|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
1-311 |
0e+00 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 578.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 1 MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSN 80
Cdd:PRK09701 1 MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 81 KNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVA 160
Cdd:PRK09701 81 KNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 161 IIEGKAGNASGEARRNGATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGK 240
Cdd:PRK09701 161 IIEGKAGNASGEARRNGATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446968931 241 TGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLMVDAEKSGKVIPLDKAPEFKLVDSILVTQ 311
Cdd:PRK09701 241 TGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLMVDAEKSGKVIPLDKAPEFKLVDSILVTQ 311
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
26-310 |
1.08e-134 |
|
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: 383.15 E-value: 1.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 26 EYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWK 105
Cdd:cd06320 1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 KGIYLVNLDEKIDMDNLKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKA 185
Cdd:cd06320 81 KGIPVINLDDAVDADALKKAGGKVTSFIGTDNVAAGALAAEYIAEKLP-GGGKVAIIEGLPGNAAAEARTKGFKETFKKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMT 265
Cdd:cd06320 160 PGLKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTGKVLVVGTDGIPEAKKSIKAGELT 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446968931 266 ATVAQNPADIGATGLKLMVDAEKSGKvIPLDKAPEFKLVDSILVT 310
Cdd:cd06320 240 ATVAQYPYLEGAMAVEAALRLLQGQK-VPAVVATPQALITKDNVD 283
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
26-308 |
2.18e-103 |
|
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: 303.81 E-value: 2.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 26 EYAVVLKTL---SNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGdfQSQLQLFEDLSNKNYKGIAFAPLSSVNLVmPVAR 102
Cdd:cd01391 1 IIGVVTSSLhqiREQFGIQRVEAIFHTADKLGASVEIRDSCWHG--SVALEQSIEFIRDNIAGVIGPGSSSVAIV-IQNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 103 AWKKGIYLVNLDEKIDMDNLKkAGGNVEAFVTTDNVAVGAKGASFIIDKLGaegGEVAIIEGKAGNaSGEARRNGATEAF 182
Cdd:cd01391 78 AQLFDIPQLALDATSQDLSDK-TLYKYFLSVVFSDTLGARLGLDIVKRKNW---TYVAAIHGEGLN-SGELRMAGFKELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 183 KKAsQIKLVASQPADWDRI-KALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARK--MV 259
Cdd:cd01391 153 KQE-GICIVASDKADWNAGeKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLVGDVSVIGSDGWADRDEvgYE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446968931 260 EAGQMTATVAQNPADIGATGLKLMVDAEKSGKVIPLDKAPEFKLVDSIL 308
Cdd:cd01391 232 VEANGLTTIKQQKMGFGITAIKAMADGSQNMHEEVWFDEKGDALGRYIL 280
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
28-294 |
1.18e-85 |
|
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: 258.27 E-value: 1.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd01536 3 GVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDA--QGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkAGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKASQ 187
Cdd:cd01536 81 IPVVAVDTDID------GGGDVVAFVGTDNYEAGKLAGEYLAEALG-GKGKVAILEGPPGSSTAIDRTKGFKEALKKYPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTAT 267
Cdd:cd01536 154 IEIVAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGDIKIVGVDGTPEALKAIKDGELDAT 233
|
250 260
....*....|....*....|....*..
gi 446968931 268 VAQNPADIGATGLKLMVDAEKSGKVIP 294
Cdd:cd01536 234 VAQDPYLQGYLAVEAAVKLLNGEKVPK 260
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
18-311 |
2.00e-79 |
|
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: 243.68 E-value: 2.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 18 STSAFAAAEY--AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFasPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVN 95
Cdd:COG1879 25 EAAAAAAKGKtiGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVV--DAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 96 LVMPVARAWKKGIYLVNLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARR 175
Cdd:COG1879 103 LAPALKKAKAAGIPVVTVDSDVD-------GSDRVAYVGSDNYAAGRLAAEYLAKALG-GKGKVAILTGSPGAPAANERT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 176 NGATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEA 255
Cdd:COG1879 175 DGFKEALKEYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKGDVKVVGFDGSPEA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446968931 256 RKMVEAGQMTATVAQNPADIGATGLKLMVDAeKSGKvipldKAPEFKLVDSILVTQ 311
Cdd:COG1879 255 LQAIKDGTIDATVAQDPYLQGYLAVDAALKL-LKGK-----EVPKEILTPPVLVTK 304
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-303 |
3.98e-74 |
|
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: 229.06 E-value: 3.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKT-LGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKK 106
Cdd:cd19970 3 ALVMKSLANEFFIEMEKGARKHAKEaNGYELLVKGIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEKIDMDNLKKAGGNVeAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKAS 186
Cdd:cd19970 83 GIAVINIDNRLDADALKEGGINV-PFVGPDNRQGAYLAGDYLAKKLG-KGGKVAIIEGIPGADNAQQRKAGFLKAFEEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 187 qIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTA 266
Cdd:cd19970 161 -MKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGKVLVVGFDNIPAVRPLLKDGKMLA 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 446968931 267 TVAQNPADIGATGLKLMVDAeKSGKVIPLDKAPEFKL 303
Cdd:cd19970 240 TIDQHPAKQAVYGIEYALKM-LNGEEVPGWVKTPVEL 275
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
28-310 |
2.17e-56 |
|
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: 183.27 E-value: 2.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVsvDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd06323 3 GLSVSTLNNPFFVSLKDGAQAEAKELGV--ELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIdmdnlkkAGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKASQ 187
Cdd:cd06323 81 IPVITVDRSV-------TGGKVVSHIASDNVAGGEMAAEYIAKKLG-GKGKVVELQGIPGTSAARERGKGFHNAIAKYPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTgKVLVVGTDGIPEARKMVEAGQMTAT 267
Cdd:cd06323 153 INVVASQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRK-DVIVVGFDGTPDAVKAVKDGKLAAT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446968931 268 VAQNPADIGATGLklmvdaEKSGKVIPLDKAPEFKLVDSILVT 310
Cdd:cd06323 232 VAQQPEEMGAKAV------ETADKYLKGEKVPKKIPVPLKLVT 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-305 |
4.27e-54 |
|
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: 177.53 E-value: 4.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd06310 3 GVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGgEVAIIEGKAGNASGEARRNGATEAFKK-AS 186
Cdd:cd06310 83 IPVIVIDSGIK-------GDAYLSYIATDNYAAGRLAAQKLAEALGGKG-KVAVLSLTAGNSTTDQREEGFKEYLKKhPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 187 QIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTA 266
Cdd:cd06310 155 GIKVLASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIVGFDSQEELLDALKNGKIDA 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 446968931 267 TVAQNPADIGATGLKLMVDAEKsGKVIPLDKAPEFKLVD 305
Cdd:cd06310 235 LVVQNPYEIGYEGIKLALKLLK-GEEVPKNIDTGAELIT 272
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
28-310 |
1.16e-53 |
|
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: 176.36 E-value: 1.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd19967 3 AVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDH--QNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIdmdnlkKAGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKASQ 187
Cdd:cd19967 81 IPVFLIDREI------NAEGVAVAQIVSDNYQGAVLLAQYFVKLMG-EKGLYVELLGKESDTNAQLRSQGFHSVIDQYPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTAT 267
Cdd:cd19967 154 LKMVAQQSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRAGDVIIVGFDGSNDVRDAIKEGKISAT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446968931 268 VAQNPADIGATGLKLMVDAEKSGKVipldKAPEFKLVDSILVT 310
Cdd:cd19967 234 VLQPAKLIARLAVEQADQYLKGGST----GKEEKQLFDCVLIT 272
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
28-286 |
4.06e-53 |
|
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: 174.42 E-value: 4.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFAsPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:pfam13407 2 GVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVG-PAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDekIDMDNlkkagGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKK-AS 186
Cdd:pfam13407 81 IPVVTFD--SDAPS-----SPRLAYVGFDNEAAGEAAGELLAEALG-GKGKVAILSGSPGDPNANERIDGFKKVLKEkYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 187 QIKLVAS-QPADWDRIKALDVATNVLQRNPN-IKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQM 264
Cdd:pfam13407 153 GIKVVAEvEGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTI 232
|
250 260
....*....|....*....|..
gi 446968931 265 TATVAQNPADIGATGLKLMVDA 286
Cdd:pfam13407 233 DATVLQDPYGQGYAAVELAAAL 254
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
33-296 |
1.72e-52 |
|
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.
Pssm-ID: 380531 [Multi-domain] Cd Length: 268 Bit Score: 173.12 E-value: 1.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 33 TLSNPFWVDMKKGIEDEA-KTLGVSVdIFASpSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLV 111
Cdd:cd06308 8 SLNDPWRAAMNEEIKAEAaKYPNVEL-IVTD-AQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 112 NLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKASQIKLV 191
Cdd:cd06308 86 VLDRKVS-------GDDYTAFIGADNVEIGRQAGEYIAELLN-GKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYPGIKIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 192 ASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEAR-KMVEAGQMTATVaQ 270
Cdd:cd06308 158 ASQDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKEIKIIGVDGLPEAGeKAVKDGILAATF-L 236
|
250 260
....*....|....*....|....*....
gi 446968931 271 NPaDIGATGLKLMVDA---EKSGKVIPLD 296
Cdd:cd06308 237 YP-TGGKEAIEAALKIlngEKVPKEIVLP 264
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-296 |
4.56e-52 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 172.97 E-value: 4.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 1 MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVsvDIFASPSEGDFQSQLQLFEDLSN 80
Cdd:PRK10653 3 MKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGY--NLVVLDSQNNPAKELANVQDLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 81 KNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKidmdnlkKAGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVA 160
Cdd:PRK10653 81 RGTKILLINPTDSDAVGNAVKMANQANIPVITLDRG-------ATKGEVVSHIASDNVAGGKMAGDFIAKKLG-EGAKVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 161 IIEGKAGNASgeARRNGatEAFKKA---SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVAN 237
Cdd:PRK10653 153 QLEGIAGTSA--ARERG--EGFKQAvaaHKFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQT 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446968931 238 AGKTgKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKL---MVDAEKSGKVIPLD 296
Cdd:PRK10653 229 AGKS-DVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGVETadkVLKGEKVEAKIPVD 289
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-294 |
8.36e-52 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 171.64 E-value: 8.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKkG 107
Cdd:cd20008 3 AVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAADA-G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDMDNlkkaggnVEAFVTTDNVAVGAKGASFIIDKLGAEG---GEVAIIEGKAGNASGEARRNGATEAFK- 183
Cdd:cd20008 82 IPVVLVDSGANTDD-------YDAFLATDNVAAGALAADELAELLKASGggkGKVAIISFQAGSQTLVDREEGFRDYIKe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 184 KASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQ 263
Cdd:cd20008 155 KYPDIEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAGKIVLVGFDSSPDEVALLKSGV 234
|
250 260 270
....*....|....*....|....*....|.
gi 446968931 264 MTATVAQNPADIGATGLKLMVDAEKSGKVIP 294
Cdd:cd20008 235 IKALVVQDPYQMGYEGVKTAVKALKGEEIVE 265
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
27-294 |
1.24e-49 |
|
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: 165.83 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKK 106
Cdd:cd06314 2 FALVPKGLNNPFWDLAEAGAEKAAKELGVNV-EFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEkiDMDNLKKaggnvEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKAS 186
Cdd:cd06314 81 GIPVITFDS--DAPDSKR-----LAYIGTDNYEAGREAGELMKKALP-GGGKVAIITGGLGADNLNERIQGFKDALKGSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 187 QIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTA 266
Cdd:cd06314 153 GIEIVDPLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVIAA 232
|
250 260
....*....|....*....|....*...
gi 446968931 267 TVAQNPADIGATGLKLMVDAEKSGKVIP 294
Cdd:cd06314 233 TVGQRPYEMGYLSVKLLYKLLKGGKPVP 260
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
28-311 |
2.43e-49 |
|
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: 165.52 E-value: 2.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVsvDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd06313 3 GFTVYGLSSEFITNLVEAMKAVAKELNV--DLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDMDNLKkaggnveAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKASQ 187
Cdd:cd06313 81 IPLVGVNALIENEDLT-------AYVGSDDVVAGELEGQAVADRLG-GKGNVVILEGPIGQSAQIDRGKGIENVLKKYPD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVASQPADWDRIKALDVATNVLQRNP-NIKAIYCANDTMAMGVAQAVANAGKTgKVLVVGTDGIPEARKMVEAGQMTA 266
Cdd:cd06313 153 IKVLAEQTANWSRDEAMSLMENWLQAYGdEIDGIIAQNDDMALGALQAVKAAGRD-DIPVVGIDGIEDALQAVKSGELIA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446968931 267 TVAQNPADIGATGLKLMVDAEKSGKVipldkaPEFKLVDSILVTQ 311
Cdd:cd06313 232 TVLQDAEAQGKGAVEVAVDAVKGEGV------EKKYYIPFVLVTK 270
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
35-311 |
1.15e-47 |
|
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.
Pssm-ID: 380532 [Multi-domain] Cd Length: 285 Bit Score: 161.23 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 35 SNPFWVDMKKGIEDEAKTLGVSVDIfaSPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLD 114
Cdd:cd06309 10 ESPWRVANTKSIKEAAKKRGYELVY--TDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 115 EKIDMdnlkKAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAFKKASQIKLVASQ 194
Cdd:cd06309 88 RTIDG----EDGSLYVTFIGSDFVEEGRRAAEWLVKNYKGGKGNVVELQGTAGSSVAIDRSKGFREVIKKHPNIKIVASQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 195 PADWDRIKALDVATNVLQRNP-NIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVEAGQMTATVAQN 271
Cdd:cd06309 164 SGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLKpgKDVLVVGIDGQKDALEAIKAGELNATVECN 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446968931 272 PAdIGATGLKLMVDAEKSGKVipldkaPEFKLVDSILVTQ 311
Cdd:cd06309 244 PL-FGPTAFDTIAKLLAGEKV------PKLIIVEERLFDK 276
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-305 |
1.77e-47 |
|
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: 160.48 E-value: 1.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd20007 3 ALVPGVTGDPFYITMQCGAEAAAKELGVELD-VQGPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDMDNLkkaggnVEAFVTTDNVAVGAKGASFIIDKLGAEGgEVAIIEGKAGNASGEARRNGATEAFKKASQ 187
Cdd:cd20007 82 IKVVTVDTTLGDPSF------VLSQIASDNVAGGALAAEALAELIGGKG-KVLVINSTPGVSTTDARVKGFAEEMKKYPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTAT 267
Cdd:cd20007 155 IKVLGVQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGKVKVVGFDASPAQVEQLKAGTIDAL 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 446968931 268 VAQNPADIGATGLKLMVDAEKsGKVIPLDKAPEFKLVD 305
Cdd:cd20007 235 IAQKPAEIGYLAVEQAVAALT-GKPVPKDILTPFVVIT 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-305 |
2.50e-47 |
|
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: 160.13 E-value: 2.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd06322 3 GVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADA--NGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEaRRNGATEAFKKASQ 187
Cdd:cd06322 81 IPVFTVDVKAD-------GAKVVTHVGTDNYAGGKLAGEYALKALLGGGGKIAIIDYPEVESVVL-RVNGFKEAIKKYPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMV-EAGQMTA 266
Cdd:cd06322 153 IEIVAEQPGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDKIKVIGFDGNPEAIKAIaKGGKIKA 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 446968931 267 TVAQNPADIGATGLKLMVDAEKsGKVIPLDKAPEFKLVD 305
Cdd:cd06322 233 DIAQQPDKIGQETVEAIVKYLA-GETVEKEILIPPKLYT 270
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-292 |
5.97e-47 |
|
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: 158.94 E-value: 5.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPS-EGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKK 106
Cdd:cd20004 3 AVIPKGTTHDFWKSVKAGAEKAAQELGVEI-YWRGPSrEDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGAeGGEVAIIEGKAGNASGEARRNGATEAFKK-A 185
Cdd:cd20004 82 GIPVVIIDSDLG-------GDAVISFVATDNYAAGRLAAKRMAKLLNG-KGKVALLRLAKGSASTTDRERGFLEALKKlA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMT 265
Cdd:cd20004 154 PGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLAGKVKFIGFDASDLLLDALRAGEIS 233
|
250 260
....*....|....*....|....*..
gi 446968931 266 ATVAQNPADIGATGLKLMVDAEKSGKV 292
Cdd:cd20004 234 ALVVQDPYRMGYLGVKTAVAALRGKPV 260
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-295 |
2.34e-46 |
|
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: 157.40 E-value: 2.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd20005 3 AVISKGFQHQFWKAVKKGAEQAAKELGVKITFEGPDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGgEVAIIEGKAGNASGEARRNGATEAFKK-AS 186
Cdd:cd20005 83 IPVVTFDSGVP-------SDLPLATVATDNYAAGALAADHLAELIGGKG-KVAIVAHDATSETGIDRRDGFKDEIKEkYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 187 QIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTA 266
Cdd:cd20005 155 DIKVVNVQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLGKIKVVGFDSGEAQIDAIKNGVIAG 234
|
250 260
....*....|....*....|....*....
gi 446968931 267 TVAQNPADIGATGLKLMVDAEKSGKVIPL 295
Cdd:cd20005 235 SVTQNPYGMGYKTVKAAVKALKGEEVEKL 263
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
28-291 |
4.28e-45 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 154.08 E-value: 4.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFasPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd19968 3 GFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVL--DAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKASQ 187
Cdd:cd19968 81 IPVVTVDRRAE-------GAAPVPHVGADNVAGGREVAKFVVDKLP-NGAKVIELTGTPGSSPAIDRTKGFHEELAAGPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVASQPADWDRIKALDVATNVLQRNPN-IKAIYCANDTMAMGVAQAVANAG-KTGKVLVVGTDGIPEARKMVEAGQMT 265
Cdd:cd19968 153 IKVVFEQTGNFERDEGLTVMENILTSLPGpPDAIICANDDMALGAIEAMRAAGlDLKKVKVIGFDAVPDALQAIKDGELY 232
|
250 260
....*....|....*....|....*.
gi 446968931 266 ATVAQNPADIGATGLKLMVDAEKSGK 291
Cdd:cd19968 233 ATVEQPPGGQARTALRILVDYLKDKK 258
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
27-292 |
6.50e-45 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380626 [Multi-domain] Cd Length: 267 Bit Score: 153.51 E-value: 6.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLG---VSVDifaspSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARA 103
Cdd:cd19971 2 FGFSYMTMNNPFFIAINDGIKKAVEANGdelITRD-----PQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 104 WKKGIYLVNLDEKIDMDNLkkaggnVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEaRRNGATEAFK 183
Cdd:cd19971 77 KEAGIPVINVDTPVKDTDL------VDSTIASDNYNAGKLCGEDMVKKLP-EGAKIAVLDHPTAESCVD-RIDGFLDAIK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 184 KASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQ 263
Cdd:cd19971 149 KNPKFEVVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKLGDILVYGVDGSPDAKAAIKDGK 228
|
250 260
....*....|....*....|....*....
gi 446968931 264 MTATVAQNPADIGATGLKLMVDAEKSGKV 292
Cdd:cd19971 229 MTATAAQSPIEIGKKAVETAYKILNGEKV 257
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-310 |
1.90e-43 |
|
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: 149.75 E-value: 1.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd06321 3 GVTVQDLGNPFFVAMVRGAEEAAAEINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDekidmdnlkKAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGgEVAIIEGKAGNASGEaRRNGATEAFKKASQ 187
Cdd:cd06321 83 IIVVAVD---------VAAEGADATVTTDNVQAGYLACEYLVEQLGGKG-KVAIIDGPPVSAVID-RVNGCKEALAEYPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGkVLVVGTDGIPEARKMV--EAGQMT 265
Cdd:cd06321 152 IKLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDD-IVITSVDGSPEAVAALkrEGSPFI 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446968931 266 ATVAQNPADIGATGLKLMVDAEKSGKVipldkAPEFKLVDSILVT 310
Cdd:cd06321 231 ATAAQDPYDMARKAVELALKILNGQEP-----APELVLIPSTLVT 270
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
38-310 |
2.69e-43 |
|
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: 149.51 E-value: 2.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 38 FWVDMKKGIEDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKI 117
Cdd:cd19972 13 FFNQIKQSVEAEAKKKGYKVITVDA--KGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 118 DmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGgEVAIIEGKAGNASGEARRNGATEAFKKASQIKLVASQPAD 197
Cdd:cd19972 91 E-------DAPGDTFIATDSVAAAKELGEWVIKQTGGKG-EIAILHGQLGTTPEVDRTKGFQEALAEAPGIKVVAEQTAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 198 WDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGA 277
Cdd:cd19972 163 WDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDHKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKMGR 242
|
250 260 270
....*....|....*....|....*....|...
gi 446968931 278 TGLKLMVDaeksgkVIPLDKAPEFKLVDSILVT 310
Cdd:cd19972 243 LAVDSAID------LLNGKAVPKEQLQDAVLTT 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
33-284 |
3.72e-43 |
|
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: 149.43 E-value: 3.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 33 TLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSegDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVN 112
Cdd:cd06319 8 DLDNPFWQIMERGVQAAAEELGYEFVTYDQKN--SANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIPVVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 113 LDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGA---EGGEVAIIEGKAGNASGEARRNGATEAFKKASQIK 189
Cdd:cd06319 86 ADIGTG-------GGDYVSYIISDNYDGGYQAGEYLAEALKEngwGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 190 LVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVA 269
Cdd:cd06319 159 VALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGDILVVGFDGDPEALDLIKDGKLDGTVA 238
|
250
....*....|....*
gi 446968931 270 QNPADIGATGLKLMV 284
Cdd:cd06319 239 QQPFGMGARAVELAI 253
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
26-286 |
1.40e-42 |
|
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: 147.87 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 26 EYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWK 105
Cdd:cd19969 1 YYVMVTFKSGHPYWDDVKEGFEDAGAELGVKTE-YTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 KGIYLVNldekIDMDNLKkagGNVEAFVTTDNVAVGAKGASFIIDKLGAEGgEVAIIEGKaGNASGEARRNGATEAFKKA 185
Cdd:cd19969 80 AGIPVVT----FDSDAPE---SKRISYVGTDNYEAGYAAAEKLAELLGGKG-KVAVLTGP-GQPNHEERVEGFKEAFAEY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMT 265
Cdd:cd19969 151 PGIEVVAVGDDNDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTGKVKIVAFDDDPETLDLIKDGVID 230
|
250 260
....*....|....*....|.
gi 446968931 266 ATVAQNPADIGATGLKLMVDA 286
Cdd:cd19969 231 ASIAQRPWMMGYWSLQFLYDL 251
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
29-304 |
1.10e-41 |
|
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: 145.45 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKT-LGVSVDIfaSPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd06301 5 VSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVI--VDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGeVAIIEGKAGNASGEARRNGATEAFKKASQ 187
Cdd:cd06301 83 IPLVYVNREPD------SKPKGVAFVGSDDIESGELQMEYLAKLLGGKGN-IAILDGVLGHEAQILRTEGNKDVLAKYPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTAT 267
Cdd:cd06301 156 MKIVAEQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDDILVAGIDATPDALKAMKAGRLDAT 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 446968931 268 VAQNPADIGATGLKLMVDAEKSGKVIPLDKAPeFKLV 304
Cdd:cd06301 236 VFQDAAGQGETAVDVAVKAAKGEEVESDIWIP-FELV 271
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-311 |
3.91e-40 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 141.20 E-value: 3.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNP--FWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWK 105
Cdd:cd20006 3 ALILKSSDPNsdFWQTVKSGAEAAAKEYGVDLEFLGPESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 KGIYLVNLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKgASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAFKKA 185
Cdd:cd20006 83 AGIPVITIDSPVN-------SKKADSFVATDNYEAGKK-AGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQALAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMT 265
Cdd:cd20006 155 PNIKIVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLGGKVKVVGFDSSVEEIQLLEEGIID 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446968931 266 ATVAQNPADIGATGLKLMVDAEKSGKVipldkaPEFKLVDSILVTQ 311
Cdd:cd20006 235 ALVVQNPFNMGYLSVQAAVDLLNGKKI------PKRIDTGSVVITK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
47-297 |
7.26e-39 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 137.88 E-value: 7.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 47 EDEAKTL-GVSVDIFASPSEGDFQSQLqlfEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMdnlkka 125
Cdd:cd06311 22 EKQAKELaDLEYKLVTSSNANEQVSQL---EDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNV------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 126 gGNVEAFVTTDNVAVGAKGASFIIDKLGAEGgEVAIIEGKAGNASGEARRNGATEAFKKASQIKLVASQPADWDRIKALD 205
Cdd:cd06311 93 -LIYDLYVAGDNPGMGVVSAEYIGKKLGGKG-NVVVLEVPSSGSVNEERVAGFKEVIKGNPGIKILAMQAGDWTREDGLK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 206 VATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMT--ATVAQNPADIgATGLKLM 283
Cdd:cd06311 171 VAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIKVMTGGGGSQEYFKRIMDGDPIwpASATYSPAMI-ADAIKLA 249
|
250
....*....|....
gi 446968931 284 VDAEKSGKVIPLDK 297
Cdd:cd06311 250 VLILKGGKTVEKEV 263
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
32-310 |
1.50e-36 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 132.15 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 32 KTLSNPFWVDMKKGIEDEAKTLGVSVdiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLV 111
Cdd:cd06318 7 RTLASPYYAALVAAAKAEAKKLGVEL--VVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGIPVI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 112 NLDEKIDmdnlkkAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAFKKA------ 185
Cdd:cd06318 85 TVDSALD------PSANVATQVGRDNKQNGVLVGKEAAKALGGDPGKIIELSGDKGNEVSRDRRDGFLAGVNEYqlrkyg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 -SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQM 264
Cdd:cd06318 159 kSNIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVKVAGADGQKEALKLIKDGKY 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446968931 265 TATVAQNPADIGATGLKLMVDAEKSGKVIpldkaPEFKLVDSILVT 310
Cdd:cd06318 239 VATGLNDPDLLGKTAVDTAAKVVKGEESF-----PEFTYTPTALIT 279
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
35-269 |
6.95e-35 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 128.49 E-value: 6.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 35 SNPFWVDMKKGIEDEAKTLGVSVDIFasPSEGDFQSQLQLFEDLSNK----------NYKGIAFAplssvnlVMPVARaw 104
Cdd:cd06324 11 DEPFWQNVTRFMQAAAKDLGIELEVL--YANRNRFKMLELAEELLARppkpdylilvNEKGVAPE-------LLELAE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 105 KKGIYLVNLDEKIDMDNLKKAGGNVE------AFVTTDNVAVGAKGASFIIDKLGA----EGGEVAIIEGKAGNASGEAR 174
Cdd:cd06324 80 QAKIPVFLINNDLTDEERALLGKPREkfkywlGSIVPDNEQAGYLLAKALIKAARKksddGKIRVLAISGDKSTPASILR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 175 RNGATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT-GK-VLVVGTDGI 252
Cdd:cd06324 160 EQGLRDALAEHPDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKpGKdVLVGGIDWS 239
|
250
....*....|....*..
gi 446968931 253 PEARKMVEAGQMTATVA 269
Cdd:cd06324 240 PEALQAVKDGELTASVG 256
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
29-304 |
8.21e-34 |
|
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: 124.62 E-value: 8.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGI 108
Cdd:cd06306 4 VLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGGYTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 109 YLVNLDEKIDMDNlkkaggnVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAFKKaSQI 188
Cdd:cd06306 84 PVIDLVNGIDSPK-------VAARVLVDFYDMGYLAGEYLVEHHPGKPVKVAWFPGPAGAGWAEDREKGFKEALAG-SNV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 189 KLVASQPADWDRIKALDVATNVLQRNPNIKAIYcANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATV 268
Cdd:cd06306 156 EIVATKYGDTGKAVQLNLVEDALQAHPDIDYIV-GNAVAAEAAVGALREAGLTGKVKVVSTYLTPGVYRGIKRGKILAAP 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 446968931 269 AQNPADIGATGLKLMVDAEKsGKVIPLDKAPEFKLV 304
Cdd:cd06306 235 SDQPVLQGRIAVDQAVRALE-GKPVPKHVGPPILVV 269
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
28-278 |
7.50e-32 |
|
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: 120.00 E-value: 7.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASpSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd19992 3 GVSFPTQQEERWQKDKEYMEEEAKELGVEL-IFQV-ADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKlgAEGGEVAIIEGKAGNASGEARRNGATEAFKKA-- 185
Cdd:cd19992 81 VPVISYDRLIL-------NADVDLYVGRDNYKVGQLQAEYALEA--VPKGNYVILSGDPGDNNAQLITAGAMDVLQPAid 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 -SQIKLVASQPAD-WDRIKALDVATNVL-QRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAG 262
Cdd:cd19992 152 sGDIKIVLDQYVKgWSPDEAMKLVENALtANNNNIDAVLAPNDGMAGGAIQALKAQGLAGKVFVTGQDAELAALKRIVEG 231
|
250
....*....|....*.
gi 446968931 263 QMTATVAQNPADIGAT 278
Cdd:cd19992 232 TQTMTVWKDLKELARA 247
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
34-294 |
6.44e-31 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380651 [Multi-domain] Cd Length: 302 Bit Score: 117.73 E-value: 6.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 34 LSNPFWVDMKKGIEDEAKTLGVSV-DIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVN 112
Cdd:cd19996 9 LGNSWRVQMIAEFEAEAAKLKKLIkELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 113 LDEKIDMDNlkkaggnVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKASQIKLVA 192
Cdd:cd19996 89 FDSGVGSDK-------YTAFVGVDDAAFGRVGAEWLVKQLG-GKGNIIALRGIAGVSVSEDRWAGAKEVFKEYPGIKIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 193 SQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTgKVLVVGTDGIPEARKMVEAGQMTATVAQNP 272
Cdd:cd19996 161 EVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRP-LVPMTGEDNNGFLKAWKELPGFKSIAPSYP 239
|
250 260
....*....|....*....|..
gi 446968931 273 ADIGATGLKLMVDAEKsGKVIP 294
Cdd:cd19996 240 PWLGATALDAALAALE-GEPVP 260
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
34-284 |
1.50e-30 |
|
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: 117.02 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 34 LSNPFW-----VDMKKGIEDEAKTL---GVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWK 105
Cdd:cd19999 4 VSNGYVgnewrAQMIADFEEVAAEYkeeGVISDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 KGIYLVNLDEKIDMDNLkkaggnveAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKA 185
Cdd:cd19999 84 AGILVVSFDQPVSSPDA--------INVVIDQYKWAAIQAQWLAEQLG-GKGNIVAINGVAGNPANEARVKAADDVFAKY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCaNDTMAMGVAQAVANAGKTGKVLV-VGTDGIPEARKMVEAGQM 264
Cdd:cd19999 155 PGIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLT-QDGMAEGVLRAFQAAGKDPPVMTgDYRKGFLRKWKELDLPDF 233
|
250 260
....*....|....*....|
gi 446968931 265 TATVAQNPADIGATGLKLMV 284
Cdd:cd19999 234 ESIGVVNPPGIGATALRIAV 253
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
27-276 |
1.69e-30 |
|
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: 116.57 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKK 106
Cdd:cd06302 2 IAFVPKVVGIPYFDAAEEGAKKAAKELGVEV-VYTGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDekIDMDNlkkagGNVEAFVT-TDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFK-K 184
Cdd:cd06302 81 GIKVITWD--SDAPP-----SARDYFVNqADDEGLGEALVDSLAKEIG-GKGKVAILSGSLTATNLNAWIKAMKEYLKsK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 185 ASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTdGIP-EARKMVEAGQ 263
Cdd:cd06302 153 YPDIELVDTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGKVAVTGI-GLPnTARPYLKDGS 231
|
250
....*....|...
gi 446968931 264 MTATVAQNPADIG 276
Cdd:cd06302 232 VKEGVLWDPAKLG 244
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
29-296 |
6.54e-30 |
|
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: 114.87 E-value: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGI 108
Cdd:cd19973 4 LITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 109 YLVNLDEKID-MDnlkkaggNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEARRNG---------- 177
Cdd:cd19973 84 LVIALDTPTDpID-------AADATFATDNFKAGVLIGEWAKAALGAKDAKIATLDLTPGHTVGVLRHQGflkgfgidek 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 178 ATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARK 257
Cdd:cd19973 157 DPESNEDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKEKGVLIVSVDGGCPGVK 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 446968931 258 MVEAGQMTATVAQNPADIGATGLKLMVDAEKSGKVIPLD 296
Cdd:cd19973 237 DVKDGIIGATSQQYPLRMAALGVEAIAAFAKTGGTKGSG 275
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
28-272 |
2.46e-29 |
|
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: 112.75 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd19965 3 VFVTHVTTNPFFQPVKKGMDDACELLGAECQ-FTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 I--YLVNLDekidmdnLKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAFKKA 185
Cdd:cd19965 82 IpvVAFNVD-------APGGENARLAFVGQDLYPAGYVLGKRIAEKFKPGGGHVLLGISTPGQSALEQRLDGIKQALKEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 S---QIKLVASQPadwDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAG 262
Cdd:cd19965 155 GrgiTYDVIDTGT---DLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGKVLVGGFDLVPEVLQGIKAG 231
|
250
....*....|
gi 446968931 263 QMTATVAQNP 272
Cdd:cd19965 232 YIDFTIDQQP 241
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
27-299 |
3.66e-28 |
|
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: 109.77 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKK 106
Cdd:cd06317 2 IALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNA--NDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEKIDMDNlkkaggnVEAFVTTDNVAVGAK----GASFIIDKLGAEGgEVAIIEGKAGNASgEARRNGATEAF 182
Cdd:cd06317 80 GIPVIAYDAVIPSDF-------QAAQVGVDNLEGGKEigkyAADYIKAELGGQA-KIGVVGALSSLIQ-NQRQKGFEEAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 183 KKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPE-ARKMVEA 261
Cdd:cd06317 151 KANPGVEIVATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQGKIKVFGWDLTKQaIFLGIDE 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 446968931 262 GQMTATVAQNPADIGATGLKLMVDAEKSGKVIPLDKAP 299
Cdd:cd06317 231 GVLQAVVQQDPEKMGYEAVKAAVKAIKGEDVEKTIDVP 268
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
28-288 |
1.44e-26 |
|
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: 106.13 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLG-VSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAfaplssVNLVMPVA----- 101
Cdd:cd01539 4 GVFIYNYDDTFISSVRKALEKAAKAGGkIELEIYDA--QNDQSTQNDQIDTMIAKGVDLLV------VNLVDRTAaqtii 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 102 -RAWKKGIYLVNLDEKIDMDNLKKaGGNVeAFVTTDNVAVGAKGASFIIDKLGAEGG---------EVAIIEGKAGNASG 171
Cdd:cd01539 76 dKAKAANIPVIFFNREPSREDLKS-YDKA-YYVGTDAEESGIMQGEIIADYWKANPEidkngdgkiQYVMLKGEPGHQDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 172 EARRNGATEAFKKAS-QIKLVASQPADWDRIKALDVATNVLQRNP-NIKAIYCANDTMAMGVAQAVANAG-----KTGKV 244
Cdd:cd01539 154 IARTKYSVKTLNDAGiKTEQLAEDTANWDRAQAKDKMDAWLSKYGdKIELVIANNDDMALGAIEALKAAGyntgdGDKYI 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446968931 245 LVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLMVDAEK 288
Cdd:cd01539 234 PVFGVDATPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLAN 277
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
28-286 |
1.81e-26 |
|
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: 105.34 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTL---GVSVDIFASPSEgDFQSQLQLFEDLSnKNYKGIAFAPLSSVNLVMPVARAW 104
Cdd:cd06307 3 GFLLPSPENPFYELLRRAIEAAAAALrdrRVRLRIHFVDSL-DPEALAAALRRLA-AGCDGVALVAPDHPLVRAAIDELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 105 KKGI---YLVNldekiDMDNLKKAggnveAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEA 181
Cdd:cd06307 81 ARGIpvvTLVS-----DLPGSRRL-----AYVGIDNRAAGRTAAWLMGRFLGRRPGKVLVILGSHRFRGHEEREAGFRSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 182 FK-KASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAmGVAQAVANAGKTGKVLVVGTDGIPEARKMVE 260
Cdd:cd06307 151 LReRFPDLTVLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNE-GIARALREAGRARRVVFIGHELTPETRRLLR 229
|
250 260
....*....|....*....|....*.
gi 446968931 261 AGQMTATVAQNPADIGATGLKLMVDA 286
Cdd:cd06307 230 DGTIDAVIDQDPELQARRAIEVLLAH 255
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
28-277 |
2.53e-26 |
|
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: 105.44 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd20003 3 AMIPKLVGVPYFTAAGQGAQEAAKELGVDV-TYDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDMD------NLkkagGNVEAFVTT--DNVAvgakgasfiiDKLGAEGgEVAIIEGKAGNASGEARRNGAT 179
Cdd:cd20003 82 IKVVTWDSDVNPDardffvNQ----ATPEGIGKTlvDMVA----------EQTGEKG-KVAIVTSSPTATNQNAWIKAMK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 180 EAFKKASQ-IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTdGIPEA-RK 257
Cdd:cd20003 147 AYIAEKYPdMKIVTTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTGKVAVTGL-STPNVmRP 225
|
250 260
....*....|....*....|
gi 446968931 258 MVEAGQMTATVAQNPADIGA 277
Cdd:cd20003 226 YVKDGTVKSVVLWDVVDLGY 245
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
28-304 |
2.66e-26 |
|
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: 104.52 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASpSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVmpVARAWKKG 107
Cdd:cd06267 3 GLIVPDISNPFFAELLRGIEDAARERGYSL-LLCN-TDEDPEREREYLRLLLSRRVDGIILAPSSLDDEL--LEELLAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDMDNLkkaggnveAFVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAFKKAsQ 187
Cdd:cd06267 79 IPVVLIDRRLDGLGV--------DSVVVDNYAGAYLATEHLIE-LGHR--RIAFIGGPLDLSTSRERLEGYRDALAEA-G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVAS--QPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVEAgq 263
Cdd:cd06267 147 LPVDPElvVEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRvpEDISVVGFDDIPLAALLTPP-- 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446968931 264 MTaTVAQNPADIGATGLKLMVDAEKSGKVIPLDKAPEFKLV 304
Cdd:cd06267 225 LT-TVRQPAYEMGRAAAELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
26-276 |
3.90e-26 |
|
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: 104.67 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 26 EYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPlSSVNLVMPV-ARAW 104
Cdd:cd20001 1 TIAVVVKVTGIAWFDRMETGVEQFAKDTGVNV-YQIGPATADAAQQVQIIEDLIAQGVDAICVVP-NDPEALEPVlKKAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 105 KKGIYLVNLDEKidmdNLKKAGGNVEAFvttDNVAVGAkgasFIIDKLGA---EGGEVAIIEGKAGNASGEARRNGATEA 181
Cdd:cd20001 79 DAGIVVITHEAS----NLKNVDYDVEAF---DNAAYGA----FIMDKLAEamgGKGKYVTFVGSLTSTSHMEWANAAVAY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 182 FKKA-SQIKLVASQPADWDRIK-ALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTdGIP-EARKM 258
Cdd:cd20001 148 QKANyPDMLLVTDRVETNDDSEtAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGKIAVVGT-GLPsVAGEY 226
|
250
....*....|....*...
gi 446968931 259 VEAGQMTATVAQNPADIG 276
Cdd:cd20001 227 LEDGTIDYIQFWDPADAG 244
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
28-285 |
3.83e-24 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 100.27 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVmpVARAWKKG 107
Cdd:COG1609 65 GVVVPDLSNPFFAELLRGIEEAARERGYQL--LLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDAR--LERLAEAG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDMDNLkkaggnveAFVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAFKKAsQ 187
Cdd:COG1609 141 IPVVLIDRPLPDPGV--------PSVGVDNRAGARLATEHLIE-LGHR--RIAFIGGPADSSSARERLAGYREALAEA-G 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVASQ--PADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVEAgq 263
Cdd:COG1609 209 LPPDPELvvEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRvpEDVSVVGFDDIPLARYLTPP-- 286
|
250 260
....*....|....*....|..
gi 446968931 264 MTaTVAQNPADIGATGLKLMVD 285
Cdd:COG1609 287 LT-TVRQPIEEMGRRAAELLLD 307
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
28-310 |
4.23e-21 |
|
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380649 [Multi-domain] Cd Length: 304 Bit Score: 91.15 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd19994 3 GISLPTKSEERWIKDGENLKSELEEAGYTVDLQYA--DDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIdMDnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAI-IEGKAGNASGEARR---NGATEAFK 183
Cdd:cd19994 81 IPVIAYDRLI-MN-----TDAVDYYVTFDNEKVGELQGQYLVDKLGLKDGKGPFnIELFAGSPDDNNAQlffKGAMEVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 184 --KASQIKLVASQP--------ADWDRIKALDVATNVLQRNP----NIKAIYCANDTMAMGVAQAVANAGKT--GKVLVV 247
Cdd:cd19994 155 pyIDDGTLVVRSGQttfeqvatPDWDTETAQARMETLLSAYYtggkKLDAVLSPNDGIARGVIEALKAAGYDtgPWPVVT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446968931 248 GTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLMVDAEKSGKVIPLDKAPEF---KLVDSILVT 310
Cdd:cd19994 235 GQDAEDASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVEVNDTKTYDngvKVVPSYLLD 300
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
27-272 |
5.96e-21 |
|
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: 89.98 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFAsPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKK 106
Cdd:cd06312 3 YVISHGSPSDPFWSVVKKGAKDAAKDLGVTVQYLG-PQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEKiDMDNLKKAGgnVEAFVTTDNVAVGAKGAsfiiDKLGAEGGEVA-IIEGKAGNASGEARRNGATEAFKKA 185
Cdd:cd06312 82 GIPVIAINSG-DDRSKERLG--ALTYVGQDEYLAGQAAG----ERALEAGPKNAlCVNHEPGNPGLEARCKGFADAFKGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 SqIKLVASQPADwDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMT 265
Cdd:cd06312 155 G-ILVELLDVGG-DPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKVKIGTFDLSPETLEAIKDGKIL 232
|
....*..
gi 446968931 266 ATVAQNP 272
Cdd:cd06312 233 FAIDQQP 239
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
29-294 |
6.20e-21 |
|
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: 89.91 E-value: 6.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKTLGVsvDIFASPSEGDFQSQLQLFEDLSNKNYKG-IAFAPLSSVNLVMPVARawkkG 107
Cdd:cd06284 4 VLVPNISNPFYSEILRGIEDAAAEAGY--DVLLGDTDSDPEREDDLLDMLRSRRVDGvILLSGRLDAELLSELSK----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkaGGNVeAFVTTDNVAVGAKGASFIIdKLGAEggEVAIIEGKAGNASGEARRNGATEAFKKASQ 187
Cdd:cd06284 78 YPIVQCCEYIP-------DSGV-PSVSIDNEAAAYDATEYLI-SLGHR--RIAHINGPLDNVYARERLEGYRRALAEAGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVA-SQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEArKMVEAgQM 264
Cdd:cd06284 147 PVDEDlIIEGDFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRvpEDVSVIGFDDIEFA-EMFSP-SL 224
|
250 260 270
....*....|....*....|....*....|
gi 446968931 265 TaTVAQNPADIGATGLKLMVDAEKSGKVIP 294
Cdd:cd06284 225 T-TIRQPRYEIGETAAELLLEKIEGEGVPP 253
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
28-294 |
1.27e-20 |
|
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: 89.24 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPSEgDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPvaRAWKKG 107
Cdd:cd06280 3 GLIVPDITNPFFTTIARGIEDAAEKHGYQV-ILANTDE-DPEKEKRYLDSLLSKQVDGIILAPSAGPSRELK--RLLKHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkagGNVEAFVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAFKKASq 187
Cdd:cd06280 79 IPIVLIDREVE--------GLELDLVAGDNREGAYKAVKHLIE-LGHR--RIGLITGPLEISTTRERLAGYREALAEAG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 IKLVAS--QPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGK--VLVVGTDGIPEArKMVEAgQ 263
Cdd:cd06280 147 IPVDESliFEGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPqdISVVGFDDSDWF-EIVDP-P 224
|
250 260 270
....*....|....*....|....*....|.
gi 446968931 264 MTAtVAQNPADIGATGLKLMVDAEKSGKVIP 294
Cdd:cd06280 225 LTV-VAQPAYEIGRIAAQLLLERIEGQGEEP 254
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
47-268 |
2.61e-20 |
|
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: 88.45 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 47 EDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIdmdnlkkAG 126
Cdd:cd19991 22 VKKAKELGAEVIVQSA--NGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLI-------LN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 127 GNVEAFVTTDNVAVGAKGASFIIDKlgAEGGEVAIIEGKAGNASGEARRNGATEAFK---KASQIKLVASQ-PADWDRIK 202
Cdd:cd19991 93 ADVDLYVSFDNEKVGELQAEALVKA--KPKGNYVLLGGSPTDNNAKLFREGQMKVLQpliDSGDIKVVGDQwVDDWDPEE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446968931 203 ALDVATNVLQRNPN-IKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATV 268
Cdd:cd19991 171 ALKIMENALTANNNkIDAVIASNDGTAGGAIQALAEQGLAGKVAVSGQDADLAACQRIVEGTQTMTI 237
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
28-310 |
1.11e-19 |
|
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: 86.71 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIfaSPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd01538 3 GVSLPNLREARWQTDRDIMVEQLEEKGAKVLV--QSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDKLGaeGGEVAIIEGKAGNASGEARRNGATEAFK---K 184
Cdd:cd01538 81 IKVIAYDRLIL-------NADVDYYISFDNEKVGELQAQALLDAKP--EGNYVLIGGSPTDNNAKLFRDGQMKVLQpaiD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 185 ASQIKLVASQPAD-WDRIKALDVATNVLQRNPN-IKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAG 262
Cdd:cd01538 152 SGKIKVVGDQWVDdWLPANAQQIMENALTANGNnVDAVVASNDGTAGGAIAALKAQGLSGGVPVSGQDADLAAIKRILAG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446968931 263 QMTATVAQNPADIGATGLKLMVDAEKSGKVIPLDKA-PEFKLVDSILVT 310
Cdd:cd01538 232 TQTMTVYKDIRLLADAAAEVAVALMRGEKPPINGTTnNGLKDVPSYLLE 280
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
34-294 |
1.58e-19 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380653 [Multi-domain] Cd Length: 302 Bit Score: 86.96 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 34 LSNPF----W-VDMKKGIEDEAKT--LGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKK 106
Cdd:cd19998 4 LSNSYsgndWrQEMINIAKAAAKQppYADKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEKIDMDNLKKaggnveafVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKAS 186
Cdd:cd19998 84 GIVVVAFDNVVDEPCAYN--------VNTDQAKAGEQTAQWLVDKLG-GKGNILMVRGVPGTSVDRDRYEGAKEVFKKYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 187 QIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTmaMGVAQAVANAGKtgKVLVVGTDGIPEARKMV---EAGQ 263
Cdd:cd19998 155 DIKVVAEYYGNWDDGTAQKAVADALAAHPDVDGVWTQGGE--TGVIKALQAAGH--PLVPVGGEAENGFRKAMlepLANG 230
|
250 260 270
....*....|....*....|....*....|.
gi 446968931 264 MTATVAQNPADIGATGLKLMVDAEKsGKVIP 294
Cdd:cd19998 231 LPGISAGSPPALSAVALKLAVAVLE-GEKEP 260
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
45-292 |
4.19e-18 |
|
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: 82.72 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 45 GIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDmdnlkk 124
Cdd:cd19995 21 GFEKAMKKLCPDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLIL------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 125 aGGNVEAFVTTDNVAVGAKGASFIIDKL---GAEGGEVAIIEGKAGNASGEARRNGATEAFKK---ASQIKLVASQPA-D 197
Cdd:cd19995 95 -GGPADYYVSFDNVAVGEAQAQSLVDHLkaiGKKGVNIVMINGSPTDNNAGLFKKGAHEVLDPlgdSGELKLVCEYDTpD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 198 WDRIKALDVATNVLQRNPN-IKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIG 276
Cdd:cd19995 174 WDPANAQTAMEQALTKLGNnIDGVLSANDGLAGGAIAALKAQGLAGKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEA 253
|
250
....*....|....*.
gi 446968931 277 ATGLKLMVDAEKSGKV 292
Cdd:cd19995 254 AAAAKVAVALLKGETP 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
27-311 |
5.33e-18 |
|
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: 82.29 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdifASPSEGDFQSQLQL--FEDLSNKNYKGIAFAPLSSVNLVMPVARAW 104
Cdd:cd06316 2 VAIAMHTTGSDWSRLQVAGIKDTFEELGIEV---VAVTDANFDPAKQItdLETLIALKPDIIISIPVDPVATAAAYKKVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 105 KKGIYLVNLDEKIDmdnLKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKK 184
Cdd:cd06316 79 DAGIKLVFMDNVPD---GLEAGKDYVSVVSSDNRGNGQIAAELLAEAIG-GKGKVGIIYHDADFYATNQRDKAFKDTLKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 185 AS-QIKLVASQPADwDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTgKVLVVGTD-GIPEARKMVEAG 262
Cdd:cd06316 155 KYpDIKIVAEQGFA-DPNDAEEVASAMLTANPDIDGIYVSWDTPALGVISALRAAGRS-DIKITTVDlGTEIALDMAKGG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446968931 263 QMTATVAQNPADIGATGLKLMVDAeKSGKvipldKAPEFKLVDSILVTQ 311
Cdd:cd06316 233 NVKGIGAQRPYDQGVAEALAAALA-LLGK-----EVPPFIGVPPLAVTK 275
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
64-286 |
1.59e-17 |
|
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: 81.22 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 64 SEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNlkkaggnvEAFVTTDNVAVGAK 143
Cdd:cd06300 42 SNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGAVTSPD--------AYNVSNDQVEWGRL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 144 GASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYcA 223
Cdd:cd06300 114 GAKWLFEALG-GKGNVLVVRGIAGAPASADRHAGVKEALAEYPGIKVVGEVFGGWDEATAQTAMLDFLATHPQVDGVW-T 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446968931 224 NDTMAMGVAQAVANAGKTgKVLVVG---TDGIPEARKMVEAGqMTATVAQNPADIGATGLKLMVDA 286
Cdd:cd06300 192 QGGEDTGVLQAFQQAGRP-PVPIVGgdeNGFAKQWWKHPKKG-LTGAAVWPPPAIGAAGLEVALRL 255
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
26-276 |
1.78e-17 |
|
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: 80.83 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 26 EYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFAsPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWK 105
Cdd:cd20002 1 TIVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVG-PADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKARE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 KGIYLVNLDEKidmdNLKKAGGNVEAFvttDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATE-AFKK 184
Cdd:cd20002 80 KGIVVITHESP----GQKGADWDVELI---DNEKFGEAQMELLAKEMG-GKGEYAIFVGSLTVPLHNLWADAAVEyQKEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 185 ASQIKLVASQ-PADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQ 263
Cdd:cd20002 152 YPNMKQVTDRiPGGEDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGLKGKVAVVGTVIPSQAAAYLKEGS 231
|
250
....*....|...
gi 446968931 264 MTATVAQNPADIG 276
Cdd:cd20002 232 ITEGYLWDPADAG 244
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-285 |
8.02e-17 |
|
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: 78.47 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASpSEGDFQSQLQLFEDLSNKNYKGIAFAPlssvnlVMPVARAWK-- 105
Cdd:cd06293 3 GLVVPDVSNPFFAEVARGVEDAARERGYAV-VLCN-SGRDPERERRYLEMLESQRVRGLIVTP------SDDDLSHLArl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 --KGIYLVNLDEKIDMDNLkkaggnveAFVTTDNVAvgakGASFIIDKLGAEGG-EVAIIEGKAGNASGEARRNGATEAF 182
Cdd:cd06293 75 raRGTAVVLLDRPAPGPAG--------CSVSVDDVQ----GGALAVDHLLELGHrRIAFVSGPLRTRQVAERLAGARAAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 183 KKA---SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARK 257
Cdd:cd06293 143 AEAgldPDEVVRELSAPDANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRvpDDVSVVGYDDLPFAAA 222
|
250 260
....*....|....*....|....*...
gi 446968931 258 MVEAgqMTaTVAQNPADIGATGLKLMVD 285
Cdd:cd06293 223 ANPP--LT-TVRQPSYELGRAAADLLLD 247
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
28-283 |
9.53e-17 |
|
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: 78.49 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKG 107
Cdd:cd06305 3 AVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDA--NGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDMDNLkkaggnveAFVTTDNVAVGAKGASFIIDKLGAEGGevaIIEGKAGNASGEARRNGATEAFKKAS- 186
Cdd:cd06305 81 IPVVTFDTDSQVPGV--------NNITQDDYALGTLSLGQLVKDLNGEGN---IAVFNVFGVPPLDKRYDIYKAVLKANp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 187 QIKLVASQPADWDRIKALDVATNV---LQRNPN--IKAIYCANDTMAMGVAQAVANAGKTgKVLVVGTDGIPEARKMV-- 259
Cdd:cd06305 150 GIKKIVAELGDVTPNTAADAQTQVealLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRT-DIKVYGVDISNQDLELMad 228
|
250 260
....*....|....*....|....
gi 446968931 260 EAGQMTATVAQNPADIGATGLKLM 283
Cdd:cd06305 229 EGSPWVATAAQDPALIGTVAVRNV 252
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
28-294 |
7.65e-16 |
|
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380514 [Multi-domain] Cd Length: 264 Bit Score: 75.63 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASpSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPvarawKKG 107
Cdd:cd06291 3 GLIVPDISNPFFAELAKYIEKELFKKGYKM-ILCN-SNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYK-----KLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDMDNlkkaggnveAFVTTDNVAVGAKGASFIIDKlGAEggEVAIIEGKAGNASGEARRNGATEAFKKA-- 185
Cdd:cd06291 76 IPIVSIDRYLSEGI---------PSVSSDNYQGGRLAAEHLIEK-GCK--KILHIGGPSNNSPANERYRGFEDALKEAgi 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 -SQIKLVASQPADWDRIKALdvATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPearkMVEAG 262
Cdd:cd06291 144 eYEIIEIDENDFSEEDAYEL--AKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRvpEDVQIIGFDGIE----ISELL 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 446968931 263 QMT-ATVAQNPADIGATGLKLMVD------AEKSGKVIP 294
Cdd:cd06291 218 YPElTTIRQPIEEMAKEAVELLLKliegeeIEESRIVLP 256
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
28-294 |
1.68e-15 |
|
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: 74.98 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSvdIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAwKKG 107
Cdd:cd19976 3 GLIVPDISNPFFSELVRGIEDTLNELGYN--IILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLLK-EEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkagGNVEAFVTTDNVAVGAKGASFIIdKLGAEggEVAIIEGKAGNASGEARrngaTEAFKKASQ 187
Cdd:cd19976 80 IPVVVLDRYIE--------DNDSDSVGVDDYRGGYEATKYLI-ELGHT--RIGCIVGPPSTYNEHER----IEGYKNALQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 188 iklVASQPADWDRIKALDV-------ATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKtgKV----LVVGTDGIPEAR 256
Cdd:cd19976 145 ---DHNLPIDESWIYSGESsleggykAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGL--KIpedlSVIGFDNIILSE 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446968931 257 KMVEAgqMTaTVAQNPADIGATGLKLMVD------AEKSGKVIP 294
Cdd:cd19976 220 YITPA--LT-TIAQPIFEMGQEAAKLLLKiiknpaKKKEEIVLP 260
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
35-272 |
1.20e-14 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380621 [Multi-domain] Cd Length: 278 Bit Score: 72.74 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 35 SNPFWVDMKKGIEDEAKTLGVSVDIfaSPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMP-VARAWKKGIyLVNL 113
Cdd:cd19966 11 GDPFWTVVYNGAKDAAADLGVDLDY--VFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTPlIEAAKKAGI-IVTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 114 DEKIDMDNLKKAGGnvEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEARRN-GATEAFKKAS-QIKLV 191
Cdd:cd19966 88 FNTDLPKLEYGDCG--LGYVGADLYAAGYTLAKELVKRGGLKTGDRVFVPGLLPGQPYRVLRTkGVIDALKEAGiKVDYL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 192 ASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAG-KTGKVLVVGTDGIPEARKMVEAGQMTATVAQ 270
Cdd:cd19966 166 EISLEPNKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGkKPGEIPVAGFDLSPATVQAIKSGYVNATIDQ 245
|
..
gi 446968931 271 NP 272
Cdd:cd19966 246 QP 247
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-285 |
1.40e-14 |
|
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: 72.18 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDlsnknYK--GIAFAplsSVNLVMPVARAW- 104
Cdd:cd06278 3 GVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDDALRQLLQ-----YRvdGVIVT---SATLSSELAEECa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 105 KKGIYLVnldekidMDNLKKAGGNVEAfVTTDNVAVGAKGASFIIDKlGAEggEVAIIEGKAGNASGEARRNGATEAFKK 184
Cdd:cd06278 75 RRGIPVV-------LFNRVVEDPGVDS-VSCDNRAGGRLAADLLLAA-GHR--RIAFLGGPEGTSTSRERERGFRAALAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 185 AsQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT---GKVLVVGTDGIPEARKmvEA 261
Cdd:cd06278 144 L-GLPPPAVEAGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGLvvpEDISVVGFDDIPMAAW--PS 220
|
250 260
....*....|....*....|....
gi 446968931 262 GQMTaTVAQNPADIGATGLKLMVD 285
Cdd:cd06278 221 YDLT-TVRQPIEEMAEAAVDLLLE 243
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
27-276 |
2.57e-14 |
|
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: 71.90 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKK 106
Cdd:cd20000 2 IAFLPKSLGNPYFDAARDGAKEAAKELGGEL-IFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEKIdmdnlkkAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEA-----RRNGATEA 181
Cdd:cd20000 81 GIKVVTFDSDV-------APEARDLFVNQADADGIGRAQVDMMAELIGGEGEFAILSATPTATNQNAwidamKKELASPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 182 FKKasqIKLVASQPADWDRIKALDVATNVLQRNPNIKAIyCANDTMAM-GVAQAVANAGKTGKVLVVGTdGIP-EARKMV 259
Cdd:cd20000 154 YAG---MKLVKVAYGDDDAQKSYQEAEALLQAYPDLKGI-IAPTTVGIaAAARALEDSGLKGKVKVTGL-GLPsEMAKYV 228
|
250
....*....|....*..
gi 446968931 260 EAGQMTATVAQNPADIG 276
Cdd:cd20000 229 KDGTVPAFALWNPIDLG 245
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
45-286 |
4.50e-14 |
|
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: 70.69 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 45 GIEDEAKTLGVSVDIfASPSEGDFQSQLQLFEDLSNKNYKGIAFapLSSVNLVMPVARAWKKGIYLVNLDEkidmdnlkk 124
Cdd:cd01574 20 GIERAARERGYSVSI-ATVDEDDPASVREALDRLLSQRVDGIIV--IAPDEAVLEALRRLPPGLPVVIVGS--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 125 AGGNVEAFVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAFKKASqIKLVASQPADWD----- 199
Cdd:cd01574 88 GPSPGVPTVSIDQEEGARLATRHLLE-LGHR--RIAHIAGPLDWVDARARLRGWREALEEAG-LPPPPVVEGDWSaasgy 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 200 RikaldvATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVEAgqMTaTVAQNPADIGA 277
Cdd:cd01574 164 R------AGRRLLDDGPVTAVFAANDQMALGALRALHERGLRvpEDVSVVGFDDIPEAAYFVPP--LT-TVRQDFAELGR 234
|
....*....
gi 446968931 278 TGLKLMVDA 286
Cdd:cd01574 235 RAVELLLAL 243
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
27-294 |
6.49e-14 |
|
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: 70.33 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVmpVARAWKK 106
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADT--GDDPERELAALDSLLSRRVDGLIITPARDDAPD--LQELAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEKIdmdnlkkaGGNVEAFVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAFKKAS 186
Cdd:cd06285 78 GVPVVLVDRRI--------GDTALPSVTVDNELGGRLATRHLLE-LGHR--RIAVVAGPLNASTGRDRLRGYRRALAEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 187 Q-IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAG-KTGKVL-VVGTDGIPEARKMVEAgq 263
Cdd:cd06285 147 LpVPDERIVPGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGlRVPEDLsVVGFDDIPLAAFLPPP-- 224
|
250 260 270
....*....|....*....|....*....|.
gi 446968931 264 MTaTVAQNPADIGATGLKLMVDAEKSGKVIP 294
Cdd:cd06285 225 LT-TVRQPKYEMGRRAAELLLQLIEGGGRPP 254
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
29-284 |
9.59e-13 |
|
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: 67.15 E-value: 9.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDfqSQLQLFEDLSNKNYKG--IAFAPLSSVNLVMPVArawKK 106
Cdd:pfam00532 6 ALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGED--TLTNAIDLLLASGADGiiITTPAPSGDDITAKAE---GY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEKIDMDNlkkaggNVEAfVTTDNVAVGAKGASFIIdKLGAEGGeVAIIEGKAgNASGEARRNGATEAFKKAS 186
Cdd:pfam00532 81 GIPVIAADDAFDNPD------GVPC-VMPDDTQAGYESTQYLI-AEGHKRP-IAVMAGPA-SALTARERVQGFMAALAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 187 ----QIKLVASqpADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGK--------TGKVLVVGTDGIPE 254
Cdd:pfam00532 151 grevKIYHVAT--GDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRvkipdivgIGINSVVGFDGLSK 228
|
250 260 270
....*....|....*....|....*....|.
gi 446968931 255 AR-KMVEagQMTATVAQNPADIGATGLKLMV 284
Cdd:pfam00532 229 AQdTGLY--LSPLTVIQLPRQLLGIKASDMV 257
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
26-310 |
9.62e-13 |
|
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: 67.32 E-value: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 26 EYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDfqSQLQLFEDLSNKNYKGIAFAP----LSSVNlvmpVA 101
Cdd:cd01540 1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGE--KVLSAIDNLIAQGAQGIVICTpdqkLGPAI----AA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 102 RAWKKGIYLVNLDekidmDNLKKAGGNVEA-FVTTDNVAVGAKGASFIIDKLGAEG----GEVAIIEGKAGNASGEARR- 175
Cdd:cd01540 75 KAKAAGIPVIAVD-----DQLVDADPMKIVpFVGIDAYKIGEAVGEWLAKEMKKRGwddvKEVGVLAITMDTLSVCVDRt 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 176 NGATEAFKKA----SQIKLVASQPADWDriKALDVATNVLQRNPNIK--AIYCANDTMAMGVAQAVANAGKTGK-VLVVG 248
Cdd:cd01540 150 DGAKDALKAAgfpeDQIFQAPYKGTDTE--GAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAGFDAEdIIGVG 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446968931 249 TDG----IPEARKmvEAGQMTATVAQNPADIGATGLKLMVDAEKSGKVIPLDkapefKLVDSILVT 310
Cdd:cd01540 228 IGGylaaDEEFKK--QPTGFKASLYISPDKHGYIAAEELYNWITDGKPPPAE-----TLTDGVIVT 286
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
29-285 |
2.53e-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: 380513 [Multi-domain] Cd Length: 267 Bit Score: 65.71 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASP--SEGDFQSQLQLFedLSNKNYKGIAFAPLSSVNLVmpvaRAWKK 106
Cdd:cd06290 4 VLVPDIDSPFYSEILNGIEEVLAESGYTL-IVSTShwNADRELEILRLL--LARKVDGIIVVGGFGDEELL----KLLAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEKIDMDNLkkaggnveAFVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAFKKA- 185
Cdd:cd06290 77 GIPVVLVDRELEGLNL--------PVVNVDNEQGGYNATNHLID-LGHR--RIVHISGPEDHPDAQERYAGYRRALEDAg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 --SQIKLVAsqPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVEA 261
Cdd:cd06290 146 leVDPRLIV--EGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRvpDDVSVIGFDDLPFSKYTTPP 223
|
250 260
....*....|....*....|....
gi 446968931 262 gqmTATVAQNPADIGATGLKLMVD 285
Cdd:cd06290 224 ---LTTVRQPLYEMGKTAAEILLE 244
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
34-251 |
4.38e-12 |
|
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: 65.39 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 34 LSNPFWVD-----MKKGIEDEAKTL---GVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWK 105
Cdd:cd19997 4 LSNSYAGNtwrqqMVDAFEEAAKKAkadGLIADYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 KGIYLVNLDEKIDMDNLKKaggnveafVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAFKKA 185
Cdd:cd19997 84 AGIKVVVFDSGVTEPCAYI--------LNNDFEDYGAASVEYVADRLG-GKGNVLEVRGVAGTSPDEEIYAGQVEALKKY 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446968931 186 SQIKLVASQPADWDRIKALDVATNVLQRNPNIKA-IYCANDtmAMGVAQAVANAGKTGKVLVVGTDG 251
Cdd:cd19997 155 PDLKVVAEVYGNWTQSVAQKAVTGILPSLPEVDAvITQGGD--GYGAAQAFEAAGRPLPIIIGGNRG 219
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
142-306 |
1.60e-11 |
|
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: 63.93 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 142 AKGASFIIDKLGA---EGGEVAIIEGKAGNASgEARRNGATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIK 218
Cdd:cd06303 142 AEGSRMLAKHFIKifpEEGKYAILYLTEGYVS-DQRGDTFIDEVARHSNLELVSAYYTDFDRESAREAARALLARHPDLD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 219 AIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIG---ATGLKLmvDAEksGKVIPL 295
Cdd:cd06303 221 FIYACSTDIALGAIDALQELGRETDIMINGWGGGSAELDALQKGGLDVTVMRMNDDNGiamAEAIKL--DLE--GREVPT 296
|
170
....*....|.
gi 446968931 296 DKAPEFKLVDS 306
Cdd:cd06303 297 VYAGDFELVTK 307
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
28-305 |
7.53e-11 |
|
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: 61.42 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQ-SQLQLFEDlsnKNYKGIAFAplSSV----------NL 96
Cdd:cd19975 3 GVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREkKYLQLLKE---KRVDGIIFA--SGTlteenkqllkNM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 97 VMPVarawkkgiylVNLDEKIDMDNLkkaggnveAFVTTDNVAVGAKGASFIIdKLGAEggEVAIIEGKAGNA-SGEARR 175
Cdd:cd19975 78 NIPV----------VLVSTESEDPDI--------PSVKIDDYQAAYDATNYLI-KKGHR--KIAMISGPLDDPnAGYPRY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 176 NGateaFKKASQ-----IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVG 248
Cdd:cd19975 137 EG----YKKALKdaglpIKENLIVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRvpEDISVIG 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446968931 249 TDGIPEArkmveagQMT----ATVAQNPADIGATGLKLMVDAEKSGKVIPLDKAPEFKLVD 305
Cdd:cd19975 213 FDNTEIA-------EMSipplTTVSQPFYEMGKKAVELLLDLIKNEKKEEKSIVLPHQIIE 266
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
42-292 |
1.01e-10 |
|
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: 61.34 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 42 MKKGIEDeaktLGVSVdiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDN 121
Cdd:cd19993 21 MKKALEK----AGAKY--ISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDRLIENPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 122 LkkaggnveAFVTTDNVAVGAKGASFIIDKLGAegGEVAIIEGKAGNASGEARRNGATEAFKKA---SQIKLVASQPAD- 197
Cdd:cd19993 95 A--------FYISFDNVEVGRMQARGVLKAKPE--GNYVFIKGSPTDPNADFLRAGQMEVLQPAidsGKIKIVGEQYTDg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 198 WDRIKALDVATNVLQRNPN-IKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIG 276
Cdd:cd19993 165 WKPANAQKNMEQILTANNNkVDAVVASNDGTAGGAVAALAAQGLAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELG 244
|
250
....*....|....*.
gi 446968931 277 ATGLKLMVDAEKSGKV 292
Cdd:cd19993 245 KEAAEIAVELAKGTKI 260
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
28-285 |
1.78e-10 |
|
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: 60.27 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPL--SSVNLVmpvARAWK 105
Cdd:cd06289 3 GLIVPDLSNPFFAELLAGIEEALEEAGYLV--FLANTGEDPERQRRFLRRMLEQGVDGLILSPAagTTAELL---RRLKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 KGIYLVNLDEKIDMDNLKkaggnveaFVTTDNVAVGAKGASFIIDkLGAegGEVAIIEGKAGNASGEARRNGATEAFKKA 185
Cdd:cd06289 78 WGIPVVLALRDVPGSDLD--------YVGIDNRLGAQLATEHLIA-LGH--RRIAFLGGLSDSSTRRERLAGFRAALAEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 SQI---KLVASQPADwdRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT-GK-VLVVGTDGIPEARKMVE 260
Cdd:cd06289 147 GLPldeSLIVPGPAT--REAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEpGRdIAVVGFDDVPEAALWTP 224
|
250 260
....*....|....*....|....*
gi 446968931 261 AgqMTaTVAQNPADIGATGLKLMVD 285
Cdd:cd06289 225 P--LT-TVSVHPREIGRRAARLLLR 246
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
29-294 |
2.60e-10 |
|
Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.
Pssm-ID: 380479 [Multi-domain] Cd Length: 265 Bit Score: 59.95 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKTLGVSVdiFASPSEGDFQSQLQLFEDLSNKNYKGIAfaplssVNLVMPVArawkkgi 108
Cdd:cd01537 4 VTIYSYDDNFMSVIRKAIEQDAKQPGVQL--LMNDSQNDQEKQNDQIDVLLAKRVKGLA------INLVDPAA------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 109 ylvnldekiDMDNLKKAGGNVEAFV---------TTDNVAVGAKGASFIIDKLGAEGG--EVAIIEGKAGNASGEARRNG 177
Cdd:cd01537 69 ---------AGVAEKARGQNVPVVFfdkepsrydKAYYVITDSKEGGIIQGDLLAKHGhiQIVLLKGPLGHPDAEARLAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 178 ATEAFKKAsQIKLVASQ--PADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIP 253
Cdd:cd01537 140 VIKELNDK-GIKTEQLQldTGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRvpSDISVFGYDALP 218
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446968931 254 EARKmveAGQMTATVAQNPADIGATGLKLMVDAEKSGKVIP 294
Cdd:cd01537 219 EALK---SGPLLTTILQDANNLGKTTFDLLLNLADNWKIDN 256
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
48-275 |
3.29e-10 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 60.14 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 48 DEAKTLGVSVdiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDmdnlkkaGG 127
Cdd:PRK10355 49 KKAESLGAKV--FVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMIN-------NA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 128 NVEAFVTTDNVAVGAKGASFIIDKLgaEGGEVAIIEGKAGNASGEARRNGATEAFK---KASQIKLVASQPAD-WDRIKA 203
Cdd:PRK10355 120 DIDFYISFDNEKVGELQAKALVDKV--PQGNYFLMGGSPVDNNAKLFRAGQMKVLKpyiDSGKIKVVGDQWVDgWLPENA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 204 LDVATNVLQRNPN-IKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATV-------AQNPADI 275
Cdd:PRK10355 198 LKIMENALTANNNkIDAVVASNDATAGGAIQALSAQGLSGKVAISGQDADLAAIKRIVAGTQTMTVykpitklANTAAEI 277
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
29-285 |
4.08e-10 |
|
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: 59.08 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASpSEGDFQSQLQLFEDLSNKNYKGIAFAP-LSSVNLVMPVArawKKG 107
Cdd:cd19977 4 LIVADILNPFFTSVVRGIEDEAYKNGYHV-ILCN-TDEDPEKEKKYIEMLRAKQVDGIIIAPtGGNEDLIEKLV---KSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDmdnlkkaggNVEA-FVTTDNVAVGAKGASFIIDKlGAEggEVAIIEGKAGNASGEARRNGATEAFKKAS 186
Cdd:cd19977 79 IPVVFVDRYIP---------GLDVdTVVVDNFKGAYQATEHLIEL-GHK--RIAFITYPLELSTRQERLEGYKAALADHG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 187 QI---KLVASqpadWDRIKALDVAT-NVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVE 260
Cdd:cd19977 147 LPvdeELIKH----VDRQDDVRKAIsELLKLEKPPDAIFAANNLITLEVLKAIKELGLRipDDIALIGFDDIPWADLFNP 222
|
250 260
....*....|....*....|....*
gi 446968931 261 AgqMTaTVAQNPADIGATGLKLMVD 285
Cdd:cd19977 223 P--LT-VIAQPTYEIGRKAAELLLD 244
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
35-304 |
7.80e-10 |
|
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380511 [Multi-domain] Cd Length: 268 Bit Score: 58.33 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 35 SNPFWVDMKKGIEDEAKTLGVSVdiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLD 114
Cdd:cd06288 11 TTPFAGDIIRGAQDAAEEHGYLL--LLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLPPELTDIPLVLLNCFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 115 EKIDMdnlkkaggnveAFVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAFKKAsQIKLVAS- 193
Cdd:cd06288 89 DDPSL-----------PSVVPDDEQGGYLATRHLIE-AGHR--RIAFIGGPEDSLATRLRLAGYRAALAEA-GIPYDPSl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 194 -QPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAG-KTGK-VLVVGTDGIPEARKMVEAgqMTaTVAQ 270
Cdd:cd06288 154 vVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGlRVPEdLSVVGFDNQELAAYLRPP--LT-TVAL 230
|
250 260 270
....*....|....*....|....*....|....
gi 446968931 271 NPADIGATGLKLMVDAEKSGKVIPLDKAPEFKLV 304
Cdd:cd06288 231 PYYEMGRRAAELLLDGIEGEPPEPGVIRVPCPLI 264
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
131-286 |
1.36e-09 |
|
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: 57.66 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 131 AFVTTDnvavGAKGASFIIDKLGAEGGE-VAIIEGKAGNASGEARRNGATEAFKKASqiklvASQPADWDRIKALDV--- 206
Cdd:cd06292 98 PWVDVD----GAAGMRQAVRHLIALGHRrIGLIGGPEGSVPSDDRLAGYRAALEEAG-----LPFDPGLVVEGENTEegg 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 207 ---ATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVEAgqMTaTVAQNPADIGATGLK 281
Cdd:cd06292 169 yaaAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRvgRDVSVVGFDDSPLAAFTHPP--LT-TVRQPIDEIGRAVVD 245
|
....*
gi 446968931 282 LMVDA 286
Cdd:cd06292 246 LLLAA 250
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
114-277 |
3.07e-09 |
|
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: 56.79 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 114 DEKIDMdnLKKAG------GNVE-----AFVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAF 182
Cdd:cd20010 72 DPRIAY--LLERGipfvvhGRSEsgapyAWVDIDNEGAFRRATRRLLA-LGHR--RIALLNGPEELNFAHQRRDGYRAAL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 183 KKAS-QIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT-GK-VLVVGTDGIPEArkMV 259
Cdd:cd20010 147 AEAGlPVDPALVREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSpGKdVSVIGHDDLLPA--LE 224
|
170
....*....|....*...
gi 446968931 260 EAGQMTATVAQNPADIGA 277
Cdd:cd20010 225 YFSPPLTTTRSSLRDAGR 242
|
|
| PRK15408 |
PRK15408 |
autoinducer 2 ABC transporter substrate-binding protein LsrB; |
8-270 |
4.65e-09 |
|
autoinducer 2 ABC transporter substrate-binding protein LsrB;
Pssm-ID: 237961 Cd Length: 336 Bit Score: 56.73 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 8 FSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDiFASPSEGDFQSQLQLFEDLSNKNYKGIA 87
Cdd:PRK15408 7 LVSALGIALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVT-YDGPTEPSVSGQVQLINNFVNQGYNAII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 88 FAPLSSVNLVMPVARAWKKGIYLVNLDEKIdmdnlkkaggNVEAFVTTDNVAVGAKGASFIID----KLGAEGGEVAIIE 163
Cdd:PRK15408 86 VSAVSPDGLCPALKRAMQRGVKVLTWDSDT----------KPECRSYYINQGTPEQLGSMLVEmaakQVGKDKAKVAFFY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 164 GKAGNASGEARRNGATEAFKKA-SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAgKTG 242
Cdd:PRK15408 156 SSPTVTDQNQWVKEAKAKIAKEhPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENL-KRD 234
|
250 260
....*....|....*....|....*...
gi 446968931 243 KVLVVGTDGIPEARKMVEAGqmtaTVAQ 270
Cdd:PRK15408 235 KVAIVGFSTPNVMRPYVKRG----TVKE 258
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
126-286 |
5.93e-09 |
|
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: 55.72 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 126 GGNVEAFVTTDNVAVGAKGASFIIDkLGAEggEVAIIeGKAGNASGEARRNGATEAFKKAS-QIKLVASQPADWDRIKAL 204
Cdd:cd06295 97 DGQSYCSVGSDNVKGGALATEHLIE-IGRR--RIAFL-GDPPHPEVADRLQGYRDALAEAGlEADPSLLLSCDFTEESGY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 205 DVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVEAgqMTaTVAQNPADIGatglKL 282
Cdd:cd06295 173 AAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISvpGDVAVVGYDDIPLAAYFRPP--LT-TVRQDLALAG----RL 245
|
....
gi 446968931 283 MVDA 286
Cdd:cd06295 246 LVEK 249
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
29-285 |
6.22e-09 |
|
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: 55.75 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPSEgDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMpvARAWKKGI 108
Cdd:cd06299 4 LLVPDIRNPFFAELASGIEDEARAHGYSV-ILGNSDE-DPEREDESLEMLLSQRVDGIIAVPTGENSEGL--QALIAQGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 109 YLVNLDEKIDmdnlkkAGGNVEAfVTTDNVavgaKGASFIIDKLGAEGGE-VAIIEGKAGNASGEAR----RNGATEAFK 183
Cdd:cd06299 80 PVVFVDREVE------GLGGVPV-VTSDNR----PGAREAVEYLVSLGHRrIGYISGPLSTSTGRERlaafRAALTAAGI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 184 KASQIkLVASQPADWDriKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAG-KTGK-VLVVGTDGIPEARKMveA 261
Cdd:cd06299 149 PIDEE-LVAFGDFRQD--SGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGlRIGDdVSLISFDDVPWFELL--S 223
|
250 260
....*....|....*....|....
gi 446968931 262 GQMTAtVAQNPADIGATGLKLMVD 285
Cdd:cd06299 224 PPLTV-IAQPVERIGRRAVELLLA 246
|
|
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
2-268 |
4.75e-08 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 53.58 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 2 NKYLKYFSGTLVGLMLSTSAFAAA-EYAVVLKTLSNPFWVDMKKGIEDEAKTLGvSVDIFASPSEGDFQSQLQLFEDLSN 80
Cdd:PRK15395 1 NKKVLTLSALMASMLFGAAAAAADtRIGVTIYKYDDNFMSVVRKAIEKDAKAAP-DVQLLMNDSQNDQSKQNDQIDVLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 81 KNYKGIAfaplssVNLVMPVA------RAWKKGIYLVNLDE---KIDMDNLKKAggnveAFVTTDNVAVGAKGASFIIDK 151
Cdd:PRK15395 80 KGVKALA------INLVDPAAaptvieKARGQDVPVVFFNKepsRKALDSYDKA-----YYVGTDSKESGIIQGDLIAKH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 152 LGAEGG---------EVAIIEGKAGNASGEARRNGATEAF-KKASQIKLVASQPADWDRIKALDVATNVLQrNPN---IK 218
Cdd:PRK15395 149 WKANPAwdlnkdgkiQYVLLKGEPGHPDAEARTTYVIKELnDKGIKTEQLQLDTAMWDTAQAKDKMDAWLS-GPNankIE 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446968931 219 AIYCANDTMAMGVAQAVANAGKTgKVLVVGTDGIPEARKMVEAGQMTATV 268
Cdd:PRK15395 228 VVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEALALVKSGAMAGTV 276
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
35-286 |
1.92e-07 |
|
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: 51.49 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 35 SNPFWVDMKKGIEDEAKTLGVSVdiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKgIYLVNLD 114
Cdd:cd06275 10 ENPFFAEVVRGVEDACFRAGYSL--ILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAALRS-IPVVVLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 115 EKIdmdnlkkAGGNVEAfVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAFKKASqIKLVAS- 193
Cdd:cd06275 87 REI-------AGDNADA-VLDDSFQGGYLATRHLIE-LGHR--RIGCITGPLEHSVSRERLAGFRRALAEAG-IEVPPSw 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 194 -QPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAG-KTGK-VLVVGTDGIPEARKMVEAgqMTaTVAQ 270
Cdd:cd06275 155 iVEGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGlRVPQdISIIGYDDIELARYFSPA--LT-TIHQ 231
|
250
....*....|....*.
gi 446968931 271 NPADIGATGLKLMVDA 286
Cdd:cd06275 232 PKDELGELAVELLLDR 247
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
29-285 |
2.97e-07 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 50.74 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKTLGVSvdIFASPSEGDFQSQLQLFEDLSNKNYKGiafaplssvnLVMPVARAwKKGI 108
Cdd:cd06282 4 VLIPSLNNPVFAEAAQGIQRAARAAGYS--LLIATTDYDPARELDAVETLLEQRVDG----------LILTVGDA-QGSE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 109 YLVNLDEK----IDMDNlkKAGGNVEAFVTTDNVAVGAKGASFIIdKLGAEggEVAIIEGKAgNASGEAR------RNGA 178
Cdd:cd06282 71 ALELLEEEgvpyVLLFN--QTENSSHPFVSVDNRLASYDVAEYLI-ALGHR--RIAMVAGDF-SASDRARlryqgyRDAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 179 TEAFKKASQIKLVASQPADWDrikalDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIpear 256
Cdd:cd06282 145 KEAGLKPIPIVEVDFPTNGLE-----EALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRvpDDVSVIGFDGI---- 215
|
250 260 270
....*....|....*....|....*....|...
gi 446968931 257 kmvEAGQMT----ATVAQNPADIGATGLKLMVD 285
Cdd:cd06282 216 ---AIGELLtptlATVVQPSRDMGRAAADLLLA 245
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
30-283 |
5.69e-07 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 50.48 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 30 VLKTLSNPFWVDMKKGI----EDEAKTLgvsvdiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVmPVARAWK 105
Cdd:PRK10014 70 IVRDLSAPFYAELTAGLtealEAQGRMV------FLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDD-LREMAEE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 KGIYLV-----NLDEKIDmdnlkkaggnveaFVTTDNVAVGAKGASFIIdKLGAEggEVAIIEGKAGNASgEARRNGATE 180
Cdd:PRK10014 143 KGIPVVfasraSYLDDVD-------------TVRPDNMQAAQLLTEHLI-RNGHQ--RIAWLGGQSSSLT-RAERVGGYC 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 181 A--------FKKASQIKLVASQPAdwdrikALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT-GK-------- 243
Cdd:PRK10014 206 AtllkfglpFHSEWVLECTSSQKQ------AAEAITALLRHNPTISAVVCYNETIAMGAWFGLLRAGRQsGEsgvdryfe 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446968931 244 --VLVVGTDGIPEArkmvEAGQMTATVAQNPA-DIGAT-GLKLM 283
Cdd:PRK10014 280 qqVALAAFTDVPEA----ELDDPPLTWASTPArEIGRTlADRMM 319
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
158-304 |
1.20e-06 |
|
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: 49.09 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 158 EVAIIEGKAGNASGEARRNGATEAFKkASQIKLVAS--QPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAV 235
Cdd:cd01545 120 RIGFIAGPPDHGASAERLEGFRDALA-EAGLPLDPDlvVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAA 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446968931 236 ANAGKT--GKVLVVGTDGIPEARKMVEAgqMTaTVAQNPADIGATGLKLMVDAEKSGKVIPLDKAPEFKLV 304
Cdd:cd01545 199 HRLGLRvpDDLSVAGFDDSPIARLVWPP--LT-TVRQPIAEMARRAVELLIAAIRGAPAGPERETLPHELV 266
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
28-293 |
1.52e-06 |
|
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: 48.81 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLqlFEDLSNKNYKG--IAFAPLSSVNLvmpvARAWK 105
Cdd:cd06296 3 DLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDW--VRRAVARGSAGvvLVTSDPTSRQL----RLLRS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 KGIYLVNLDEKIDMDnlkkagGNVEAfVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAFKKA 185
Cdd:cd06296 77 AGIPFVLIDPVGEPD------PDLPS-VGATNWAGGRLATEHLLD-LGHR--RIAVITGPPRSVSGRARLAGYRAALAEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 186 SqiklVASQPA-----DWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKM 258
Cdd:cd06296 147 G----IAVDPDlvregDFTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRvpDDLSVIGFDDTPPARWT 222
|
250 260 270
....*....|....*....|....*....|....*
gi 446968931 259 veAGQMTaTVAQNPADIGATGLKLMVDAEKSGKVI 293
Cdd:cd06296 223 --SPPLT-TVHQPLREMGAVAVRLLLRLLEGGPPD 254
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
162-285 |
2.26e-06 |
|
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: 46.95 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 162 IEGKAGNASGEARRNGATEAFKKAsQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT 241
Cdd:pfam13377 15 PEGDRDDPYSDLRERGFREAAREL-GLDVEPTLYAGDDEAEAAAARERLRWLGALPTAVFVANDEVALGVLQALREAGLR 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446968931 242 --GKVLVVGTDGIPEARKMVEAgqMTaTVAQNPADIGATGLKLMVD 285
Cdd:pfam13377 94 vpEDLSVIGFDDSPLAALVSPP--LT-TVRVDAEELGRAAAELLLD 136
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
28-285 |
4.55e-06 |
|
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380506 [Multi-domain] Cd Length: 266 Bit Score: 47.16 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 28 AVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASpSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAwkKG 107
Cdd:cd06283 3 GVIVADITNPFSSLLLKGIEDVCREAGYQL-LICN-SNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQ--KG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 108 IYLVNLDEKIDMDNLkkaggnveAFVTTDNVAvgakgASF-IIDKLGAEGGE-VAII-EGKAGNASGEARRNGATEAFKK 184
Cdd:cd06283 79 LPVVLVDRQIEPLNW--------DTVVTDNYD-----ATYeATEHLKEQGYErIVFVtEPIKGISTRRERLQGFLDALAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 185 AS-QIKLVASQPADWDRIKAlDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGktgkvLVVGTD-GI-----PEARK 257
Cdd:cd06283 146 YNiEGDVYVIEIEDTEDLQQ-ALAAFLSQHDGGKTAIFAANGVVLLRVLRALKALG-----IRIPDDvGLcgfddWDWAD 219
|
250 260
....*....|....*....|....*...
gi 446968931 258 MVEAGqMTaTVAQNPADIGATGLKLMVD 285
Cdd:cd06283 220 LIGPG-IT-TIRQPTYEIGKAAAEILLE 245
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
29-300 |
7.62e-06 |
|
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: 46.69 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 29 VVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEgdfqSQLQLFEDLSNKNYK--GIAFAPLSSVNLVMPVARAWKK 106
Cdd:cd06297 4 LLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSE----YRLEKYLRNSTLAYQcdGLVMASLDLTELFEEVIVPTEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 107 GIYLVNLDEK-IDmdnlkkaggnveaFVTTDNVAvGAKGASFIIDKLGaeGGEVAII----EGKAGNASGEARRNGATEA 181
Cdd:cd06297 80 PVVLIDANSMgYD-------------CVYVDNVK-GGFMATEYLAGLG--EREYVFFgieeDTVFTETVFREREQGFLEA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 182 FKKASQ-IKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT-GK-VLVVGTDGIPEArkm 258
Cdd:cd06297 144 LNKAGRpISSSRMFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRvGEdVAVIGFDGQPWA--- 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446968931 259 vEAGQMTaTVAQNPADIGATGLKLMVD--AEKSGKVIPLDKAPE 300
Cdd:cd06297 221 -ASPGLT-TVRQPVEEMGEAAAKLLLKrlNEYGGPPRSLKFEPE 262
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
133-256 |
1.26e-05 |
|
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: 45.97 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 133 VTTDNVAVGAKGASFIIDkLGAEggEVAIIEGKAGNASGEARRNGATEAFKKAS-QIKLVASQPADWDRIKALDVATNVL 211
Cdd:cd06270 96 VWLDNEQGGRLAAEHLLD-LGHR--RIACITGPLDIPDARERLAGYRDALAEAGiPLDPSLIIEGDFTIEGGYAAAKQLL 172
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446968931 212 QRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEAR 256
Cdd:cd06270 173 ARGLPFTALFAYNDDMAIGALAALHEAGIKvpEDVSVIGFDDVPLAR 219
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
175-287 |
1.90e-05 |
|
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: 45.28 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 175 RNGATEAFKKASQIKLVASqpADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGI 252
Cdd:cd06279 156 RDALEEAGLDLDDVPVVEA--PGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRvpEDLSVTGFDDI 233
|
90 100 110
....*....|....*....|....*....|....*
gi 446968931 253 PEARKmveAGQMTATVAQNPADIGATGLKLMVDAE 287
Cdd:cd06279 234 PEAAA---ADPGLTTVRQPAVEKGRAAARLLLGLL 265
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
34-295 |
2.60e-05 |
|
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380486 [Multi-domain] Cd Length: 269 Bit Score: 44.82 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 34 LSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQL--------FEDLSNKNYKGIafaplsSVNLVmpvarawk 105
Cdd:cd01544 14 LEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLESLLEKVdgiiaigkFSKEEIEKLKKL------NPNIV-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 106 kGIYLVNLDEKIDMdnlkkaggnveafVTTDnvavGAKGASFIIDKLGAEG-GEVAIIegkAGNASGEARRNGATE---- 180
Cdd:cd01544 80 -FVDSNPDPDGFDS-------------VVPD----FEQAVRQALDYLIELGhRRIGFI---GGKEYTSDDGEEIEDprlr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 181 AFKKASQIKLVASQP----ADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPE 254
Cdd:cd01544 139 AFREYMKEKGLYNEEyiyiGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKvpEDISIISFNDIEV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446968931 255 ARkmveagQMT---ATVAQNPADIGATGLKLMVDAEKSGKVIPL 295
Cdd:cd01544 219 AK------YVTpplTTVHIPTEEMGRTAVRLLLERINGGRTIPK 256
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
169-256 |
5.23e-05 |
|
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380484 [Multi-domain] Cd Length: 259 Bit Score: 44.02 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 169 ASGEARRNGATEAFKKASQIKLVASQpADWDRIKALDVATNVLQRNPnIKAIYCANDTMAMGVAQAVANAGKT--GKVLV 246
Cdd:cd01542 128 AVGVARKQGYLDALKEHGIDEVEIVE-TDFSMESGYEAAKELLKENK-PDAIICATDNIALGAIKALRELGIKipEDISV 205
|
90
....*....|
gi 446968931 247 VGTDGIPEAR 256
Cdd:cd01542 206 AGFGGYDLSE 215
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
44-293 |
5.92e-05 |
|
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: 43.70 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 44 KGIEDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVnLVMP----VARAWKKGIYLVNLDEKIDM 119
Cdd:cd01541 19 QGIESVLSENGYSLLLALT--NNDVEKEREILESLLDQNVDGLIIEPTKSA-LPNPnldlYEELQKKGIPVVFINSYYPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 120 DNLkkaggnveAFVTTDNVAVGAKGASFIIDKlgaegG--EVAIIEgKAGNASGEARRNGATEAFKKASQI----KLVAS 193
Cdd:cd01541 96 LDA--------PSVSLDDEKGGYLATKHLIDL-----GhrRIAGIF-KSDDLQGVERYQGFIKALREAGLPidddRILWY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 194 QPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVEagQMTaTVAQN 271
Cdd:cd01541 162 STEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRvpEDLSVVGFDDSYLASLSEP--PLT-SVVHP 238
|
250 260
....*....|....*....|....*.
gi 446968931 272 PADIGATG----LKLMVDAEKSGKVI 293
Cdd:cd01541 239 KEELGRKAaellLRMIEEGRKPESVI 264
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
136-304 |
1.21e-04 |
|
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: 42.87 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 136 DNVAVGAKGASFIIDK-------LGAEGGevaiiegkaGNASGEARRNGATEAFKKA---SQIKLVASQPADwdrIKALD 205
Cdd:cd01575 99 SNFAAGRAMARHLIERgyrriafVGARLD---------GDSRARQRLEGFRDALAEAglpLPLVLLVELPSS---FALGR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 206 VATN-VLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVeaGQMTaTVAQNPADIGATG--- 279
Cdd:cd01575 167 EALAeLLARHPDLDAIFCSNDDLALGALFECQRRGIRvpGDIAIAGFGDLDIAAALP--PALT-TVRVPRYEIGRKAael 243
|
170 180
....*....|....*....|....*.
gi 446968931 280 -LKLMVDAEKSGKVIPLDkapeFKLV 304
Cdd:cd01575 244 lLARLEGEEPEPRVVDLG----FELV 265
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
132-294 |
1.30e-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: 380497 [Multi-domain] Cd Length: 268 Bit Score: 42.88 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 132 FVTTDNVAVGAKGASFIIDkLGAEggEVAIIEGK-AGNASGEARRNGATEAFKKASQI---KLVASQPADWDRIKALdvA 207
Cdd:cd06273 95 SIGFDNRAAAARAAQHLLD-LGHR--RIAVISGPtAGNDRARARLAGIRDALAERGLElpeERVVEAPYSIEEGREA--L 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 208 TNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEARKMVEAgqMTaTVAQNPADIGATGLKLMVD 285
Cdd:cd06273 170 RRLLARPPRPTAIICGNDVLALGALAECRRLGISvpEDLSITGFDDLELAAHLSPP--LT-TVRVPAREIGELAARYLLA 246
|
....*....
gi 446968931 286 AEKSGKVIP 294
Cdd:cd06273 247 LLEGGPPPK 255
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
158-286 |
5.45e-04 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 41.13 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 158 EVAIIEGKAGNASGEARRNGATEAFKKAsQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVAN 237
Cdd:PRK09526 183 RIALLAGPESSVSARLRLAGWLEYLTDY-QLQPIAVREGDWSAMSGYQQTLQMLREGPVPSAILVANDQMALGVLRALHE 261
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446968931 238 AGKT--GKVLVVGTDGIPEARKMVEAgqMTaTVAQNPADIGATGLKLMVDA 286
Cdd:PRK09526 262 SGLRvpGQISVIGYDDTEDSSYFIPP--LT-TIKQDFRLLGKEAVDRLLAL 309
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
38-249 |
6.21e-04 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 41.09 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 38 FWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSvNLVMPVARAWKKGIYLVNLDEKI 117
Cdd:PRK10936 60 YWLSVNYGMVEEAKRLGVDLKVLEAGGYYNLAKQQQQLEQCVAWGADAILLGAVTP-DGLNPDLELQAANIPVIALVNGI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 118 DMDNlkkaggnVEAFVTTDNVAVGAKGASFIIDKLGAEGGE--VAIIEGKAGNASGEARRNGATEAFKKaSQIKLVASQP 195
Cdd:PRK10936 139 DSPQ-------VTTRVGVSWYQMGYQAGRYLAQWHPKGSKPlnVALLPGPEGAGGSKAVEQGFRAAIAG-SDVRIVDIAY 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446968931 196 ADWDRIKALDVATNVLQRNPNIKaiYCANDTMAMGVAQA-VANAGKTGKVLVVGT 249
Cdd:PRK10936 211 GDNDKELQRNLLQELLERHPDID--YIAGSAVAAEAAIGeLRGRNLTDKIKLVSF 263
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
141-304 |
4.17e-03 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 38.17 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 141 GAKGASFIIDKLGAEGG-EVAIIegkagnaSGEARRNGATEAFKKASQI-------KLVASQPADWDRIKALDVATNVLQ 212
Cdd:cd06287 102 SAATARLLLEHLHGAGArQVALL-------TGSSRRNSSLESEAAYLRFaqeygttPVVYKVPESEGERAGYEAAAALLA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446968931 213 RNPNIKAIYCANDTMAMGVAQAVANAGKT---GKVLVVGTDGIpeaRKMVEAGQMTAtVAQNPADIGATGLKLMVdAEKS 289
Cdd:cd06287 175 AHPDIDAVCVPVDAFAVGAMRAARDSGRSvpeDLMVVTRYDGI---RARTADPPLTA-VDLHLDRVARTAIDLLF-ASLS 249
|
170
....*....|....*
gi 446968931 290 GKVIPLDKAPEFKLV 304
Cdd:cd06287 250 GEERSVEVGPAPELV 264
|
|
| |
