFNAGAK 175
Cdd:cd01541 78 ELQKKG--IPVVFINSYYPELDA-PSVSLDDEKGGYLATKHLIdlghRRIAGIFKSDDLQGV-------ERYQGFIKALR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493711027 176 EHKF-----NVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFD 240
Cdd:cd01541 148 EAGLpidddRILWYSTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLrvpEDLSVVGFD 220
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
28-242 |
1.90e-10 |
|
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: 60.23 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVIST-----LNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANvqdlTVRGtkLMLINPTDSDAVgNSILM 102
Cdd:cd01544 1 TIGIIQWYseeeeLEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLESLLE----KVDG--IIAIGKFSKEEI-EKLKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 103 ANKakiPVITLDRAANkGEVVSHVASDNRMGGKMAADFIAKK--------TGNDAkviqlEGISGTSAARERGEGFNAGA 174
Cdd:cd01544 74 LNP---NIVFVDSNPD-PDGFDSVVPDFEQAVRQALDYLIELghrrigfiGGKEY-----TSDDGEEIEDPRLRAFREYM 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493711027 175 KEH----KFNVLAsqpADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG---RDDVLVVGFDGT 242
Cdd:cd01544 145 KEKglynEEYIYI---GEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGikvPEDISIISFNDI 216
|
|
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
8-279 |
2.04e-10 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 60.51 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 8 TLFTAFALTATVSVNAMAKES---IALVISTLNNPFFVTMKDAAQKEADKL-GYELIVLDSQDNPAKELANVQDLTVRGT 83
Cdd:PRK15395 3 KVLTLSALMASMLFGAAAAAAdtrIGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 84 KLMLINPTDSDAVGNSILMANKAKIPVITLDRAANKGEVVSH-----VASDNRMGGKMAADFIAKKTG-------NDAKV 151
Cdd:PRK15395 83 KALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYdkayyVGTDSKESGIIQGDLIAKHWKanpawdlNKDGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 152 IQ---LEGISGTSAARERG----EGFNAgaKEHKFNVLASQPADFDRTKGLNVMQNLLTAHPA--VQAVFAQNDEMALGA 222
Cdd:PRK15395 163 IQyvlLKGEPGHPDAEARTtyviKELND--KGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNAnkIEVVIANNDAMAMGA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 493711027 223 LRALQTAGRDDVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQIGIVGVQIADKVLKG 279
Cdd:PRK15395 241 VEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADG 297
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
155-296 |
3.94e-10 |
|
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 57.35 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 155 EGISGTSAARERGEGFNAGAKEHKFNVLASQ--PADFDRTKGLNVMQNLLTAHPavQAVFAQNDEMALGALRALQTAGR- 231
Cdd:pfam13377 16 EGDRDDPYSDLRERGFREAARELGLDVEPTLyaGDDEAEAAAARERLRWLGALP--TAVFVANDEVALGVLQALREAGLr 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493711027 232 --DDVLVVGFDGTndgikavqggKLGA-------TIAQRPDQIGIVGVQIADKVLKGEK-VEATVPVELELVVKQ 296
Cdd:pfam13377 94 vpEDLSVIGFDDS----------PLAAlvsppltTVRVDAEELGRAAAELLLDLLNGEPaPPERVLLPPELVERE 158
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
47-296 |
7.75e-10 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 58.85 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 47 AAQKEADKLGYELIV--LDSQDNPAKELAnVQDLTVRGTKLMLIN-PTDSDAVgnSILMANKAKIPVITLDRAANKgeVV 123
Cdd:PRK09526 84 AIKSRADQLGYSVVIsmVERSGVEACQAA-VNELLAQRVSGVIINvPLEDADA--EKIVADCADVPCLFLDVSPQS--PV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 124 SHVASDNRMGGKMAADFIAkkTGNDAKVIQLEGISGTSAARERGEGFNAGAKEHKFNVLASQPADFDRTKGLNVMQNLLT 203
Cdd:PRK09526 159 NSVSFDPEDGTRLGVEHLV--ELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQPIAVREGDWSAMSGYQQTLQMLR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 204 AHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTNDG---IKAVqggklgATIAQRPDQIGIVGVQIADKVL 277
Cdd:PRK09526 237 EGPVPSAILVANDQMALGVLRALHESGLrvpGQISVIGYDDTEDSsyfIPPL------TTIKQDFRLLGKEAVDRLLALS 310
|
250
....*....|....*....
gi 493711027 278 KGEKVEATVPVELELVVKQ 296
Cdd:PRK09526 311 QGQAVKGSQLLPTSLVVRK 329
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
29-286 |
1.29e-09 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380656 Cd Length: 296 Bit Score: 58.06 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLD-SQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAK 107
Cdd:cd20001 2 IAVVVKVTGIAWFDRMETGVEQFAKDTGVNVYQIGpATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 108 IPVITlDRAANKGEVVSHV-ASDNRMGGKMAADFIAKKTGNDAKVIQLEGiSGTSAARErgEGFNAGAKEHKFN------ 180
Cdd:cd20001 82 IVVIT-HEASNLKNVDYDVeAFDNAAYGAFIMDKLAEAMGGKGKYVTFVG-SLTSTSHM--EWANAAVAYQKANypdmll 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 181 VLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIA 259
Cdd:cd20001 158 VTDRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLqGKIAVVGTGLPSVAGEYLEDGTIDYIQF 237
|
250 260
....*....|....*....|....*..
gi 493711027 260 QRPDQIGIVGVQIADKVLKGEKVEATV 286
Cdd:cd20001 238 WDPADAGYAMNALAVMVLEGEKITDGT 264
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
28-213 |
8.17e-09 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 55.65 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLIN---PTDSDAVGNsilMAN 104
Cdd:PRK11303 63 SIGLIIPDLENTSYARIAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVStslPPEHPFYQR---LQN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 105 KAkIPVITLDRAANKGEVVShVASDNRMGGKM-AADFIAKktgnDAKVIQLEG-ISGTSAARERGEGFNAGAKEHKFNVL 182
Cdd:PRK11303 140 DG-LPIIALDRALDREHFTS-VVSDDQDDAEMlAESLLKF----PAESILLLGaLPELSVSFEREQGFRQALKDDPREVH 213
|
170 180 190
....*....|....*....|....*....|.
gi 493711027 183 ASQPADFDRTKGLNVMQNLLTAHPAVQAVFA 213
Cdd:PRK11303 214 YLYANSFEREAGAQLFEKWLETHPMPDALFT 244
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
103-244 |
3.97e-08 |
|
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); Ligand-binding domain of DNA transcription repressor specific for xylose (XylR), a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of XylR 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: 380485 [Multi-domain] Cd Length: 265 Bit Score: 53.36 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 103 ANKAKIPVITLDrAANKGEVVSHVASDNRMGGKMAAD-FIAKKTGNDAKViqleGISGTSAARERGEGFNAGAKEHKFNV 181
Cdd:cd01543 67 LRRLGIPVVNVS-GSRPEPGFPRVTTDNEAIGRMAAEhLLERGFRHFAFC----GFRNAAWSRERGEGFREALREAGYEC 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493711027 182 LASQPADFDRTKGLNVMQNLLTA------HPAvqAVFAQNDEMALGALRALQTAGR---DDVLVVGFDgtND 244
Cdd:cd01543 142 HVYESPPSGSSRSWEEEREELADwlkslpKPV--GIFACNDDRARQVLEACREAGIrvpEEVAVLGVD--ND 209
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
39-283 |
4.59e-07 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380657 Cd Length: 295 Bit Score: 50.39 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 39 PFFVTMKDAAQKEADKLGYELIVLDSQD-NPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKIPVITLDRAA 117
Cdd:cd20002 12 PWFNRMEQGVKKAGKEFGVNAYQVGPADaDPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVITHESPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 118 NKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEGISGTSAARERGEGFNAGAKEHKFN---VLASQPADFDRTKG 194
Cdd:cd20002 92 QKGADWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKYPNmkqVTDRIPGGEDVDVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 195 LNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR-DDVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQIGIVGVQIA 273
Cdd:cd20002 172 RQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGLkGKVAVVGTVIPSQAAAYLKEGSITEGYLWDPADAGYAMVYIA 251
|
250
....*....|
gi 493711027 274 DKVLKGEKVE 283
Cdd:cd20002 252 KMLLDGKRKE 261
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
58-239 |
6.15e-07 |
|
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];
Pssm-ID: 440447 [Multi-domain] Cd Length: 314 Bit Score: 49.93 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 58 ELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKIPVITLD------RAANKGEVVSHVASDNR 131
Cdd:COG0683 46 ELVVEDDASDPDTAVAAARKLIDQDKVDAIVGPLSSGVALAVAPVAEEAGVPLISPSatapalTGPECSPYVFRTAPSDA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 132 MGGKMAADFIAKKTGNDaKVIQLegISGTSAARERGEGFNAGAKEHKFNVLASQPADFDRTKGLNVMQNLLTAHPavQAV 211
Cdd:COG0683 126 QQAEALADYLAKKLGAK-KVALL--YDDYAYGQGLAAAFKAALKAAGGEVVGEEYYPPGTTDFSAQLTKIKAAGP--DAV 200
|
170 180
....*....|....*....|....*....
gi 493711027 212 FAQN-DEMALGALRALQTAGRDDVLVVGF 239
Cdd:COG0683 201 FLAGyGGDAALFIKQAREAGLKGPLNKAF 229
|
|
| PRK15408 |
PRK15408 |
autoinducer 2 ABC transporter substrate-binding protein LsrB; |
5-281 |
1.44e-06 |
|
autoinducer 2 ABC transporter substrate-binding protein LsrB;
Pssm-ID: 237961 Cd Length: 336 Bit Score: 49.02 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 5 KLATLFTAFALtATVSVNAMAKESIALVISTLNNPFFVTMKDAAQKEADKLGYELivldSQDNPAK-----ELANVQDLT 79
Cdd:PRK15408 3 KKIALVSALGI-ALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVDV----TYDGPTEpsvsgQVQLINNFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 80 VRGTKLMLINPTDSDAVGNSILMANKAKIPVITLDRAANKgEVVSHVASD---NRMGG---KMAADFIAKKTGNDAKVIQ 153
Cdd:PRK15408 78 NQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKP-ECRSYYINQgtpEQLGSmlvEMAAKQVGKDKAKVAFFYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 154 LEGISGTSAARErgEGFNAGAKEH-KFNVLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRD 232
Cdd:PRK15408 157 SPTVTDQNQWVK--EAKAKIAKEHpGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRD 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 493711027 233 DVLVVGFDGTNDGIKAVQGGKLGATIAQRPDQIGIVGVQIADKVLKGEK 281
Cdd:PRK15408 235 KVAIVGFSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLKKGK 283
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
29-231 |
4.93e-06 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 47.40 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNsILMANKAKI 108
Cdd:PRK10014 67 IGLIVRDLSAPFYAELTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDL-REMAEEKGI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 109 PVITLDRAaNKGEVVSHVASDNRMGGKMAADFIAKKtGNdaKVIQLEGISGTSAAR-ERGEGFNA-----GAKEHKFNVL 182
Cdd:PRK10014 146 PVVFASRA-SYLDDVDTVRPDNMQAAQLLTEHLIRN-GH--QRIAWLGGQSSSLTRaERVGGYCAtllkfGLPFHSEWVL 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493711027 183 ASqpaDFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR 231
Cdd:PRK10014 222 EC---TSSQKQAAEAITALLRHNPTISAVVCYNETIAMGAWFGLLRAGR 267
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
58-254 |
7.19e-06 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 46.88 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 58 ELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKIPVITLdrAANKGEVVS----HVASDNRMG 133
Cdd:pfam13458 44 ELVVADDQGDPDVAAAAARRLVDQDGVDAIVGGVSSAVALAVAEVLAKKGVPVIGP--AALTGEKCSpyvfSLGPTYSAQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 134 GKMAADFIAKKTGND-AKVIQLEGISGTSAARergeGFNAGAKEHKFNVLASQPADFDRTKGLNVMQNLLTAHPavQAVF 212
Cdd:pfam13458 122 ATALGRYLAKELGGKkVALIGADYAFGRALAA----AAKAAAKAAGGEVVGEVRYPLGTTDFSSQVLQIKASGA--DAVL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493711027 213 AQND-EMALGALRALQTAG--RDDVLVVGFDGTNDGIKAVQGGKL 254
Cdd:pfam13458 196 LANAgADTVNLLKQAREAGldAKGIKLVGLGGDEPDLKALGGDAA 240
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
28-285 |
7.89e-06 |
|
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380521 [Multi-domain] Cd Length: 268 Bit Score: 46.51 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELAnvqdltvrgtklmLINPTDSDAVGNSILMANK-- 105
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELD-------------LLNTMLSKQVDGIIFMGDElt 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 106 ---------AKIPVITLDRAANKGEVVShVASDNRMGGK-MAADFIAKktGNDaKVIQLEGISGTSAARERGE-GFNAGA 174
Cdd:cd06298 68 eeireefkrSPVPVVLAGTVDSDHEIPS-VNIDYEQAAYdATKSLIDK--GHK-KIAFVSGPLKEYINNDKKLqGYKRAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 175 KE--HKFN---VLAsqpADFDRTKGLNVMQNLLTAHPAvQAVFAQNDEMALGALRALQTAGR---DDVLVVGFDGTNdgI 246
Cdd:cd06298 144 EEagLEFNeplIFE---GDYDYDSGYELYEELLESGEP-DAAIVVRDEIAVGLLNAAQDRGLkvpEDLEIIGFDNTR--Y 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 493711027 247 KAVQGGKLgATIAQRPDQIGIVGVQIADKVLKGEKVEAT 285
Cdd:cd06298 218 ATMSRPQL-TSINQPLYDIGAVAMRLLTKLMNKEEVEET 255
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
86-240 |
1.12e-05 |
|
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, 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 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: 380496 [Multi-domain] Cd Length: 266 Bit Score: 45.83 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 86 MLINPTDSDAvgnSILMANKAKIPVITLDRAANKgevVSHVASDNRMGGKMAADFIAKKTGNDAKVIQleGISGTSAARE 165
Cdd:cd06272 61 IVFGISDSDI---EYLNKNKPKIPIVLYNRESPK---YSTVNVDNEKAGRLAVLLLIQKGHKSIAYIG--NPNSNRNQTL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 166 RGEGFNAGAKEHKFNVLAS--QPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG---RDDVLVVGFD 240
Cdd:cd06272 133 RGKGFIETCEKHGIHLSDSiiDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGisiPEDISIVSYD 212
|
|
| PBP1_ABC_transporter_LIVBP-like |
cd06268 |
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ... |
48-253 |
1.14e-05 |
|
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily; Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.
Pssm-ID: 380492 [Multi-domain] Cd Length: 298 Bit Score: 46.17 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 48 AQKEADKLG------YELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKIPVITL-----DRA 116
Cdd:cd06268 26 AVEEINAAGgingrkLELVIADDQGDPETAVAVARKLVDDDKVLAVVGHYSSSVTLAAAPIYQEAGIPLISPgstapELT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 117 ANKGEVVSHVASDNRMGGKMAADFIAKKtGNDAKV--IQLEGISGTSAArergEGFNAGAKEHKFNVLASQPADFDRTKG 194
Cdd:cd06268 106 EGGGPYVFRTVPSDAMQAAALADYLAKK-LKGKKVaiLYDDYDYGKSLA----DAFKKALKALGGEIVAEEDFPLGTTDF 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493711027 195 LNVMQNLLTAHPAVQAVFAQNDEMALgALRALQTAGrDDVLVVGFDGTNDGIKAVQGGK 253
Cdd:cd06268 181 SAQLTKIKAAGPDVLFLAGYGADAAN-ALKQARELG-LKLPILGGDGLYSPELLKLGGE 237
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
29-241 |
3.62e-05 |
|
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) 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 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: 380495 [Multi-domain] Cd Length: 264 Bit Score: 44.34 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVIS---TLNNPFFVTMKDAAQKEADKLGYELIVLdsQDNPAKELANVQDLT----VRGTKLMLINPTDSdavgnSIL 101
Cdd:cd06271 2 IALVFPvteTELNGTVSE*VSGITEEAGTTGYHLLVW--PFEEAES*VPIRDLVetgsADGVILSEIEPNDP-----RVQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 102 MANKAKIPVITLDRAaNKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVIQLEgiSGTSAARERGEGFNAGAKEHKFNV 181
Cdd:cd06271 75 FLTKQNFPFVAHGRS-D*PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPP--ARYSPHDRRLQGYVRA*RDAGLTG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493711027 182 LAsQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG---RDDVLVVGFDG 241
Cdd:cd06271 152 YP-LDADTTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGlkiGEDVSIIGKDS 213
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
28-280 |
1.06e-04 |
|
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380655 Cd Length: 298 Bit Score: 43.01 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 28 SIALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAK-ELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKA 106
Cdd:cd20000 1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGPTTATAEaQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 107 KIPVITLDRAANKGEVVSHVASDNRMG-GKMAADFIAKKTGNDAKVIQLegiSGTSAARERgegfNAGAKEHKfNVLASQ 185
Cdd:cd20000 81 GIKVVTFDSDVAPEARDLFVNQADADGiGRAQVDMMAELIGGEGEFAIL---SATPTATNQ----NAWIDAMK-KELASP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 186 P-----------ADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAG-RDDVLVVGFDGTNDGIKAVQGGK 253
Cdd:cd20000 153 EyagmklvkvayGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGlKGKVKVTGLGLPSEMAKYVKDGT 232
|
250 260
....*....|....*....|....*..
gi 493711027 254 LGATIAQRPDQIGIVGVQIADKVLKGE 280
Cdd:cd20000 233 VPAFALWNPIDLGYLAAYAAAALAQGE 259
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
86-295 |
1.72e-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: 380510 [Multi-domain] Cd Length: 268 Bit Score: 42.41 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 86 MLINPTDSDAVGNSILmanKAKIPVITLDRAANKGEVVSHVasDNRmGGKMAADFIAKKTGNDAKVIQL-EGISGTSAAR 164
Cdd:cd06287 61 IVVEPTVEDPILARLR---QRGVPVVSIGRAPGTDEPVPYV--DLQ-SAATARLLLEHLHGAGARQVALlTGSSRRNSSL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 165 ERGEGFNAGAKEHKFN-VLASQPADFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGR---DDVLVVgfd 240
Cdd:cd06287 135 ESEAAYLRFAQEYGTTpVVYKVPESEGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRsvpEDLMVV--- 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493711027 241 gTN-DGIKAVQGGKLGATIAQRPDQIGIVGVQIADKVLKGEKVEATVPVELELVVK 295
Cdd:cd06287 212 -TRyDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSVEVGPAPELVVR 266
|
|
| PBP1_ABC_sugar_binding-like |
cd06315 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
29-152 |
9.70e-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: 40.02 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 29 IALVISTLNNPFFVTMKDAAQKEADKLGYELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSDAVGNSILMANKAKI 108
Cdd:cd06315 3 IAYVASDLRNGGVLGVGRGVKEAAAALGWKVDVLDGGGTVTGRLAALNQALALKPDGIILGGDDAVELQEPLKKAVKAGI 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 493711027 109 PVITLDRAA-----NKGEVVSHVASDNRMGGKMAADFIAKKTGNDAKVI 152
Cdd:cd06315 83 PVVGWHAAAspgpiPELGLFTNITTDPREVAETAAALVIAQSGGKAGVV 131
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
188-240 |
3.68e-03 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 38.44 E-value: 3.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 493711027 188 DFDRTKGLNVMQNLLTAHPAVQAVFAQNDEMALGalrALQTAGR------DDVLVVGFD 240
Cdd:PRK11041 194 DFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALG---ALSQAKRmglrvpQDLSIIGFD 249
|
|
| PBP1_ABC_ligand_binding-like |
cd06343 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
58-255 |
6.61e-03 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however its ligand specificity has not been determined experimentally.
Pssm-ID: 380566 [Multi-domain] Cd Length: 355 Bit Score: 37.55 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 58 ELIVLDSQDNPAKELANVQDLTVRGTKLMLINPTDSdAVGNSIL-MANKAKIPVITLDRAANKGEVVSH-----VASDNR 131
Cdd:cd06343 49 ELIVEDDGYDPARAVAAVRKLVEQDKVFAIVGGLGT-PTNLAVRpYLNEAGVPQLFPATGASALSPPPKpytfgVQPSYE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 132 MGGKMAADFIAkKTGNDAKViqleGI--SGTSAARERGEGFNAGAKEHKFNVLASQP-----ADFDrtkglNVMQNLLTA 204
Cdd:cd06343 128 DEGRILADYIV-ETLPAAKV----AVlyQNDDFGKDGLEGLKEALKAYGLEVVAEETyepgdTDFS-----SQVLKLKAA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493711027 205 HP-AVqaVFAQNDEMALGALRALQTAGRDDVLVVGFDGTNDGIKAVQGGKLG 255
Cdd:cd06343 198 GAdVV--VLGTLPKEAAAALKEAAKLGWKPTFLGSSVSADPTTLAKAGGDAA 247
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
32-153 |
6.71e-03 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 37.58 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 32 VISTLNNPFFVTMKDAAQKEADKLGYELIVLDsqDNPAKELANVQDLTVRGTKLMLInPTDSDAVGNS---ILMANKAKI 108
Cdd:COG2984 137 VLYNPSEANSVAQVEELKKAAKKLGLELVEAT--VTSSNEIQQALQSLAGKVDAIYV-PTDNTVVSALeaiAKVAARAKI 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 493711027 109 PVITLDRA-ANKGEVVSHVASDNRMG---GKMAADFIAKKTGNDAKVIQ 153
Cdd:COG2984 214 PVFGGDDSsVKAGALAGYGIDYYELGrqaAEMALRILKGEKPADIPVET 262
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
163-243 |
6.72e-03 |
|
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380664 [Multi-domain] Cd Length: 266 Bit Score: 37.52 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493711027 163 ARERGEGFNAGAKEHKFNVLASQPADFDRT--KGLNVMQNLLTAHPAVQAVFAQNDEMALGALRALQTAGRD---DVLVV 237
Cdd:cd20009 133 AQHRLRGFRRALAEAGLEVEPLLIVTLDSSaeAIRAAARRLLRQPPRPDGIICASEIAALGALAGLEDAGLVvgrDVDVV 212
|
....*.
gi 493711027 238 GFDGTN 243
Cdd:cd20009 213 AKETSP 218
|
|
| |
