|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-295 |
0e+00 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 572.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 1 MNMKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTV 80
Cdd:PRK10653 1 MNMKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 81 RGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGT 160
Cdd:PRK10653 81 RGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIAKKLGEGAKVIQLEGIAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 161 SAARERGEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFD 240
Cdd:PRK10653 161 SAARERGEGFKQAVAAHKFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 732686642 241 GTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 295
Cdd:PRK10653 241 GTPDGIKAVNRGKLAATIAQQPDQIGAIGVETADKVLKGEKVEAKIPVDLKLVTK 295
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
28-294 |
6.40e-145 |
|
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: 407.84 E-value: 6.40e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQP 186
Cdd:cd06323 81 IPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAKYpKINVVASQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 187 ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIG 266
Cdd:cd06323 161 ADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQPEEMG 240
|
250 260
....*....|....*....|....*...
gi 732686642 267 AKGVETADKVLKGEKVQAKYPVDLKLVV 294
Cdd:cd06323 241 AKAVETADKYLKGEKVPKKIPVPLKLVT 268
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
28-292 |
5.07e-95 |
|
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: 281.38 E-value: 5.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQAT-KGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQ 185
Cdd:cd01536 81 IPVVAVDTDIDgGGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYpDIEIVAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 186 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQ 264
Cdd:cd01536 161 PANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTgDIKIVGVDGTPEALKAIKDGELDATVAQDPYL 240
|
250 260
....*....|....*....|....*...
gi 732686642 265 IGAKGVETADKVLKGEKVQAKYPVDLKL 292
Cdd:cd01536 241 QGYLAVEAAVKLLNGEKVPKEILTPVTL 268
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
6-295 |
7.80e-93 |
|
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: 277.19 E-value: 7.80e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 6 LATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKI 85
Cdd:COG1879 13 ALALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 86 LLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARE 165
Cdd:COG1879 93 IIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 166 RGEGFQQAVAAH-KFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTP 243
Cdd:COG1879 173 RTDGFKEALKEYpGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKgDVKVVGFDGSP 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 732686642 244 DGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 295
Cdd:COG1879 253 EALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTK 304
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
28-293 |
7.17e-80 |
|
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: 242.84 E-value: 7.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADK-LGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKyPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQ 185
Cdd:cd06308 81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYpGIKIVASQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 186 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPD-GEKAVNDGKLAATIaqLPD 263
Cdd:cd06308 161 DGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGLPEaGEKAVKDGILAATF--LYP 238
|
250 260 270
....*....|....*....|....*....|
gi 732686642 264 QIGAKGVETADKVLKGEKVQAKYPVDLKLV 293
Cdd:cd06308 239 TGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
28-293 |
7.84e-78 |
|
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.
Pssm-ID: 380532 [Multi-domain] Cd Length: 285 Bit Score: 238.27 E-value: 7.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQAT---KGEVVSHIASDNVLGGKIAGDYIAKKAGEG-AKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVL 182
Cdd:cd06309 81 IPVILVDRTIDgedGSLYVTFIGSDFVEEGRRAAEWLVKNYKGGkGNVVELQGTAGSSVAIDRSKGFREVIKKHpNIKIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 183 ASQPADFDRIKGLNVMQNLLTAHP-DVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKAVNDGKLAATI 258
Cdd:cd06309 161 ASQSGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLKpgkDVLVVGIDGQKDALEAIKAGELNATV 240
|
250 260 270
....*....|....*....|....*....|....*
gi 732686642 259 AQLPDQiGAKGVETADKVLKGEKVQAKYPVDLKLV 293
Cdd:cd06309 241 ECNPLF-GPTAFDTIAKLLAGEKVPKLIIVEERLF 274
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
28-293 |
1.02e-74 |
|
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: 229.90 E-value: 1.02e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQ-ATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQ 185
Cdd:cd19967 81 IPVFLIDREiNAEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQYpELKMVAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 186 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQ 264
Cdd:cd19967 161 SADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRAgDVIIVGFDGSNDVRDAIKEGKISATVLQPAKL 240
|
250 260 270
....*....|....*....|....*....|.
gi 732686642 265 IGAKGVETADKVLKGEK--VQAKYPVDLKLV 293
Cdd:cd19967 241 IARLAVEQADQYLKGGStgKEEKQLFDCVLI 271
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-292 |
5.65e-72 |
|
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: 222.46 E-value: 5.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGE-VVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSaARERGEGFQQAVAAH-KFNVLASQ 185
Cdd:cd19971 81 IPVINVDTPVKDTDlVDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLDHPTAES-CVDRIDGFLDAIKKNpKFEVVAQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 186 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQ 264
Cdd:cd19971 160 DGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKlGDILVYGVDGSPDAKAAIKDGKMTATAAQSPIE 239
|
250 260
....*....|....*....|....*...
gi 732686642 265 IGAKGVETADKVLKGEKVQAKYPVDLKL 292
Cdd:cd19971 240 IGKKAVETAYKILNGEKVEKEIVVPTFL 267
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-294 |
1.53e-71 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380545 [Multi-domain] Cd Length: 270 Bit Score: 221.77 E-value: 1.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQP 186
Cdd:cd06322 81 IPVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKALLGGGGKIAIIDYPEVESVVLRVNGFKEAIKKYpNIEIVAEQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 187 ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVN-DGKLAATIAQLPDQ 264
Cdd:cd06322 161 GDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDkIKVIGFDGNPEAIKAIAkGGKIKADIAQQPDK 240
|
250 260 270
....*....|....*....|....*....|
gi 732686642 265 IGAKGVETADKVLKGEKVQAKYPVDLKLVV 294
Cdd:cd06322 241 IGQETVEAIVKYLAGETVEKEILIPPKLYT 270
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
28-293 |
3.55e-71 |
|
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: 220.72 E-value: 3.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQP 186
Cdd:cd19968 81 IPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAAGpKIKVVFEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 187 ADFDRIKGLNVMQNLLTAHP-DVQAVFAQNDEMALGALRALQTAG--KSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPD 263
Cdd:cd19968 161 GNFERDEGLTVMENILTSLPgPPDAIICANDDMALGAIEAMRAAGldLKKVKVIGFDAVPDALQAIKDGELYATVEQPPG 240
|
250 260 270
....*....|....*....|....*....|
gi 732686642 264 QIGAKGVETADKVLKGEKVQAKYPVDLKLV 293
Cdd:cd19968 241 GQARTALRILVDYLKDKKAPKKVNLKPKLI 270
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
29-296 |
1.54e-69 |
|
periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.
Pssm-ID: 380543 [Multi-domain] Cd Length: 283 Bit Score: 217.13 E-value: 1.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 29 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQaaPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLD-------RQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAA-HK 178
Cdd:cd06320 82 GIPVINLDdavdadaLKKAGGKVTSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKKaPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 179 FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAAT 257
Cdd:cd06320 162 LKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTgKVLVVGTDGIPEAKKSIKAGELTAT 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 732686642 258 IAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVKQ 296
Cdd:cd06320 242 VAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKD 280
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
28-296 |
2.58e-67 |
|
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: 210.97 E-value: 2.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQP 186
Cdd:cd06313 81 IPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYpDIKVLAEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 187 ADFDRIKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQI 265
Cdd:cd06313 161 ANWSRDEAMSLMENWLQAYGDeIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDALQAVKSGELIATVLQDAEAQ 240
|
250 260 270
....*....|....*....|....*....|.
gi 732686642 266 GAKGVETADKVLKGEKVQAKYPVDLKLVVKQ 296
Cdd:cd06313 241 GKGAVEVAVDAVKGEGVEKKYYIPFVLVTKD 271
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-292 |
8.52e-65 |
|
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: 204.41 E-value: 8.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADK-LGYNLVV--LDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMAN 104
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEaNGYELLVkgIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVITLD------RQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHK 178
Cdd:cd19970 81 DAGIAVINIDnrldadALKEGGINVPFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 179 FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAAT 257
Cdd:cd19970 161 MKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKMLAT 240
|
250 260 270
....*....|....*....|....*....|....*
gi 732686642 258 IAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKL 292
Cdd:cd19970 241 IDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPVEL 275
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
28-293 |
7.33e-64 |
|
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: 202.08 E-value: 7.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADK-LGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQ-ATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLAS 184
Cdd:cd06301 82 GIPLVYVNREpDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYpGMKIVAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIAQLPD 263
Cdd:cd06301 162 QTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDdILVAGIDATPDALKAMKAGRLDATVFQDAA 241
|
250 260 270
....*....|....*....|....*....|
gi 732686642 264 QIGAKGVETADKVLKGEKVQAKYPVDLKLV 293
Cdd:cd06301 242 GQGETAVDVAVKAAKGEEVESDIWIPFELV 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-296 |
1.99e-63 |
|
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: 201.05 E-value: 1.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGE----GAKVIELQGIAGTSAARERGEGFQQAVAAHKFNVLA 183
Cdd:cd06319 81 IPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKEngwgGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 184 S-QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQL 261
Cdd:cd06319 161 LrQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTgDILVVGFDGDPEALDLIKDGKLDGTVAQQ 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 732686642 262 PDQIGAKGVETADKVLKGEKVQAK-YPVDLKLVVKQ 296
Cdd:cd06319 241 PFGMGARAVELAIQALNGDNTVEKeIYLPVLLVTSE 276
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
28-282 |
2.68e-61 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 195.71 E-value: 2.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQ-ATKGEVVSHIASDNVLGGKIAGDYIAKKAG-EGAKVIELQGIAGTSAARERGEGFQQAV--------AAH 177
Cdd:cd06318 81 IPVITVDSAlDPSANVATQVGRDNKQNGVLVGKEAAKALGgDPGKIIELSGDKGNEVSRDRRDGFLAGVneyqlrkyGKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 178 KFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVM-VVGFDGTPDGEKAVNDGKLAA 256
Cdd:cd06318 161 NIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVkVAGADGQKEALKLIKDGKYVA 240
|
250 260
....*....|....*....|....*.
gi 732686642 257 TIAQLPDQIGAKGVETADKVLKGEKV 282
Cdd:cd06318 241 TGLNDPDLLGKTAVDTAAKVVKGEES 266
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-293 |
4.19e-61 |
|
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: 194.97 E-value: 4.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVA-AHKFNVLASQP 186
Cdd:cd19972 81 IPVIAVDRNPEDAPGDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAeAPGIKVVAEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 187 ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQI 265
Cdd:cd19972 161 ADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDhKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKM 240
|
250 260
....*....|....*....|....*...
gi 732686642 266 GAKGVETADKVLKGEKVQAKYPVDLKLV 293
Cdd:cd19972 241 GRLAVDSAIDLLNGKAVPKEQLQDAVLT 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-293 |
4.54e-60 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380544 [Multi-domain] Cd Length: 270 Bit Score: 192.12 E-value: 4.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYN--LVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 105
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGakVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQAtKGeVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAgTSAARERGEGFQQAVAAHK-FNVLAS 184
Cdd:cd06321 81 AGIIVVAVDVAA-EG-ADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPP-VSAVIDRVNGCKEALAEYPgIKLVDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVND--GKLAATIAQLP 262
Cdd:cd06321 158 QNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSVDGSPEAVAALKRegSPFIATAAQDP 237
|
250 260 270
....*....|....*....|....*....|..
gi 732686642 263 DQIGAKGVETADKVLKGEKVQAK-YPVDLKLV 293
Cdd:cd06321 238 YDMARKAVELALKILNGQEPAPElVLIPSTLV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-286 |
4.98e-55 |
|
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: 179.46 E-value: 4.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 105
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVgpESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH--KFNVLA 183
Cdd:cd06310 81 KGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHpgGIKVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 184 SQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIAQLP 262
Cdd:cd06310 161 SQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGqIKIVGFDSQEELLDALKNGKIDALVVQNP 240
|
250 260
....*....|....*....|....
gi 732686642 263 DQIGAKGVETADKVLKGEKVQAKY 286
Cdd:cd06310 241 YEIGYEGIKLALKLLKGEEVPKNI 264
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
29-281 |
2.43e-54 |
|
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433182 [Multi-domain] Cd Length: 259 Bit Score: 177.12 E-value: 2.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 29 IALVVSTLNNPFFVSLKDGAQKEADKLGYN-LVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEvIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH--KFNVLAS- 184
Cdd:pfam13407 81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKypGIKVVAEv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 QPADFDRIKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIAQLP 262
Cdd:pfam13407 161 EGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGkVVVTGFDATPEALEAIKDGTIDATVLQDP 240
|
250
....*....|....*....
gi 732686642 263 DQIGAKGVETADKVLKGEK 281
Cdd:pfam13407 241 YGQGYAAVELAAALLKGKK 259
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
3-295 |
2.42e-52 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 173.91 E-value: 2.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 3 MKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTV 80
Cdd:PRK09701 1 MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFasPSEGDFQSQLQLFEDLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 81 RGTKILLINPTDSDAVGNAVKMANQANIPVITLDR-------QATKGEVVSHIASDNVLGGKIAGDYIAKKAG-EGAKVI 152
Cdd:PRK09701 81 KNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEkidmdnlKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 153 ELQGIAGTSAARERGEGFQQA-VAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK 231
Cdd:PRK09701 161 IIEGKAGNASGEARRNGATEAfKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732686642 232 -SDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGV------ETADKVLKGEKVQAKYPVDLKLVVK 295
Cdd:PRK09701 241 tGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLklmvdaEKSGKVIPLDKAPEFKLVDSILVTQ 311
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-289 |
3.27e-52 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380662 [Multi-domain] Cd Length: 271 Bit Score: 172.04 E-value: 3.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL-DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQgPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLD-RQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAA-HKFNVLAS 184
Cdd:cd20007 81 GIKVVTVDtTLGDPSFVLSQIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMKKyPGIKVLGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIAQLPD 263
Cdd:cd20007 161 QYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGkVKVVGFDASPAQVEQLKAGTIDALIAQKPA 240
|
250 260
....*....|....*....|....*.
gi 732686642 264 QIGAKGVETADKVLKGEKVQAKYPVD 289
Cdd:cd20007 241 EIGYLAVEQAVAALTGKPVPKDILTP 266
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-286 |
2.24e-49 |
|
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: 165.10 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANq 105
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLgpATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAK----KAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH--KF 179
Cdd:cd20008 80 AGIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAEllkaSGGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKypDI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 180 NVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATI 258
Cdd:cd20008 160 EIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAgKIVLVGFDSSPDEVALLKSGVIKALV 239
|
250 260
....*....|....*....|....*...
gi 732686642 259 AQLPDQIGAKGVETADKVLKGEKVQAKY 286
Cdd:cd20008 240 VQDPYQMGYEGVKTAVKALKGEEIVEKN 267
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
28-285 |
8.33e-46 |
|
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: 155.37 E-value: 8.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAvgNAVKMANQAN 107
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDD--ELLEELLAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQAtKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIE-LQGIAGTSAARERGEGFQQAVAAHKFNVLAS-- 184
Cdd:cd06267 79 IPVVLIDRRL-DGLGVDSVVVDNYAGAYLATEHLIEL---GHRRIAfIGGPLDLSTSRERLEGYRDALAEAGLPVDPElv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndgkLAA----- 256
Cdd:cd06267 155 VEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRvpeDISVVGFDDIP----------LAAlltpp 224
|
250 260 270
....*....|....*....|....*....|.
gi 732686642 257 --TIAQLPDQIGAKGVETADKVLKGEKVQAK 285
Cdd:cd06267 225 ltTVRQPAYEMGRAAAELLLERIEGEEEPPR 255
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
28-285 |
2.26e-45 |
|
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: 154.28 E-value: 2.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQN-NPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQ 185
Cdd:cd06314 81 GIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKGSpGIEIVDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 186 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQ 264
Cdd:cd06314 161 SDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKvGKVKIVGFDTLPETLQGIKDGVIAATVGQRPYE 240
|
250 260
....*....|....*....|.
gi 732686642 265 IGAKGVETADKVLKGEKVQAK 285
Cdd:cd06314 241 MGYLSVKLLYKLLKGGKPVPD 261
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
22-285 |
2.61e-45 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 156.13 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 22 NAMAK-------DTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGtkILLINPT 91
Cdd:COG1609 50 NAAARslrtgrtRTIGVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLsrrVDG--LILAGSR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 92 DSDAvgnAVKMANQANIPVITLDRQaTKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVI-ELQGIAGTSAARERGEGF 170
Cdd:COG1609 128 LDDA---RLERLAEAGIPVVLIDRP-LPDPGVPSVGVDNRAGARLATEHLIEL---GHRRIaFIGGPADSSSARERLAGY 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 171 QQAVAAHKFNVLASQ--PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDG 245
Cdd:COG1609 201 REALAEAGLPPDPELvvEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRvpeDVSVVGFDDIPLA 280
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 732686642 246 EkaVNDGKLaATIAQLPDQIGAKGVETADKVLKGEKVQAK 285
Cdd:COG1609 281 R--YLTPPL-TTVRQPIEEMGRRAAELLLDRIEGPDAPPE 317
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
28-294 |
6.35e-45 |
|
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: 153.06 E-value: 6.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGtkILLInpTDSDAVGNAVKman 104
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKrnkVDG--IILG--SHSLDIEEYKK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 qANIPVITLDRQATKGevVSHIASDNVLGGKIAGDYIAKKageGAK-VIELQGIAGTSAARERGEGFQQAVAAH--KFNV 181
Cdd:cd06291 74 -LNIPIVSIDRYLSEG--IPSVSSDNYQGGRLAAEHLIEK---GCKkILHIGGPSNNSPANERYRGFEDALKEAgiEYEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 182 LASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKAVNdgKLaATI 258
Cdd:cd06291 148 IEIDENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRvpeDVQIIGFDGIEISELLYP--EL-TTI 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 732686642 259 AQLPDQIGAKGVETADKVLKGEKVQAK-YPVDLKLVV 294
Cdd:cd06291 225 RQPIEEMAKEAVELLLKLIEGEEIEESrIVLPVELIE 261
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-295 |
1.74e-44 |
|
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: 152.00 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 105
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRgpSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH--KFNVLA 183
Cdd:cd20004 81 QGIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAKGSASTTDRERGFLEALKKLapGLKVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 184 SQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLP 262
Cdd:cd20004 161 DQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLAgKVKFIGFDASDLLLDALRAGEISALVVQDP 240
|
250 260 270
....*....|....*....|....*....|...
gi 732686642 263 DQIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 295
Cdd:cd20004 241 YRMGYLGVKTAVAALRGKPVPKRIDTGVVLVTK 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
28-286 |
1.76e-42 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380651 [Multi-domain] Cd Length: 302 Bit Score: 147.77 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYN---LVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMAN 104
Cdd:cd19996 1 TIGFSNAGLGNSWRVQMIAEFEAEAAKLKKLikeLIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHK-FNVLA 183
Cdd:cd19996 81 AAGIPVVLFDSGVGSDKYTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYPgIKIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 184 SQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGE--KAVNDGKLAATIaqL 261
Cdd:cd19996 161 EVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTGEDNNGFLKawKELPGFKSIAPS--Y 238
|
250 260
....*....|....*....|....*
gi 732686642 262 PDQIGAKGVETADKVLKGEKVQAKY 286
Cdd:cd19996 239 PPWLGATALDAALAALEGEPVPKYV 263
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
29-289 |
2.68e-42 |
|
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: 146.96 E-value: 2.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 29 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANI 108
Cdd:cd19992 2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 109 PVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIeLQGIAGTSAARERGEGF----QQAVAAHKFNVLAS 184
Cdd:cd19992 82 PVISYDRLILNADVDLYVGRDNYKVGQLQAEYALEAVPKGNYVI-LSGDPGDNNAQLITAGAmdvlQPAIDSGDIKIVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 QPAD-FDRIKGLNVMQNLLTA-HPDVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQL 261
Cdd:cd19992 161 QYVKgWSPDEAMKLVENALTAnNNNIDAVLAPNDGMAGGAIQALKAQGlAGKVFVTGQDAELAALKRIVEGTQTMTVWKD 240
|
250 260
....*....|....*....|....*...
gi 732686642 262 PDQIGAKGVETADKVLKGEKVQAKYPVD 289
Cdd:cd19992 241 LKELARAAADAAVKLAKGEKPQTTDETI 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-295 |
2.66e-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: 380540 [Multi-domain] Cd Length: 281 Bit Score: 139.05 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAG----DYIAKKAGEGAKVielqGIAGTSAA---RERGEGFQQAVAAH-KF 179
Cdd:cd06317 81 IPVIAYDAVIPSDFQAAQVGVDNLEGGKEIGkyaaDYIKAELGGQAKI----GVVGALSSliqNQRQKGFEEALKANpGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 180 NVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPD-GEKAVNDGKLAAT 257
Cdd:cd06317 157 EIVATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQgKIKVFGWDLTKQaIFLGIDEGVLQAV 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 732686642 258 IAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 295
Cdd:cd06317 237 VQQDPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-259 |
7.59e-38 |
|
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: 136.19 E-value: 7.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVV-STLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKI--LLINPTDSDAVGnAVKMAN 104
Cdd:cd06324 1 RVVFINpGKEDEPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARPPKPdyLILVNEKGVAPE-LLELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVITLDRQATKGEV-------------VSHIASDNVLGG-KIAGDYIA----KKAGEGAKVIELQGIAGTSAARER 166
Cdd:cd06324 80 QAKIPVFLINNDLTDEERallgkprekfkywLGSIVPDNEQAGyLLAKALIKaarkKSDDGKIRVLAISGDKSTPASILR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 167 GEGFQQAVAAH-KFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGT 242
Cdd:cd06324 160 EQGLRDALAEHpDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLkpgKDVLVGGIDWS 239
|
250
....*....|....*..
gi 732686642 243 PDGEKAVNDGKLAATIA 259
Cdd:cd06324 240 PEALQAVKDGELTASVG 256
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-290 |
1.93e-37 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 133.64 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQP 186
Cdd:cd06311 81 IPVVNFDRGLNVLIYDLYVAGDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNpGIKILAMQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 187 ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDV-MVVGFDGTPDGEKAVNDGK--LAATIAQLPD 263
Cdd:cd06311 161 GDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIkVMTGGGGSQEYFKRIMDGDpiWPASATYSPA 240
|
250 260 270
....*....|....*....|....*....|
gi 732686642 264 QIgAKGVETADKVLKGEK---VQAKYPVDL 290
Cdd:cd06311 241 MI-ADAIKLAVLILKGGKtveKEVIIPSTL 269
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-278 |
1.54e-36 |
|
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: 131.82 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 105
Cdd:cd19973 1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAagKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQATKGEVV-SHIASDNVLGGKIAGDYIAKKAGEG-AKVIELQGIAGTSAARERGEGF-----------QQ 172
Cdd:cd19973 81 AGVLVIALDTPTDPIDAAdATFATDNFKAGVLIGEWAKAALGAKdAKIATLDLTPGHTVGVLRHQGFlkgfgidekdpES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 173 AVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKAVND 251
Cdd:cd19973 161 NEDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKeKGVLIVSVDGGCPGVKDVKD 240
|
250 260
....*....|....*....|....*..
gi 732686642 252 GKLAATIAQLPDQIGAKGVETADKVLK 278
Cdd:cd19973 241 GIIGATSQQYPLRMAALGVEAIAAFAK 267
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-285 |
2.16e-36 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 131.21 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 105
Cdd:cd20005 1 YIAVISKGFQHQFWKAVKKGAEQAAKELGVKITFEgpDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFN--VLA 183
Cdd:cd20005 81 KGIPVVTFDSGVPSDLPLATVATDNYAAGALAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDikVVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 184 SQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKAVNDGKLAATIAQLP 262
Cdd:cd20005 161 VQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKlGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNP 240
|
250 260
....*....|....*....|...
gi 732686642 263 DQIGAKGVETADKVLKGEKVQAK 285
Cdd:cd20005 241 YGMGYKTVKAAVKALKGEEVEKL 263
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-295 |
3.28e-34 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 125.40 E-value: 3.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVV--STLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMA 103
Cdd:cd20006 1 KIALILksSDPNSDFWQTVKSGAEAAAKEYGVDLEFLgpESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 104 NQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKF-NVL 182
Cdd:cd20006 81 KKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQALAEYPNiKIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 183 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQL 261
Cdd:cd20006 161 ETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGlGGKVKVVGFDSSVEEIQLLEEGIIDALVVQN 240
|
250 260 270
....*....|....*....|....*....|....
gi 732686642 262 PDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 295
Cdd:cd20006 241 PFNMGYLSVQAAVDLLNGKKIPKRIDTGSVVITK 274
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
25-284 |
1.52e-33 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 124.48 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 25 AKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMAN 104
Cdd:COG4213 1 GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAK--VIELQGIAGTSAARERGEGF----QQAVAAHK 178
Cdd:COG4213 81 AAGIPVIAYDRLILNSDVDYYVSFDNVKVGELQGQYLVDGLPLKGKgnIELFGGSPTDNNATLFFEGAmsvlQPYIDSGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 179 FNVLASQPA-DFDRIKGLNVMQNLLTAHP-DVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLA 255
Cdd:COG4213 161 LVVVSGQWTlGWDPETAQKRMENLLTANGnKVDAVLAPNDGLAGGIIQALKAQGLAgKVVVTGQDAELAAVQRILAGTQY 240
|
250 260
....*....|....*....|....*....
gi 732686642 256 ATIAQLPDQIGAKGVETADKVLKGEKVQA 284
Cdd:COG4213 241 MTVYKDTRELAEAAAELAVALAKGEKPEV 269
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
28-272 |
1.59e-33 |
|
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: 123.52 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVgNAVKMANQAN 107
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDD-DAELLAALRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAKKageGAKVIE-LQGIAGTSAARERGEGFQQAVAAHKFNVLAS-- 184
Cdd:cd06275 80 IPVVVLDREIAGDNADA-VLDDSFQGGYLATRHLIEL---GHRRIGcITGPLEHSVSRERLAGFRRALAEAGIEVPPSwi 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDGTPdgekavndgkLAA----- 256
Cdd:cd06275 156 VEGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGlrvPQDISIIGYDDIE----------LARyfspa 225
|
250
....*....|....*...
gi 732686642 257 --TIAQLPDQIGAKGVET 272
Cdd:cd06275 226 ltTIHQPKDELGELAVEL 243
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-243 |
2.00e-33 |
|
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: 123.03 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYN--LVVLDSQNNPAKELANVQDLTVRGtkILLINPTDSDAVgnaVKMANQ 105
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRplLFNVDDEDDVDDALRQLLQYRVDG--VIVTSATLSSEL---AEECAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQATkGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIE-LQGIAGTSAARERGEGFQQAVAAHKFNVLAS 184
Cdd:cd06278 76 RGIPVVLFNRVVE-DPGVDSVSCDNRAGGRLAADLLLAA---GHRRIAfLGGPEGTSTSRERERGFRAALAELGLPPPAV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732686642 185 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS----DVMVVGFDGTP 243
Cdd:cd06278 152 EAGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGLvvpeDISVVGFDDIP 214
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
28-260 |
3.67e-33 |
|
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: 123.46 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLG-YNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGkIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQATKGEV--------VSHIASDN-VLGGKIAGDYIAK-----KAGEGakVIE---LQGIAGTSAARERGEG 169
Cdd:cd01539 82 NIPVIFFNREPSREDLksydkayyVGTDAEESgIMQGEIIADYWKAnpeidKNGDG--KIQyvmLKGEPGHQDAIARTKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 170 FQQAVAAH--KFNVLASQPADFDRIKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAG------KSDVMVVGFD 240
Cdd:cd01539 160 SVKTLNDAgiKTEQLAEDTANWDRAQAKDKMDAWLSKYGDkIELVIANNDDMALGAIEALKAAGyntgdgDKYIPVFGVD 239
|
250 260
....*....|....*....|
gi 732686642 241 GTPDGEKAVNDGKLAATIAQ 260
Cdd:cd01539 240 ATPEALEAIKEGKMLGTVLN 259
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
28-282 |
2.21e-32 |
|
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: 120.38 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQ--NNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 105
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGgyTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGA-KVIELQGIAGTSAARERGEGFQQAVAAHKFNVLAS 184
Cdd:cd06306 81 AGIPVIDLVNGIDSPKVAARVLVDFYDMGYLAGEYLVEHHPGKPvKVAWFPGPAGAGWAEDREKGFKEALAGSNVEIVAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 QPADFDRIKGLNVMQNLLTAHPDVQAVFAqNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPD 263
Cdd:cd06306 161 KYGDTGKAVQLNLVEDALQAHPDIDYIVG-NAVAAEAAVGALREAGLTgKVKVVSTYLTPGVYRGIKRGKILAAPSDQPV 239
|
250
....*....|....*....
gi 732686642 264 QIGAKGVETADKVLKGEKV 282
Cdd:cd06306 240 LQGRIAVDQAVRALEGKPV 258
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
46-281 |
3.15e-32 |
|
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: 120.89 E-value: 3.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 46 DGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDrQATKGEVVSH 125
Cdd:cd06300 24 DAAQSGQKGLVKELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFD-GAVTSPDAYN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 126 IASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQPADFDRIKGLNVMQNLLTA 204
Cdd:cd06300 103 VSNDQVEWGRLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEALAEYpGIKVVGEVFGGWDEATAQTAMLDFLAT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732686642 205 HPDVQAVFAQNDEmALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGK--LAATIAQLPDQIGAKGVETADKVLKGEK 281
Cdd:cd06300 183 HPQVDGVWTQGGE-DTGVLQAFQQAGRPPVPIVGGDENGFAKQWWKHPKkgLTGAAVWPPPAIGAAGLEVALRLLEGQG 260
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
28-281 |
9.53e-32 |
|
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: 118.52 E-value: 9.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPT--DSDAVGNAVKmanq 105
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSagPSRELKRLLK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAKKageGAKVIEL-QGIAGTSAARERGEGFQQAVAAHKFNVLAS 184
Cdd:cd06280 77 HGIPIVLIDREVEGLELDL-VAGDNREGAYKAVKHLIEL---GHRRIGLiTGPLEISTTRERLAGYREALAEAGIPVDES 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 --QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEkaVNDGKLAAtIA 259
Cdd:cd06280 153 liFEGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEipqDISVVGFDDSDWFE--IVDPPLTV-VA 229
|
250 260
....*....|....*....|..
gi 732686642 260 QLPDQIGAKGVETADKVLKGEK 281
Cdd:cd06280 230 QPAYEIGRIAAQLLLERIEGQG 251
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
28-286 |
1.08e-30 |
|
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: 116.24 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVsHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGiAGTSAARERGEGFQQAVAAHK--FNVLASQ 185
Cdd:cd06305 81 IPVVTFDTDSQVPGVN-NITQDDYALGTLSLGQLVKDLNGEGNIAVFNV-FGVPPLDKRYDIYKAVLKANPgiKKIVAEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 186 PADFDrikglNVMQN-------LLTAHPD--VQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAV--NDGKL 254
Cdd:cd06305 159 GDVTP-----NTAADaqtqveaLLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISNQDLELMadEGSPW 233
|
250 260 270
....*....|....*....|....*....|..
gi 732686642 255 AATIAQLPDQIGAKGVETADKVLKGEKVQAKY 286
Cdd:cd06305 234 VATAAQDPALIGTVAVRNVARKLAGEDLPDKY 265
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-282 |
1.77e-30 |
|
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: 115.40 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTK--ILLINPTDSDAVgNAVKManq 105
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDgiIVVGGFGDEELL-KLLAE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 aNIPVITLDRQaTKGEVVSHIASDNVLGGKIAGDYIAKKageGA-KVIELQGIAGTSAARERGEGFQQAVAAH--KFNVL 182
Cdd:cd06290 77 -GIPVVLVDRE-LEGLNLPVVNVDNEQGGYNATNHLIDL---GHrRIVHISGPEDHPDAQERYAGYRRALEDAglEVDPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 183 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGE-----------KA 248
Cdd:cd06290 152 LIVEGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRvpdDVSVIGFDDLPFSKyttpplttvrqPL 231
|
250 260 270
....*....|....*....|....*....|....
gi 732686642 249 VNDGKLAATIaqLPDQIGAKGVETADKVLKGEKV 282
Cdd:cd06290 232 YEMGKTAAEI--LLELIEGKGRPPRRIILPTELV 263
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
28-281 |
6.54e-30 |
|
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: 113.88 E-value: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDavGNAVKMANQ-A 106
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNIS--DEAIIKLLKeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAKKAGEgaKVIELQGIAGTSAARERGEGFQQAVAAHKFNVLASQ- 185
Cdd:cd19976 79 KIPVVVLDRYIEDNDSDS-VGVDDYRGGYEATKYLIELGHT--RIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWi 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 186 -PADFDrIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKAvnDGKLaATIAQL 261
Cdd:cd19976 156 ySGESS-LEGGYKAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKipeDLSVIGFDNIILSEYI--TPAL-TTIAQP 231
|
250 260
....*....|....*....|
gi 732686642 262 PDQIGAKGVETADKVLKGEK 281
Cdd:cd19976 232 IFEMGQEAAKLLLKIIKNPA 251
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-271 |
3.25e-29 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 111.98 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPtdSDAVGNAVKMANQAN 107
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTP--SDDDLSHLARLRARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQAtKGEVVSHIASDNVLGGKIAGDYIakkAGEGAKVIE-LQGIAGTSAARERGEGFQQAVAAHKFN----VL 182
Cdd:cd06293 79 TAVVLLDRPA-PGPAGCSVSVDDVQGGALAVDHL---LELGHRRIAfVSGPLRTRQVAERLAGARAAVAEAGLDpdevVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 183 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndgkLAA--- 256
Cdd:cd06293 155 ELSAPDANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRvpdDVSVVGYDDLP----------FAAaan 224
|
250
....*....|....*....
gi 732686642 257 ----TIAQLPDQIGAKGVE 271
Cdd:cd06293 225 ppltTVRQPSYELGRAAAD 243
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
28-294 |
5.18e-29 |
|
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: 111.48 E-value: 5.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKE---LANVQDLTVRGtkILLINPTDSdavgNAVKMAN 104
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREddlLDMLRSRRVDG--VILLSGRLD----AELLSEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVItldrQA---TKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIELqgIAGTSA---ARERGEGFQQAVAAHK 178
Cdd:cd06284 75 SKRYPIV----QCceyIPDSGVPSVSIDNEAAAYDATEYLISL---GHRRIAH--INGPLDnvyARERLEGYRRALAEAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 179 --FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTpdgekavndgK 253
Cdd:cd06284 146 lpVDEDLIIEGDFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRvpeDVSVIGFDDI----------E 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 732686642 254 LAA-------TIAQLPDQIGAKGVET-ADKVLKGEKVQAKYPVDLKLVV 294
Cdd:cd06284 216 FAEmfspsltTIRQPRYEIGETAAELlLEKIEGEGVPPEHIILPHELIV 264
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
28-283 |
7.30e-29 |
|
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: 111.11 E-value: 7.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGtkILLINPTDSDAVGNAVKman 104
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKekrVDG--IIFASGTLTEENKQLLK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAKKageGAKVIELqgIAG----TSAARERGEGFQQAVAAH--K 178
Cdd:cd19975 76 NMNIPVVLVSTESEDPDIPS-VKIDDYQAAYDATNYLIKK---GHRKIAM--ISGplddPNAGYPRYEGYKKALKDAglP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 179 FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDGTPDGEKAVNdgKLa 255
Cdd:cd19975 150 IKENLIVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGirvPEDISVIGFDNTEIAEMSIP--PL- 226
|
250 260
....*....|....*....|....*...
gi 732686642 256 ATIAQLPDQIGAKGVETADKVLKGEKVQ 283
Cdd:cd19975 227 TTVSQPFYEMGKKAVELLLDLIKNEKKE 254
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
28-268 |
1.31e-28 |
|
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: 110.35 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINP---TDSDAVgnavKMAN 104
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPaagTTAELL----RRLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVITLDRQATkGEVVSHIASDNVLGGKIAGDYIAkkaGEGAKVIE-LQGIAGTSAARERGEGFQQAVAAHKFNVLA 183
Cdd:cd06289 77 AWGIPVVLALRDVP-GSDLDYVGIDNRLGAQLATEHLI---ALGHRRIAfLGGLSDSSTRRERLAGFRAALAEAGLPLDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 184 SQ--PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGTPdgEKAVNDGKLaATI 258
Cdd:cd06289 153 SLivPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLepgRDIAVVGFDDVP--EAALWTPPL-TTV 229
|
250
....*....|
gi 732686642 259 AQLPDQIGAK 268
Cdd:cd06289 230 SVHPREIGRR 239
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-272 |
2.08e-27 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 107.31 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAvGNAVKMANqAN 107
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDA-PDLQELAA-RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVShIASDNVLGGKIAGDYIakkAGEG-AKVIELQGIAGTSAARERGEGFQQAVAAHKFNVLASQ- 185
Cdd:cd06285 79 VPVVLVDRRIGDTALPS-VTVDNELGGRLATRHL---LELGhRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERi 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 186 -PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndgkLAA----- 256
Cdd:cd06285 155 vPGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRvpeDLSVVGFDDIP----------LAAflppp 224
|
250
....*....|....*...
gi 732686642 257 --TIAQLPDQIGAKGVET 272
Cdd:cd06285 225 ltTVRQPKYEMGRRAAEL 242
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
28-240 |
2.68e-27 |
|
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380494 [Multi-domain] Cd Length: 266 Bit Score: 106.84 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTK-ILLINPTDSDAvgnAVKMANQA 106
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDaIILHSRALSDE---ELILIAEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQATKgevVSH--IASDNVLGGKIAGDYIAKKageGAKVIE-LQGIAGTSAARERGEGFQQAVAAH--KFNV 181
Cdd:cd06270 78 IPPLVVINRYIPG---LADrcVWLDNEQGGRLAAEHLLDL---GHRRIAcITGPLDIPDARERLAGYRDALAEAgiPLDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732686642 182 LASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFD 240
Cdd:cd06270 152 SLIIEGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKvpeDVSVIGFD 213
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
58-282 |
3.82e-27 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380654 [Multi-domain] Cd Length: 313 Bit Score: 107.39 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 58 NLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVShIASDNVLGGKIA 137
Cdd:cd19999 36 DLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPVSSPDAIN-VVIDQYKWAAIQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 138 GDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHK-FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQnD 216
Cdd:cd19999 115 AQWLAEQLGGKGNIVAINGVAGNPANEARVKAADDVFAKYPgIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLTQ-D 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732686642 217 EMALGALRALQTAGKSDVMVVGfDGTPDGEKAVNDGKLAA--TIAQL-PDQIGAKGVETADKVLKGEKV 282
Cdd:cd19999 194 GMAEGVLRAFQAAGKDPPVMTG-DYRKGFLRKWKELDLPDfeSIGVVnPPGIGATALRIAVRLLQGKEL 261
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
28-296 |
3.89e-27 |
|
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: 106.48 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLN-NPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGtkILLINPTdSDAVGNAVKMA 103
Cdd:cd06288 1 TIGLITDDIAtTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLsrrVDG--IIYASMH-HREVTLPPELT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 104 NqanIPVITLDRQATKGEVVSHIAsDNVLGGKIAGDYIAKKageGAKVIELqgIAGTS---AARERGEGFQQAVAAHKFN 180
Cdd:cd06288 78 D---IPLVLLNCFDDDPSLPSVVP-DDEQGGYLATRHLIEA---GHRRIAF--IGGPEdslATRLRLAGYRAALAEAGIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 181 VLAS--QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDgtpdgekavnDGKLA 255
Cdd:cd06288 149 YDPSlvVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRvpeDLSVVGFD----------NQELA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 732686642 256 A------TIAQLP-DQIGAKGVETA-DKVLKGEKVQAKYPVDLKLVVKQ 296
Cdd:cd06288 219 AylrpplTTVALPyYEMGRRAAELLlDGIEGEPPEPGVIRVPCPLIERE 267
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
29-273 |
5.19e-27 |
|
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: 106.18 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 29 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQaNI 108
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQ-NV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 109 PVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEgaKVIELQGIAGTSAARERGEGFQQAV--AAHKFNVLASQP 186
Cdd:cd01537 81 PVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHI--QIVLLKGPLGHPDAEARLAGVIKELndKGIKTEQLQLDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 187 ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGTPDGEKAvndGKLAATIAQLPD 263
Cdd:cd01537 159 GDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLrvpSDISVFGYDALPEALKS---GPLLTTILQDAN 235
|
250
....*....|
gi 732686642 264 QIGAKGVETA 273
Cdd:cd01537 236 NLGKTTFDLL 245
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
28-243 |
7.90e-27 |
|
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: 105.69 E-value: 7.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAvGNAVKMANQaN 107
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNE-DLIEKLVKS-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRqATKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIELQGIA-GTSAARERGEGFQQAVAAHKfnvlasQP 186
Cdd:cd19977 79 IPVVFVDR-YIPGLDVDTVVVDNFKGAYQATEHLIEL---GHKRIAFITYPlELSTRQERLEGYKAALADHG------LP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732686642 187 ADFDRIKGLNVMQN-------LLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGTP 243
Cdd:cd19977 149 VDEELIKHVDRQDDvrkaiseLLKLEKPPDAIFAANNLITLEVLKAIKELGLripDDIALIGFDDIP 215
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
28-272 |
6.52e-26 |
|
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: 103.13 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAvgNAVKMANQAN 107
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENS--EGLQALIAQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIelQGIAGTSAARERGEGFQQAVAAHKFNV--LASQ 185
Cdd:cd06299 79 LPVVFVDREVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYI--SGPLSTSTGRERLAAFRAALTAAGIPIdeELVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 186 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDGTPDGEkaVNDGKLAAtIAQLP 262
Cdd:cd06299 157 FGDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGlriGDDVSLISFDDVPWFE--LLSPPLTV-IAQPV 233
|
250
....*....|
gi 732686642 263 DQIGAKGVET 272
Cdd:cd06299 234 ERIGRRAVEL 243
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
28-281 |
7.11e-25 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380480 [Multi-domain] Cd Length: 283 Bit Score: 100.96 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERG---EGFQQAVAAHKFNVLAS 184
Cdd:cd01538 81 IKVIAYDRLILNADVDYYISFDNEKVGELQAQALLDAKPEGNYVLIGGSPTDNNAKLFRDgqmKVLQPAIDSGKIKVVGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 QPAD-FDRIKGLNVMQNLLTAH-PDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIAQL 261
Cdd:cd01538 161 QWVDdWLPANAQQIMENALTANgNNVDAVVASNDGTAGGAIAALKAQGLSGgVPVSGQDADLAAIKRILAGTQTMTVYKD 240
|
250 260
....*....|....*....|
gi 732686642 262 PDQIGAKGVETADKVLKGEK 281
Cdd:cd01538 241 IRLLADAAAEVAVALMRGEK 260
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-282 |
8.10e-25 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380539 [Multi-domain] Cd Length: 294 Bit Score: 100.78 E-value: 8.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLV-VLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd06316 1 KVAIAMHTTGSDWSRLQVAGIKDTFEELGIEVVaVTDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQAT----KGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFNVL 182
Cdd:cd06316 81 GIKLVFMDNVPDgleaGKDYVSVVSSDNRGNGQIAAELLAEAIGGKGKVGIIYHDADFYATNQRDKAFKDTLKEKYPDIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 183 ASQPADFDRI-KGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFD-GTPDGEKAVNDGKLAATIAQ 260
Cdd:cd06316 161 IVAEQGFADPnDAEEVASAMLTANPDIDGIYVSWDTPALGVISALRAAGRSDIKITTVDlGTEIALDMAKGGNVKGIGAQ 240
|
250 260
....*....|....*....|..
gi 732686642 261 LPDQIGAKGVETADKVLKGEKV 282
Cdd:cd06316 241 RPYDQGVAEALAAALALLGKEV 262
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
28-289 |
5.53e-24 |
|
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: 98.47 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL-DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd06302 1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQATKG--EVVSHIASDNVLGGKIAgDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH--KFNVL 182
Cdd:cd06302 81 GIKVITWDSDAPPSarDYFVNQADDEGLGEALV-DSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKypDIELV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 183 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFdGTP-DGEKAVNDGKLAATIAQ 260
Cdd:cd06302 160 DTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGkVAVTGI-GLPnTARPYLKDGSVKEGVLW 238
|
250 260
....*....|....*....|....*....
gi 732686642 261 LPDQIGAKGVETADKVLKGEKVQAKYPVD 289
Cdd:cd06302 239 DPAKLGYLTVYAAYQLLKGKGFTEDSDDV 267
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
28-272 |
1.43e-23 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 98.23 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVkMANQAN 107
Cdd:PRK10423 58 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREI-MQRYPS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGevVSHIASDN-VLGGKIAGDYIAKKageGAKVIELqgIAG---TSAARERGEGFQQAVAAHKFNVLA 183
Cdd:PRK10423 137 VPTVMMDWAPFDG--DSDLIQDNsLLGGDLATQYLIDK---GYTRIAC--ITGpldKTPARLRLEGYRAAMKRAGLNIPD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 184 SQP--ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDgtpdgekavnDGKLA--- 255
Cdd:PRK10423 210 GYEvtGDFEFNGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLSvpqDIAVIGYD----------DIELArym 279
|
250 260
....*....|....*....|.
gi 732686642 256 ----ATIAQLPDQIGAKGVET 272
Cdd:PRK10423 280 tpplTTIHQPKDELGELAIDV 300
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-262 |
1.44e-23 |
|
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: 96.92 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVV-STLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELA-NVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 105
Cdd:cd06312 1 TIYVIShGSPSDPFWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQArLIEQAIAAKPDGIIVTIPDPDALEPALKRAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITL----DRQATKGEVVSHIASDNVLGGKIAGDYiAKKAGEGAKVIELQgIAGTSAARERGEGFQQAVAAHKFNV 181
Cdd:cd06312 81 AGIPVIAInsgdDRSKERLGALTYVGQDEYLAGQAAGER-ALEAGPKNALCVNH-EPGNPGLEARCKGFADAFKGAGILV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 182 LASQPADfDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQ 260
Cdd:cd06312 159 ELLDVGG-DPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGlKGKVKIGTFDLSPETLEAIKDGKILFAIDQ 237
|
..
gi 732686642 261 LP 262
Cdd:cd06312 238 QP 239
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
29-296 |
1.76e-23 |
|
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380482 [Multi-domain] Cd Length: 294 Bit Score: 97.36 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 29 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTD---SDAVgnaVKMANQ 105
Cdd:cd01540 2 IGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDqklGPAI---AAKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQ---ATKGEVVSHIASDNVLGGKIAGDYIAKKAGE---------GAKVIELQGIagtSAARERGEGFQQA 173
Cdd:cd01540 79 AGIPVIAVDDQlvdADPMKIVPFVGIDAYKIGEAVGEWLAKEMKKrgwddvkevGVLAITMDTL---SVCVDRTDGAKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 174 VAAHKF---NVLASQPADFDRIKGLNVMQNLLTAHPDVQ--AVFAQNDEMALGALRALQTAG--KSDVMVVGFDG--TPD 244
Cdd:cd01540 156 LKAAGFpedQIFQAPYKGTDTEGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAGfdAEDIIGVGIGGylAAD 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 732686642 245 GEKAVNDGKLAATIAQLPDQIGAKGVET-ADKVLKGEKVQAKYPVDLKLVVKQ 296
Cdd:cd01540 236 EEFKKQPTGFKASLYISPDKHGYIAAEElYNWITDGKPPPAETLTDGVIVTRD 288
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
50-284 |
2.51e-23 |
|
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: 96.54 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 50 KEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASD 129
Cdd:cd19991 23 KKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNADVDLYVSFD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 130 NVLGGKIAGDYIAKKAGEGAKVIeLQGIAGTSAARERGEG----FQQAVAAHKFNVLASQ-PADFDRIKGLNVMQNLLTA 204
Cdd:cd19991 103 NEKVGELQAEALVKAKPKGNYVL-LGGSPTDNNAKLFREGqmkvLQPLIDSGDIKVVGDQwVDDWDPEEALKIMENALTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 205 H-PDVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKV 282
Cdd:cd19991 182 NnNKIDAVIASNDGTAGGAIQALAEQGlAGKVAVSGQDADLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKN 261
|
..
gi 732686642 283 QA 284
Cdd:cd19991 262 EA 263
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
29-288 |
5.72e-23 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 95.41 E-value: 5.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 29 IALVVSTLN---NPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKmANQ 105
Cdd:cd01391 2 IGVVTSSLHqirEQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNL-AQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLD------RQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAgtsAARERGEGFQQAVAAHKF 179
Cdd:cd01391 81 FDIPQLALDatsqdlSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLN---SGELRMAGFKELAKQEGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 180 NVLASQPADFDRI-KGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKA--VNDGKLA 255
Cdd:cd01391 158 CIVASDKADWNAGeKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLvGDVSVIGSDGWADRDEVgyEVEANGL 237
|
250 260 270
....*....|....*....|....*....|...
gi 732686642 256 ATIAQLPDQIGAKGVETADKVLKGEKVQAKYPV 288
Cdd:cd01391 238 TTIKQQKMGFGITAIKAMADGSQNMHEEVWFDE 270
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
50-290 |
7.07e-23 |
|
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: 95.62 E-value: 7.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 50 KEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRqATKGEVVSHIASD 129
Cdd:cd19993 23 KALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDR-LIENPIAFYISFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 130 NVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERG---EGFQQAVAAHKFNVLASQPAD-FDRIKGLNVMQNLLTAH 205
Cdd:cd19993 102 NVEVGRMQARGVLKAKPEGNYVFIKGSPTDPNADFLRAgqmEVLQPAIDSGKIKIVGEQYTDgWKPANAQKNMEQILTAN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 206 P-DVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQ 283
Cdd:cd19993 182 NnKVDAVVASNDGTAGGAVAALAAQGlAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKGTKIE 261
|
....*..
gi 732686642 284 AKYPVDL 290
Cdd:cd19993 262 AIKGAAL 268
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
29-262 |
9.26e-23 |
|
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: 94.65 E-value: 9.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 29 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQN-NPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd19965 2 FVFVTHVTTNPFFQPVKKGMDDACELLGAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGE--VVSHIASDNVLGGKIAGDYIAKKAG-EGAKVIELQGIAGTSAARERGEGFQQAVAAHK----FN 180
Cdd:cd19965 82 IPVVAFNVDAPGGEnaRLAFVGQDLYPAGYVLGKRIAEKFKpGGGHVLLGISTPGQSALEQRLDGIKQALKEYGrgitYD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 181 VLASQPadfDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIA 259
Cdd:cd19965 162 VIDTGT---DLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGkVLVGGFDLVPEVLQGIKAGYIDFTID 238
|
...
gi 732686642 260 QLP 262
Cdd:cd19965 239 QQP 241
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-296 |
1.22e-22 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 94.50 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTK-ILLINPTDSDAVgnaVKMANQA 106
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDgLILVGSDHDPEL---FELLEQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDrQATKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIELqgIAGTSA----ARERGEGFQQAVAAHKFNVL 182
Cdd:cd06273 78 QVPYVLTW-SYDEDSPHPSIGFDNRAAAARAAQHLLDL---GHRRIAV--ISGPTAgndrARARLAGIRDALAERGLELP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 183 ASQ--PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndgkLAA- 256
Cdd:cd06273 152 EERvvEAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISvpeDLSITGFDDLE----------LAAh 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 732686642 257 ------TIAQLPDQIgakGVETADKV---LKGEKVQAKYPVDLKLVVKQ 296
Cdd:cd06273 222 lsppltTVRVPAREI---GELAARYLlalLEGGPPPKSVELETELIVRE 267
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
26-277 |
2.49e-22 |
|
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: 93.73 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 26 KDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINP--TDSDAVgnaVKMA 103
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTpaPSGDDI---TAKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 104 NQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIaKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFNVLA 183
Cdd:pfam00532 78 EGYGIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYL-IAEGHKRPIAVMAGPASALTARERVQGFMAALAAAGREVKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 184 SQPA--DFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG----KSDVM-----VVGFDGTPDGEKAVNDG 252
Cdd:pfam00532 157 YHVAtgDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrvkiPDIVGiginsVVGFDGLSKAQDTGLYL 236
|
250 260
....*....|....*....|....*
gi 732686642 253 KLAATIaQLPDQIgaKGVETADKVL 277
Cdd:pfam00532 237 SPLTVI-QLPRQL--LGIKASDMVY 258
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
28-286 |
3.70e-22 |
|
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: 93.00 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAvgNAVKMANQAN 107
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNN--DAYLELAQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQaTKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIEL--QGIAGTSAARERGEGFQQAVAAHKFN--VLA 183
Cdd:cd06283 79 LPVVLVDRQ-IEPLNWDTVVTDNYDATYEATEHLKEQ---GYERIVFvtEPIKGISTRRERLQGFLDALARYNIEgdVYV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 184 SQPADFDRIKglNVMQNLLTAHPDVQ-AVFAQNDEMALGALRALQTAGKS---DVMVVGFDgTPDGEKAVNDGklAATIA 259
Cdd:cd06283 155 IEIEDTEDLQ--QALAAFLSQHDGGKtAIFAANGVVLLRVLRALKALGIRipdDVGLCGFD-DWDWADLIGPG--ITTIR 229
|
250 260
....*....|....*....|....*..
gi 732686642 260 QLPDQIGAKGVETADKVLKGEKVQAKY 286
Cdd:cd06283 230 QPTYEIGKAAAEILLERIEGDSGEPKE 256
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
28-246 |
1.03e-21 |
|
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: 91.87 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD-SQNNPAKELANVQDLT---VRGtkILLINPTDSDAvgNAVKMA 103
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATvDEDDPASVREALDRLLsqrVDG--IIVIAPDEAVL--EALRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 104 NqANIPVITLDrqATKGEVVSHIASDNVLGGKIAGDYIAkkaGEGAKVIELqgIAGTS---AARERGEGFQQAVAAHKFN 180
Cdd:cd01574 77 P-PGLPVVIVG--SGPSPGVPTVSIDQEEGARLATRHLL---ELGHRRIAH--IAGPLdwvDARARLRGWREALEEAGLP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732686642 181 VLASQPADFDRIKGLNVMQNLLtAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGE 246
Cdd:cd01574 149 PPPVVEGDWSAASGYRAGRRLL-DDGPVTAVFAANDQMALGALRALHERGLRvpeDVSVVGFDDIPEAA 216
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-277 |
1.37e-21 |
|
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: 91.58 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDavGNAV-KMANQA 106
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQ--GSEAlELLEEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQaTKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIELQGI--AGTSAARERGEGFQQAVAAHKFN---- 180
Cdd:cd06282 79 GVPYVLLFNQ-TENSSHPFVSVDNRLASYDVAEYLIAL---GHRRIAMVAGdfSASDRARLRYQGYRDALKEAGLKpipi 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 181 --VLASQPADFDRIKglnvmqNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEkaVNDGKLa 255
Cdd:cd06282 155 veVDFPTNGLEEALT------SLLSGPNPPTALFCSNDLLALSVISALRRLGIRvpdDVSVIGFDGIAIGE--LLTPTL- 225
|
250 260
....*....|....*....|..
gi 732686642 256 ATIAQLPDQIgakGVETADKVL 277
Cdd:cd06282 226 ATVVQPSRDM---GRAAADLLL 244
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
28-282 |
1.43e-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: 92.31 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd19994 1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKGEVVSHIAS-DNVLGGKIAGDYIAKKA----GEGAKVIELqgIAGTSA----------ARERgegFQQ 172
Cdd:cd19994 81 IPVIAYDRLIMNTDAVDYYVTfDNEKVGELQGQYLVDKLglkdGKGPFNIEL--FAGSPDdnnaqlffkgAMEV---LQP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 173 AVAAHKFnVLASQPADFDRI--------KGLNVMQNLLTAHP----DVQAVFAQNDEMALGALRALQTAGK-SDVM--VV 237
Cdd:cd19994 156 YIDDGTL-VVRSGQTTFEQVatpdwdteTAQARMETLLSAYYtggkKLDAVLSPNDGIARGVIEALKAAGYdTGPWpvVT 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 732686642 238 GFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKV 282
Cdd:cd19994 235 GQDAEDASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEV 279
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
58-285 |
3.45e-21 |
|
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: 90.81 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 58 NLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIA 137
Cdd:cd19995 34 KVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPADYYVSFDNVAVGEAQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 138 GDYIAK----KAGEGAKVIELQGIAGTSAARERGEG----FQQAVAAHKFNVLASQPA-DFDRIKGLNVMQNLLTAHPD- 207
Cdd:cd19995 114 AQSLVDhlkaIGKKGVNIVMINGSPTDNNAGLFKKGahevLDPLGDSGELKLVCEYDTpDWDPANAQTAMEQALTKLGNn 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732686642 208 VQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQAK 285
Cdd:cd19995 194 IDGVLSANDGLAGGAIAALKAQGlAGKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGETPPSD 272
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
28-243 |
4.25e-21 |
|
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: 90.25 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDL---TVRGtkILLINPTDSDAvgnAVKMAN 104
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALlsrRPAG--LILTGTEHTPA---TRKLLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVI-TLDRQATKGEVVshIASDNVLGGKIAGDYIAKKageGAKVIelqGIAGTSA-----ARERGEGFQQAVAAHK 178
Cdd:cd01575 76 AAGIPVVeTWDLPDDPIDMA--VGFSNFAAGRAMARHLIER---GYRRI---AFVGARLdgdsrARQRLEGFRDALAEAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732686642 179 FN----VLASQPADFDRikGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTP 243
Cdd:cd01575 148 LPlplvLLVELPSSFAL--GREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRvpgDIAIAGFGDLD 217
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
38-286 |
2.04e-20 |
|
ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380517 [Multi-domain] Cd Length: 269 Bit Score: 88.41 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 38 NPFFVSLKDGAQKEADKLGYNLVvLDSQNNPAKELANVQDLtVRGTKI---LLINPTDSDAVgnaVKMANQANIPVITLD 114
Cdd:cd06294 16 NPFFSEVLRGISQVANENGYSLL-LATGNTEEELLEEVKRM-VRGRRVdgfILLYSKEDDPL---IEYLKEEGFPFVVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 115 RQATKGEVvSHIASDNVLGGKIAGDYIAKKageGAKVIELqgIAGTSAA---RERGEGFQQAVAAHKFNVLASQ--PADF 189
Cdd:cd06294 91 KPLDDNDV-LYVDNDNVQAGYEATEYLIDK---GHKRIAF--IGGDKNLvvsIDRLQGYKQALKEAGLPLDDDYilLLDF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 190 DRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKAVNdgkLAATIAQLPDQIG 266
Cdd:cd06294 165 SEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRvpeDVSIISFNNSPLAELASP---PLTSVDINPYELG 241
|
250 260
....*....|....*....|
gi 732686642 267 AKGVETADKVLKGEKVQAKY 286
Cdd:cd06294 242 REAAKLLINLLEGPESLPKN 261
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
48-293 |
2.48e-20 |
|
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: 88.88 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 48 AQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATkGEVVSHIA 127
Cdd:cd19998 25 AKQPPYADKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVVD-EPCAYNVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 128 SDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNVLASQPADFDRIKGLNVMQNLLTAHP 206
Cdd:cd19998 104 TDQAKAGEQTAQWLVDKLGGKGNILMVRGVPGTSVDRDRYEGAKEVFKKYpDIKVVAEYYGNWDDGTAQKAVADALAAHP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 207 DVQAVFAQNDEMalGALRALQTAGKsDVMVVGFDGTPDGEKAVND---GKLAATIAQLPDQIGAKGVETADKVLKGEKVQ 283
Cdd:cd19998 184 DVDGVWTQGGET--GVIKALQAAGH-PLVPVGGEAENGFRKAMLEplaNGLPGISAGSPPALSAVALKLAVAVLEGEKEP 260
|
250
....*....|
gi 732686642 284 AKYPVDLKLV 293
Cdd:cd19998 261 KTIELPLPWV 270
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
28-295 |
2.93e-20 |
|
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: 88.00 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKE---LANVQDLTVRGtkiLLINPTDSdavgnAVKMAN 104
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEreiLESLLDQNVDG---LIIEPTKS-----ALPNPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 --------QANIPVITLDRqATKGEVVSHIASDNVLGGKIAGDYIA----KKAGEGAKVIELQGIagtsaarERGEGFQQ 172
Cdd:cd01541 73 ldlyeelqKKGIPVVFINS-YYPELDAPSVSLDDEKGGYLATKHLIdlghRRIAGIFKSDDLQGV-------ERYQGFIK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 173 AVAAHKF-----NVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPD 244
Cdd:cd01541 145 ALREAGLpidddRILWYSTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRvpeDLSVVGFDDSYL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 732686642 245 GEKAvnDGKLaATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 295
Cdd:cd01541 225 ASLS--EPPL-TSVVHPKEELGRKAAELLLRMIEEGRKPESVIFPPELIER 272
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
28-296 |
6.43e-20 |
|
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: 86.92 E-value: 6.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVV-------STLNNPFFVSLKDGAQKEADKLGYNLVVLdsqnNPAKELANVQDLTVRGTK---ILLINPTDSDAVg 97
Cdd:cd06295 5 TIAVVVpmdphgdQSITDPFFLELLGGISEALTDRGYDMLLS----TQDEDANQLARLLDSGRAdglIVLGQGLDHDAL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 98 naVKMANQaNIPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAKKageGAKVIELQGIAGTSAARERGEGFQQAVAAH 177
Cdd:cd06295 80 --RELAQQ-GLPMVVWGAPEDGQSYCS-VGSDNVKGGALATEHLIEI---GRRRIAFLGDPPHPEVADRLQGYRDALAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 178 KFNVLASQ--PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndg 252
Cdd:cd06295 153 GLEADPSLllSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISvpgDVAVVGYDDIP--------- 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 732686642 253 kLAA-------TIAQLPDQIGAKGVETADKVLKGEKVQAKyPVDLKLVVKQ 296
Cdd:cd06295 224 -LAAyfrppltTVRQDLALAGRLLVEKLLALIAGEPVTSS-MLPVELVVRE 272
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
28-294 |
9.57e-20 |
|
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: 86.56 E-value: 9.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGTKILLINPTDSDavgnaVKMAN 104
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVargSAGVVLVTSDPTSRQ-----LRLLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVITLD-RQATKGEVVShIASDNVLGGKIAGDYIAkkaGEGAKVIE-LQGIAGTSAARERGEGFQQAVAAH----- 177
Cdd:cd06296 76 SAGIPFVLIDpVGEPDPDLPS-VGATNWAGGRLATEHLL---DLGHRRIAvITGPPRSVSGRARLAGYRAALAEAgiavd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 178 KFNVLASqpaDFDRIKGLNVMQNLLtAHPDV-QAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKAVndgK 253
Cdd:cd06296 152 PDLVREG---DFTYEAGYRAARELL-ELPDPpTAVFAGNDEQALGVYRAARALGLRvpdDLSVIGFDDTPPARWTS---P 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 732686642 254 LAATIAQLPDQIGAKGVETADKVLKGEKVQAKyPVDL--KLVV 294
Cdd:cd06296 225 PLTTVHQPLREMGAVAVRLLLRLLEGGPPDAR-RIELatELVV 266
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
86-266 |
1.52e-19 |
|
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: 86.24 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 86 LLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAArE 165
Cdd:cd19969 60 IAVSAIDPEALTPTINKAVDAGIPVVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQPNHE-E 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 166 RGEGFQQAVAAHK-FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTP 243
Cdd:cd19969 139 RVEGFKEAFAEYPgIEVVAVGDDNDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTgKVKIVAFDDDP 218
|
170 180
....*....|....*....|...
gi 732686642 244 DGEKAVNDGKLAATIAQLPDQIG 266
Cdd:cd19969 219 ETLDLIKDGVIDASIAQRPWMMG 241
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
28-296 |
1.88e-19 |
|
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: 85.68 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVV--LDSQNNPAKE--LANVQDLTVRGtkILLINP-TDSDAVgnaVKM 102
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVepCDSDDEDLADrlRRFLSRSRPDG--VILTPPlSDDPAL---LDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 103 ANQANIPVITLDRqATKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIEL-QGIAGTSAARERGEGFQQAVAAH--KF 179
Cdd:cd01545 76 LDELGIPYVRIAP-GTDDDRSPSVRIDDRAAAREMTRHLIAL---GHRRIGFiAGPPDHGASAERLEGFRDALAEAglPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 180 NVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndgkLAA 256
Cdd:cd01545 152 DPDLVVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRvpdDLSVAGFDDSP----------IAR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 732686642 257 -------TIAQLPDQIGAKGVET-ADKVLKGEKVQAKYPVDLKLVVKQ 296
Cdd:cd01545 222 lvwppltTVRQPIAEMARRAVELlIAAIRGAPAGPERETLPHELVIRE 269
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-242 |
4.02e-19 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 84.60 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTK--ILLINPTDSDAVGNAVkmaNQ 105
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDglILTPGDEDDPELAAAL---AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQAtkGEVVSHIASDNVLGGKIAGDYIakkAGEGAKVIEL-QGIAGTSAARERGEGFQQAVAAHKFNV--- 181
Cdd:cd06281 78 LDIPVVLIDRDL--PGDIDSVLVDHRSGVRQATEYL---LSLGHRRIALlTGGPDIRPGRERIAGFKAAFAAAGLPPdpd 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732686642 182 ---LASQPADFdrikGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGT 242
Cdd:cd06281 153 lvrLGSFSADS----GFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRipgDLSVVSIGDS 215
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
39-262 |
4.40e-19 |
|
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: 84.68 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 39 PFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQD-LTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQA 117
Cdd:cd19966 13 PFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEaIAAKPDGIAIMGHPGDGAYTPLIEAAKKAGIIVTSFNTDL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 118 TKGEVVS----HIASDNVLGGKIAGDYIAKKAG--EGAKVIELQGIAGTSAARERGEGFQQAVAAH--KFNVLASQPADF 189
Cdd:cd19966 93 PKLEYGDcglgYVGADLYAAGYTLAKELVKRGGlkTGDRVFVPGLLPGQPYRVLRTKGVIDALKEAgiKVDYLEISLEPN 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732686642 190 DRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK--SDVMVVGFDGTPDGEKAVNDGKLAATIAQLP 262
Cdd:cd19966 173 KPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKkpGEIPVAGFDLSPATVQAIKSGYVNATIDQQP 247
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
29-287 |
1.65e-18 |
|
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: 82.99 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 29 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD----SQNNPAKELANVQDLTvRGTKILLINPTDSDAVGNAVKMAN 104
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRihfvDSLDPEALAAALRRLA-AGCDGVALVAPDHPLVRAAIDELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAK-KAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH--KFNV 181
Cdd:cd06307 81 ARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRfLGRRPGKVLVILGSHRFRGHEEREAGFRSVLRERfpDLTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 182 LASQPADFDRIKGLNVMQNLLTAHPDVQAVF---AQNDemalGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAAT 257
Cdd:cd06307 161 LEVLEGLDDDELAYELLRELLARHPDLVGIYnagGGNE----GIARALREAGRArRVVFIGHELTPETRRLLRDGTIDAV 236
|
250 260 270
....*....|....*....|....*....|
gi 732686642 258 IAQLPDQIGAKGVETADKVLKGEKVQAKYP 287
Cdd:cd06307 237 IDQDPELQARRAIEVLLAHLGGKGPAPPQP 266
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
28-293 |
5.48e-18 |
|
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: 81.39 E-value: 5.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTK-ILLINPTDSDAvgnAVKMANQA 106
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDgIILFATEITDE---HRKALKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQATKGEVVSHiasDNVLGGKIAGDYIAKKageGAKVIELQGIAGT--SAARERGEGFQQAVAAHKFNVLAS 184
Cdd:cd01542 78 KIPVVVLGQEHEGFSCVYH---DDYGAGKLLGEYLLKK---GHKNIAYIGVDEEdiAVGVARKQGYLDALKEHGIDEVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 185 QPADFDRIKGLNVMQNLLTAHPDvQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEkaVNDGKLaATIAQL 261
Cdd:cd01542 152 VETDFSMESGYEAAKELLKENKP-DAIICATDNIALGAIKALRELGIKipeDISVAGFGGYDLSE--FVSPSL-TTVKFD 227
|
250 260 270
....*....|....*....|....*....|..
gi 732686642 262 PDQIGAKGVETADKVLKGEKVQAKYPVDLKLV 293
Cdd:cd01542 228 YEEAGEKAAELLLDMIEGEKVPKKQKLPYELI 259
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
125-296 |
7.12e-18 |
|
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: 82.03 E-value: 7.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 125 HIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTsAARERGEGFQQAVAAH-KFNVLASQPADFDRIKGLNVMQNLLT 203
Cdd:cd06303 136 YVGFDHAEGSRMLAKHFIKIFPEEGKYAILYLTEGY-VSDQRGDTFIDEVARHsNLELVSAYYTDFDRESAREAARALLA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 204 AHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQigaKGVETADKV---LKG 279
Cdd:cd06303 215 RHPDLDFIYACSTDIALGAIDALQELGREtDIMINGWGGGSAELDALQKGGLDVTVMRMNDD---NGIAMAEAIkldLEG 291
|
170
....*....|....*..
gi 732686642 280 EKVQAKYPVDLKLVVKQ 296
Cdd:cd06303 292 REVPTVYAGDFELVTKG 308
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
28-272 |
2.46e-17 |
|
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: 80.00 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLN----NPFFVSLKDGAQKEADKLGYNlVVLDSQNNPAKELANVQDLT----VRGtkILLINPTDSDAVGNA 99
Cdd:cd06292 1 LIGYVVPELPggfsDPFFDEFLAALGHAAAARGYD-VLLFTASGDEDEIDYYRDLVrsrrVDG--FVLASTRHDDPRVRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 100 VKmanQANIPVITLDRQATKGEVvSHIASDNVLGGKIAGDYIAKKageGAKVIEL-QGIAGTSAARERGEGFQQAVAAHK 178
Cdd:cd06292 78 LH---EAGVPFVAFGRANPDLDF-PWVDVDGAAGMRQAVRHLIAL---GHRRIGLiGGPEGSVPSDDRLAGYRAALEEAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 179 fnvLASQPA-----DFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavn 250
Cdd:cd06292 151 ---LPFDPGlvvegENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRvgrDVSVVGFDDSP------- 220
|
250 260
....*....|....*....|....*....
gi 732686642 251 dgkLAA-------TIAQLPDQIGAKGVET 272
Cdd:cd06292 221 ---LAAfthppltTVRQPIDEIGRAVVDL 246
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
36-248 |
3.35e-17 |
|
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: 79.56 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 36 LNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAkELANVQDLTVRGtkILLINPTDSDAVgnaVKMANQANIPVITLDR 115
Cdd:cd06279 14 FSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGS-AAAAVRNAAVDG--FIVYGLSDDDPA---VAALRRRGLPLVVVDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 116 QATKGevVSHIASDNVLGGKIAGDY-----------IAKKAGEGAKVIELQGIAGTSA----ARERGEGFQQAVAAHKFN 180
Cdd:cd06279 88 PAPPG--IPSVGIDDRAAARAAARHlldlghrriaiLSLRLDRGRERGPVSAERLAAAtnsvARERLAGYRDALEEAGLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732686642 181 VLASQP---ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKA 248
Cdd:cd06279 166 LDDVPVveaPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRvpeDLSVTGFDDIPEAAAA 239
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
28-245 |
4.86e-17 |
|
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: 79.13 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVST----LNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAkELANVQDLtVRGTK---ILLINPTDSDAvgnAV 100
Cdd:cd20010 1 AIGLVLPLdpgdLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGED-ELATYRRL-VERGRvdgFILARTRVNDP---RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 101 KMANQANIPVITLDRQATKGEVvSHIASDNVLGGKIAgdyIAKKAGEGAKVIEL-QGIAGTSAARERGEGFQQAVAAHKF 179
Cdd:cd20010 76 AYLLERGIPFVVHGRSESGAPY-AWVDIDNEGAFRRA---TRRLLALGHRRIALlNGPEELNFAHQRRDGYRAALAEAGL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732686642 180 NVLAS--QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDG 245
Cdd:cd20010 152 PVDPAlvREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSpgkDVSVIGHDDLLPA 222
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
28-289 |
7.86e-17 |
|
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380658 Cd Length: 298 Bit Score: 78.86 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNlVVLD--SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 105
Cdd:cd20003 1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVD-VTYDgpTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 ANIPVITLDRQATKG--EVVSHIASDNVLGgKIAGDYIAKKAGEGAKVIELQG-------IAGTSAARERgegfqQAVAA 176
Cdd:cd20003 80 KGIKVVTWDSDVNPDarDFFVNQATPEGIG-KTLVDMVAEQTGEKGKVAIVTSsptatnqNAWIKAMKAY-----IAEKY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 177 HKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQnDEMAL-GALRALQTAGKS-DVMVVGFdGTPDGEKA-VNDGK 253
Cdd:cd20003 154 PDMKIVTTQYGQEDPAKSLQVAENILKAYPDLKAIIAP-DSVALpGAAEAVEQLGRTgKVAVTGL-STPNVMRPyVKDGT 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 732686642 254 LAATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVD 289
Cdd:cd20003 232 VKSVVLWDVVDLGYLAVYVARALADGTLLKVGDFFV 267
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
7-282 |
1.84e-16 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 78.45 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 7 ATLVSAVALSATVSANAMAKdtIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD--SQNNPAKELANVQDLTVRGTK 84
Cdd:PRK10936 29 LAQRTSLQYSPLLKAKKAWK--LCALYPHLKDSYWLSVNYGMVEEAKRLGVDLKVLEagGYYNLAKQQQQLEQCVAWGAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 85 ILLINPTDSDAVGNAVKMAnQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEG---AKVIELQGIAGTS 161
Cdd:PRK10936 107 AILLGAVTPDGLNPDLELQ-AANIPVIALVNGIDSPQVTTRVGVSWYQMGYQAGRYLAQWHPKGskpLNVALLPGPEGAG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 162 AARERGEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVF--AQNDEMALGALRALQTAGKsdVMVVGF 239
Cdd:PRK10936 186 GSKAVEQGFRAAIAGSDVRIVDIAYGDNDKELQRNLLQELLERHPDIDYIAgsAVAAEAAIGELRGRNLTDK--IKLVSF 263
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 732686642 240 DGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKV 282
Cdd:PRK10936 264 YLSHQVYRGLKRGKVLAAPSDQMVLQGRLAIDQAVRQLEGAPV 306
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
28-271 |
5.85e-16 |
|
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: 75.96 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVV--LDSQNNPAKELANVqdLTVRGTKILLINPTDSDAVGNAVKMANQ 105
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIfpLLSEYRLEKYLRNS--TLAYQCDGLVMASLDLTELFEEVIVPTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 106 AniPVITLDRQAtkgEVVSHIASDNVLGGKIAGDYIAKKaGEG---AKVIELQGIAGTSAARERGEGFQQAVAAHKFNVL 182
Cdd:cd06297 79 K--PVVLIDANS---MGYDCVYVDNVKGGFMATEYLAGL-GEReyvFFGIEEDTVFTETVFREREQGFLEALNKAGRPIS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 183 ASQP--ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGTPDGEKAVndgklAAT 257
Cdd:cd06297 153 SSRMfrIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLrvgEDVAVIGFDGQPWAASPG-----LTT 227
|
250
....*....|....
gi 732686642 258 IAQLPDQIGAKGVE 271
Cdd:cd06297 228 VRQPVEEMGEAAAK 241
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
37-240 |
6.72e-16 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 75.74 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 37 NNPFFVSLKDGAQKEADKLGYNL--VVLDSQNNPAKELANVQDLTVRGTkILLINPTDSDAVgnavKMANQANIPVITLD 114
Cdd:cd06277 17 ETPFFSELIDGIEREARKYGYNLliSSVDIGDDFDEILKELTDDQSSGI-ILLGTELEEKQI----KLFQDVSIPVVVVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 115 RQAtkgEVVS--HIASDNVLGGKIAGDYIAKKageGAKVIE-LQGIAGTSAARERGEGFQQAVAAHKFnvlasqPADFDR 191
Cdd:cd06277 92 NYF---EDLNfdCVVIDNEDGAYEAVKYLVEL---GHTRIGyLASSYRIKNFEERRRGFRKAMRELGL------SEDPEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732686642 192 IKGLNV--------MQNLLTAHPDV-QAVFAQNDEMALGALRALQTAGKS---DVMVVGFD 240
Cdd:cd06277 160 EFVVSVgpegaykdMKALLDTGPKLpTAFFAENDIIALGCIKALQEAGIRvpeDVSVIGFD 220
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
28-295 |
9.15e-16 |
|
ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to CcpA which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree.
Pssm-ID: 380509 [Multi-domain] Cd Length: 262 Bit Score: 75.27 E-value: 9.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTvrgTKIL--LI-----NPTDsdavgnaV 100
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLK---TKQIdgLIitsreNDWE-------V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 101 KMANQANIPVITLDRqaTKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIelqGIA------GTSAARERGEGFQQAV 174
Cdd:cd06286 71 IEPYAKYGPIVLCEE--TDSPDIPSVYIDRYEAYLEALEYLKEK---GHRKI---GYClgrpesSSASTQARLKAYQDVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 175 AAHKfnvLASQPAD-FDRIK----GLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGE 246
Cdd:cd06286 143 GEHG---LSLREEWiFTNCHtiedGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRvpeDLAVIGFDNQPISE 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 732686642 247 kAVNdgklAATIAQLPDQIGAKGVETADKVLKGEKVQaKYPVDLKLVVK 295
Cdd:cd06286 220 -LLN----LTTIDQPLEEMGKEAFELLLSQLESKEPT-KKELPSKLIER 262
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
28-243 |
8.91e-15 |
|
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: 72.56 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVST-----LNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANvqdlTVRGtkILLINPTDSDAVgNAVKM 102
Cdd:cd01544 1 TIGIIQWYseeeeLEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLESLLE----KVDG--IIAIGKFSKEEI-EKLKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 103 ANQ-----------ANIPVITLD-RQATKgEVVSHIASdnvLG-GKIAgdYIAKKAGEGAKVIELQGIagtsaaRERGeg 169
Cdd:cd01544 74 LNPnivfvdsnpdpDGFDSVVPDfEQAVR-QALDYLIE---LGhRRIG--FIGGKEYTSDDGEEIEDP------RLRA-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 170 FQQAVAAH----KFNVLAsqpADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGT 242
Cdd:cd01544 140 FREYMKEKglynEEYIYI---GEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKvpeDISIISFNDI 216
|
.
gi 732686642 243 P 243
Cdd:cd01544 217 E 217
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
52-296 |
3.67e-14 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 71.56 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 52 ADKLGYNLVV--LDSQNNPAKELAnVQDLTVRGTKILLIN-PTDSDavgNAVKMANQ-ANIPVITLDRQATKgeVVSHIA 127
Cdd:PRK09526 89 ADQLGYSVVIsmVERSGVEACQAA-VNELLAQRVSGVIINvPLEDA---DAEKIVADcADVPCLFLDVSPQS--PVNSVS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 128 SDNVLGGKIAGDYIAkkAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPD 207
Cdd:PRK09526 163 FDPEDGTRLGVEHLV--ELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQPIAVREGDWSAMSGYQQTLQMLREGPV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 208 VQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDgeKAVNDGKLaATIAQLPDQIGAKGVETADKVLKGEKVQA 284
Cdd:PRK09526 241 PSAILVANDQMALGVLRALHESGLRvpgQISVIGYDDTED--SSYFIPPL-TTIKQDFRLLGKEAVDRLLALSQGQAVKG 317
|
250
....*....|..
gi 732686642 285 KYPVDLKLVVKQ 296
Cdd:PRK09526 318 SQLLPTSLVVRK 329
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
28-282 |
4.75e-14 |
|
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: 71.17 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEA-----DKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKM 102
Cdd:cd19997 1 VIALSNSYAGNTWRQQMVDAFEEAAkkakaDGLIADYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 103 ANQANIPVITLDRQATKgEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAH-KFNV 181
Cdd:cd19997 81 ACDAGIKVVVFDSGVTE-PCAYILNNDFEDYGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKKYpDLKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 182 LASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEmALGALRALQTAGKsDVMVVGFDGTPDGEK---AVNDGKLAATI 258
Cdd:cd19997 160 VAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGD-GYGAAQAFEAAGR-PLPIIIGGNRGEFLKwwqEEYAKNGYETV 237
|
250 260
....*....|....*....|....*
gi 732686642 259 AQLPDQ-IGAKGVETADKVLKGEKV 282
Cdd:cd19997 238 SVSTDPgQGSAAFWVALDILNGKDV 262
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
11-240 |
6.80e-14 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 70.91 E-value: 6.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 11 SAVALSATVSANamakDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLI-- 88
Cdd:PRK10703 48 SAVARSLKVNHT----KSIGLLATSSEAPYFAEIIEAVEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVmc 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 89 --NPTDSDAVgnavkMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIElqGIAGTSAARER 166
Cdd:PRK10703 124 seYPEPLLAM-----LEEYRHIPMVVMDWGEAKADFTDAIIDNAFEGGYLAGRYLIERGHRDIGVIP--GPLERNTGAGR 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732686642 167 GEGFQQAVAAHKFNVLAS--QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFD 240
Cdd:PRK10703 197 LAGFMKAMEEANIKVPEEwiVQGDFEPESGYEAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGlrvPQDISVIGYD 275
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
151-284 |
1.33e-13 |
|
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: 66.98 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 151 VIELQGIAGTSAARERGEGFQQAVAAHKFNVLASQ--PADFDRIKGLNVMQNLLTAHPDvqAVFAQNDEMALGALRALQT 228
Cdd:pfam13377 12 LIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLyaGDDEAEAAAARERLRWLGALPT--AVFVANDEVALGVLQALRE 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 732686642 229 AGKS---DVMVVGFDGTPDGEKAVNDgklAATIAQLPDQIGAKGVETADKVLKGEKVQA 284
Cdd:pfam13377 90 AGLRvpeDLSVIGFDDSPLAALVSPP---LTTVRVDAEELGRAAAELLLDLLNGEPAPP 145
|
|
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
3-258 |
3.51e-13 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 68.60 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 3 MKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKL-GYNLVVLDSQNNPAKELANVQDLTVR 81
Cdd:PRK15395 1 NKKVLTLSALMASMLFGAAAAAADTRIGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 82 GTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSH-----IASDNVLGGKIAGDYIAK-----------KA 145
Cdd:PRK15395 81 GVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYdkayyVGTDSKESGIIQGDLIAKhwkanpawdlnKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 146 GEGAKVIeLQGIAGTSAARERGEGFQQAVAAH--KFNVLASQPADFDRIKGLNVMQNLLTAHP--DVQAVFAQNDEMALG 221
Cdd:PRK15395 161 GKIQYVL-LKGEPGHPDAEARTTYVIKELNDKgiKTEQLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMG 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 732686642 222 ALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATI 258
Cdd:PRK15395 240 AVEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTV 276
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
3-284 |
6.02e-13 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 68.23 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 3 MKKLATLVSAVALSATVSANAMAKD-TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVR 81
Cdd:PRK10355 1 MKIKNILLTLCASLLLTSVAAHAKEvKIGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQMSQIENMINR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 82 GTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIeLQGIAGTS 161
Cdd:PRK10355 81 GVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDFYISFDNEKVGELQAKALVDKVPQGNYFL-MGGSPVDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 162 AARERGEG----FQQAVAAHKFNVLASQPAD-FDRIKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAGKS-DV 234
Cdd:PRK10355 160 NAKLFRAGqmkvLKPYIDSGKIKVVGDQWVDgWLPENALKIMENALTANNNkIDAVVASNDATAGGAIQALSAQGLSgKV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 732686642 235 MVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQA 284
Cdd:PRK10355 240 AISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKA 289
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
28-227 |
1.80e-12 |
|
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
Pssm-ID: 380498 [Multi-domain] Cd Length: 264 Bit Score: 66.08 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLI----NPTDSDAVGNAvkma 103
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVapstPPDDIYYLCQA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 104 nqANIPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAkkAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKF---- 179
Cdd:cd06274 77 --AGLPVVFLDRPFSGSDAPS-VVSDNRAGARALTEKLL--AAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGItegd 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 732686642 180 -NVLASqpaDFDRIKGLNVMQNLLTAHPDV-QAVFAQNDEMALGALRALQ 227
Cdd:cd06274 152 dWILAE---GYDRESGYQLMAELLARLGGLpQALFTSSLTLLEGVLRFLR 198
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-272 |
1.81e-10 |
|
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: 380629 [Multi-domain] Cd Length: 270 Bit Score: 60.26 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVS---TLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKEL---ANVQDLTVRGtkILLINPTDSDAVgnavK 101
Cdd:cd19974 1 NIAVLIPerfFGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELnlpSIISEEKVDG--IIILGEISKEYL----E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 102 MANQANIPVITLDRQATKGEVvSHIASDNVLGGKIAGDYIAKKageGAKVIelqGIAG----TSAARERGEGFQQAVAAH 177
Cdd:cd19974 75 KLKELGIPVVLVDHYDEELNA-DSVLSDNYYGAYKLTSYLIEK---GHKKI---GFVGdinyTSSFMDRYLGYRKALLEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 178 KfnvLASQPADF---DRIKGLNVMQNLLTA----HPDvqAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgEK 247
Cdd:cd19974 148 G---LPPEKEEWlleDRDDGYGLTEEIELPlklmLPT--AFVCANDSIAIQLIKALKEKGYRvpeDISVVGFDNIE--LA 220
|
250 260
....*....|....*....|....*
gi 732686642 248 AVNDGKLaATIAQLPDQIGAKGVET 272
Cdd:cd19974 221 ELSTPPL-TTVEVDKEAMGRRAVEQ 244
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
28-243 |
7.31e-10 |
|
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380521 [Multi-domain] Cd Length: 268 Bit Score: 58.46 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDL---TVRGtkILLINPTDSDavgNAVKMAN 104
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMlskQVDG--IIFMGDELTE---EIREEFK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QANIPVI---TLDRQATkgevvshIASDNVLGGKIAGDYIAKKAGEGAKVIEL-QGIAGTSAARERGE-GFQQAV--AAH 177
Cdd:cd06298 76 RSPVPVVlagTVDSDHE-------IPSVNIDYEQAAYDATKSLIDKGHKKIAFvSGPLKEYINNDKKLqGYKRALeeAGL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732686642 178 KFN---VLAsqpADFDRIKGLNVMQNLLTA-HPDvqAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTP 243
Cdd:cd06298 149 EFNeplIFE---GDYDYDSGYELYEELLESgEPD--AAIVVRDEIAVGLLNAAQDRGLKvpeDLEIIGFDNTR 216
|
|
| PRK15408 |
PRK15408 |
autoinducer 2 ABC transporter substrate-binding protein LsrB; |
3-291 |
1.31e-08 |
|
autoinducer 2 ABC transporter substrate-binding protein LsrB;
Pssm-ID: 237961 Cd Length: 336 Bit Score: 55.19 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 3 MKKLATLVSAVALsATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNlVVLDSQNNP--AKELANVQDLTV 80
Cdd:PRK15408 1 RKKKIALVSALGI-ALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVD-VTYDGPTEPsvSGQVQLINNFVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 81 RGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQaTKGEVVSHIASD---NVLGG---KIAGDYIAKKAgegAKVIEL 154
Cdd:PRK15408 79 QGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSD-TKPECRSYYINQgtpEQLGSmlvEMAAKQVGKDK---AKVAFF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 155 QGIAGTSAARERGEGFQQAVAAH--KFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS 232
Cdd:PRK15408 155 YSSPTVTDQNQWVKEAKAKIAKEhpGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRD 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732686642 233 DVMVVGFDgTPDGEKA-VNDGklaaTIAQ--LPD--QIGAKGVETADKVLKGEKVQAKYPVDLK 291
Cdd:PRK15408 235 KVAIVGFS-TPNVMRPyVKRG----TVKEfgLWDvvQQGKISVYVANELLKKGKLNVGDSLDVP 293
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
29-246 |
2.76e-08 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 54.33 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 29 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQaNI 108
Cdd:PRK10014 67 IGLIVRDLSAPFYAELTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMAEEK-GI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 109 PVITLDRqATKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIELQGIAGTSAAR-ERGEGF-----QQAVAAHKFNVL 182
Cdd:PRK10014 146 PVVFASR-ASYLDDVDTVRPDNMQAAQLLTEHLIRN---GHQRIAWLGGQSSSLTRaERVGGYcatllKFGLPFHSEWVL 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732686642 183 ---ASQPADFDrikglnVMQNLLTAHPDVQAVFAQNDEMALGA----LRALQTAGKSD--------VMVVGFDGTPDGE 246
Cdd:PRK10014 222 ectSSQKQAAE------AITALLRHNPTISAVVCYNETIAMGAwfglLRAGRQSGESGvdryfeqqVALAAFTDVPEAE 294
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
28-280 |
7.77e-08 |
|
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: 52.64 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD-SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd20000 1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGpTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQATKGEVVSHIASDNVLG-GKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKF---NVL 182
Cdd:cd20000 81 GIKVVTFDSDVAPEARDLFVNQADADGiGRAQVDMMAELIGGEGEFAILSATPTATNQNAWIDAMKKELASPEYagmKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 183 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFdGTPDGEKA-VNDGKLAATIAQ 260
Cdd:cd20000 161 KVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGkVKVTGL-GLPSEMAKyVKDGTVPAFALW 239
|
250 260
....*....|....*....|
gi 732686642 261 LPDQIGAKGVETADKVLKGE 280
Cdd:cd20000 240 NPIDLGYLAAYAAAALAQGE 259
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
28-282 |
1.10e-07 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380656 Cd Length: 296 Bit Score: 52.28 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD-SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd20001 1 TIAVVVKVTGIAWFDRMETGVEQFAKDTGVNVYQIGpATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITldrqatkgevvsHIAS------------DNVLGGKIAGDYIAKKAGEGAKVIelqGIAGTSAARERGEGFQQAV 174
Cdd:cd20001 81 GIVVIT------------HEASnlknvdydveafDNAAYGAFIMDKLAEAMGGKGKYV---TFVGSLTSTSHMEWANAAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 175 AAHKFN------VLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFdGTPDGEK 247
Cdd:cd20001 146 AYQKANypdmllVTDRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGkIAVVGT-GLPSVAG 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 732686642 248 A-VNDGKLAATIAQLPDQIGAKGVETADKVLKGEKV 282
Cdd:cd20001 225 EyLEDGTIDYIQFWDPADAGYAMNALAVMVLEGEKI 260
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
28-281 |
1.57e-07 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380657 Cd Length: 295 Bit Score: 51.55 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD-SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 106
Cdd:cd20002 1 TIVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVGpADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 107 NIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFN---VLA 183
Cdd:cd20002 81 GIVVITHESPGQKGADWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKYPNmkqVTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 184 SQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQLP 262
Cdd:cd20002 161 RIPGGEDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGlKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDP 240
|
250
....*....|....*....
gi 732686642 263 DQIGAKGVETADKVLKGEK 281
Cdd:cd20002 241 ADAGYAMVYIAKMLLDGKR 259
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
58-230 |
2.56e-07 |
|
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];
Pssm-ID: 440447 [Multi-domain] Cd Length: 314 Bit Score: 51.09 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 58 NLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVIT-------LDRQATKGEVVSHIASDN 130
Cdd:COG0683 46 ELVVEDDASDPDTAVAAARKLIDQDKVDAIVGPLSSGVALAVAPVAEEAGVPLISpsatapaLTGPECSPYVFRTAPSDA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 131 VLgGKIAGDYIAKKAGeGAKV--IELQGIAGTSAArergEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDV 208
Cdd:COG0683 126 QQ-AEALADYLAKKLG-AKKValLYDDYAYGQGLA----AAFKAALKAAGGEVVGEEYYPPGTTDFSAQLTKIKAAGPDA 199
|
170 180
....*....|....*....|..
gi 732686642 209 qAVFAQNDEMALGALRALQTAG 230
Cdd:COG0683 200 -VFLAGYGGDAALFIKQAREAG 220
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
103-240 |
2.88e-06 |
|
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); Ligand-binding domain of DNA transcription repressor specific for xylose (XylR), a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of XylR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380485 [Multi-domain] Cd Length: 265 Bit Score: 47.58 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 103 ANQANIPVITLDRqATKGEVVSHIASDNVLGGKIAGDYIakkagegakvIELQ-------GIAGTSAARERGEGFQQAVA 175
Cdd:cd01543 67 LRRLGIPVVNVSG-SRPEPGFPRVTTDNEAIGRMAAEHL----------LERGfrhfafcGFRNAAWSRERGEGFREALR 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732686642 176 AHKFNVLASQPADFDRIKGLNVMQNLLTA------HPdVqAVFAQNDEMALGALRALQTAGKS---DVMVVGFD 240
Cdd:cd01543 136 EAGYECHVYESPPSGSSRSWEEEREELADwlkslpKP-V-GIFACNDDRARQVLEACREAGIRvpeEVAVLGVD 207
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
28-244 |
3.39e-06 |
|
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380495 [Multi-domain] Cd Length: 264 Bit Score: 47.42 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVS---TLNNPFFVSLKDGAQKEADKLGYNLVVLDSQnnPAKELANVQDLT----VRGTKILLINPTDSdavgnAV 100
Cdd:cd06271 1 VIALVFPvteTELNGTVSE*VSGITEEAGTTGYHLLVWPFE--EAES*VPIRDLVetgsADGVILSEIEPNDP-----RV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 101 KMANQANIPVITLDRQATkGEVVSHIASDNVLGGKIAGDYIAkkaGEGAKVIELQGI-AGTSAARERGEGFQQAVAAHKF 179
Cdd:cd06271 74 QFLTKQNFPFVAHGRSD*-PIGHAWVDIDNEAGAYEAVERLA---GLGHRRIAFIVPpARYSPHDRRLQGYVRA*RDAGL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732686642 180 NVLAsQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDGTPD 244
Cdd:cd06271 150 TGYP-LDADTTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGlkiGEDVSIIGKDSAPF 216
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
21-243 |
4.66e-06 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 47.46 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 21 ANAMA-----KDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINptdSDA 95
Cdd:PRK10401 49 ANAQAlatqvSDTIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVH---SKA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 96 VGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKkagEGAKVIelqGIAGTSAARE----RGEGFQ 171
Cdd:PRK10401 126 LSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDNVSGARMATRMLLN---NGHQRI---GYLSSSHGIEddamRRAGWM 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732686642 172 QAVAAHKFNVLASQPA--DFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTP 243
Cdd:PRK10401 200 SALKEQGIIPPESWIGtgTPDMQGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAiplHLSIIGFDDIP 276
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
28-213 |
4.91e-06 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 47.18 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLIN---PTDSDAVgnaVKMAN 104
Cdd:PRK11303 63 SIGLIIPDLENTSYARIAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVStslPPEHPFY---QRLQN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 105 QAnIPVITLDRqATKGEVVSHIASDNVLGGKIAGDYIAKKAGE-----GAkVIELqgiagtSAARERGEGFQQAVAAHKF 179
Cdd:PRK11303 140 DG-LPIIALDR-ALDREHFTSVVSDDQDDAEMLAESLLKFPAEsilllGA-LPEL------SVSFEREQGFRQALKDDPR 210
|
170 180 190
....*....|....*....|....*....|....
gi 732686642 180 NVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFA 213
Cdd:PRK11303 211 EVHYLYANSFEREAGAQLFEKWLETHPMPDALFT 244
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
10-296 |
3.40e-05 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 44.60 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 10 VSAVALSATVSANAMAKD-------TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVqDLTVrg 82
Cdd:PRK11041 12 VEQAVLEVGYSPQSLGRNlkrnesrTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFV-NLII-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 83 TK----ILLIN---PTDsdavgnaVKMANQANIPVITLDRQ-ATKGEVVS-HIasDNVLGGKIAGDYIAKKageGAKVIE 153
Cdd:PRK11041 89 TKqidgMLLLGsrlPFD-------ASKEEQRNLPPMVMANEfAPELELPTvHI--DNLTAAFEAVNYLHEL---GHKRIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 154 LqgIAGTSAA---RERGEGFQQAVAAHKFNVLASQPA--DFDRIKGLNVMQNLLtAHPDV-QAVFAQNDEMALGALRALQ 227
Cdd:PRK11041 157 C--IAGPEEMplcHYRLQGYVQALRRCGITVDPQYIArgDFTFEAGAKALKQLL-DLPQPpTAVFCHSDVMALGALSQAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 228 TAG---KSDVMVVGFDgtpdgekavnDGKLA-------ATIAQLPDQIGAKGVETADKVLKGEKVQA-KYPVDLKLVVKQ 296
Cdd:PRK11041 234 RMGlrvPQDLSIIGFD----------DIDLAqycdpplTTVAQPRYEIGREAMLLLLEQLQGHHVSSgSRLLDCELIIRG 303
|
|
| PBP1_ABC_transporter_LIVBP-like |
cd06268 |
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ... |
28-255 |
9.43e-05 |
|
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily; Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.
Pssm-ID: 380492 [Multi-domain] Cd Length: 298 Bit Score: 43.08 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVV--STLNNPFFVSLKDG---AQKEADKLG------YNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAV 96
Cdd:cd06268 1 KIGVVVplTGPYADYGEEILRGvalAVEEINAAGgingrkLELVIADDQGDPETAVAVARKLVDDDKVLAVVGHYSSSVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 97 GNAVKMANQANIPVITL-----DRQATKGEVVSHIASDNVLGGKIAGDYIAKKaGEGAKVIEL--QGIAGTSAArergEG 169
Cdd:cd06268 81 LAAAPIYQEAGIPLISPgstapELTEGGGPYVFRTVPSDAMQAAALADYLAKK-LKGKKVAILydDYDYGKSLA----DA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 170 FQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALgALRALQTAGKsDVMVVGFDGTPDGEKAV 249
Cdd:cd06268 156 FKKALKALGGEIVAEEDFPLGTTDFSAQLTKIKAAGPDVLFLAGYGADAAN-ALKQARELGL-KLPILGGDGLYSPELLK 233
|
....*.
gi 732686642 250 NDGKLA 255
Cdd:cd06268 234 LGGEAA 239
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
86-283 |
1.46e-04 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 42.41 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 86 LLINPTDSDAvgnAVKMANQANIPVITLDRQATKGEVVSHIasdNVLGGKIAGDYIAKKAGEGAKVIEL-QGIAGTSAAR 164
Cdd:cd06287 61 IVVEPTVEDP---ILARLRQRGVPVVSIGRAPGTDEPVPYV---DLQSAATARLLLEHLHGAGARQVALlTGSSRRNSSL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 165 ERGEGFQQAVAAHKFN-VLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVgfd 240
Cdd:cd06287 135 ESEAAYLRFAQEYGTTpVVYKVPESEGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSvpeDLMVV--- 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 732686642 241 GTPDGEKA-VNDGKLAATIAQLpDQIGAKGVETADKVLKGEKVQ 283
Cdd:cd06287 212 TRYDGIRArTADPPLTAVDLHL-DRVARTAIDLLFASLSGEERS 254
|
|
| PBP1_ABC_ligand_binding-like |
cd06343 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
58-255 |
4.96e-04 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however its ligand specificity has not been determined experimentally.
Pssm-ID: 380566 [Multi-domain] Cd Length: 355 Bit Score: 41.01 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 58 NLVVLDSQNNPAKELANVQDLTVRGtKILLINPTDSDAVGNAV-KMANQANIPVITLDRQATKGEVVSH-----IASDNV 131
Cdd:cd06343 49 ELIVEDDGYDPARAVAAVRKLVEQD-KVFAIVGGLGTPTNLAVrPYLNEAGVPQLFPATGASALSPPPKpytfgVQPSYE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 132 LGGKIAGDYIAKKAGeGAKVielqGIAG--TSAARERGEGFQQAVAAHKFNVLASQP-----ADFDrikglNVMQNLLTA 204
Cdd:cd06343 128 DEGRILADYIVETLP-AAKV----AVLYqnDDFGKDGLEGLKEALKAYGLEVVAEETyepgdTDFS-----SQVLKLKAA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 732686642 205 HPDVQAVFAQNDEmALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLA 255
Cdd:cd06343 198 GADVVVLGTLPKE-AAAALKEAAKLGWKPTFLGSSVSADPTTLAKAGGDAA 247
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
59-230 |
5.30e-04 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 41.10 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 59 LVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVIT---LDRQATKGEVVSHIASDNVLgGK 135
Cdd:pfam13458 45 LVVADDQGDPDVAAAAARRLVDQDGVDAIVGGVSSAVALAVAEVLAKKGVPVIGpaaLTGEKCSPYVFSLGPTYSAQ-AT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 136 IAGDYIAKKAGeGAKVIELQgiAGTSAARERGEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVqaVFAQN 215
Cdd:pfam13458 124 ALGRYLAKELG-GKKVALIG--ADYAFGRALAAAAKAAAKAAGGEVVGEVRYPLGTTDFSSQVLQIKASGADA--VLLAN 198
|
170
....*....|....*.
gi 732686642 216 D-EMALGALRALQTAG 230
Cdd:pfam13458 199 AgADTVNLLKQAREAG 214
|
|
| PBP1_ABC_sugar_binding-like |
cd06315 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-152 |
5.44e-04 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380538 Cd Length: 278 Bit Score: 40.79 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 107
Cdd:cd06315 2 TIAYVASDLRNGGVLGVGRGVKEAAAALGWKVDVLDGGGTVTGRLAALNQALALKPDGIILGGDDAVELQEPLKKAVKAG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 732686642 108 IPVITLDRQATKG-----EVVSHIASDNVLGGKIAGDYIAKKAGEGAKVI 152
Cdd:cd06315 82 IPVVGWHAAASPGpipelGLFTNITTDPREVAETAAALVIAQSGGKAGVV 131
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
28-243 |
5.85e-04 |
|
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380496 [Multi-domain] Cd Length: 266 Bit Score: 40.82 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTLNNPFFVS-LKDGAQKEADKLGYNLVVLDSQNNP-----AKELANvqDLTVRGtkILLINPTDSDAVGNAVk 101
Cdd:cd06272 1 TIGLYWPSVGERVALTrLLSGINEAISKQGYNINLSICPYKVghlctAKGLFS--ENRFDG--VIVFGISDSDIEYLNK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 102 maNQANIPVITLDRQATKgevVSHIASDNVLGGKIAGDYIAKKageGAKVIELQG-IAGTSAARERGEGFQQAVAAHKFN 180
Cdd:cd06272 76 --NKPKIPIVLYNRESPK---YSTVNVDNEKAGRLAVLLLIQK---GHKSIAYIGnPNSNRNQTLRGKGFIETCEKHGIH 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732686642 181 VLAS--QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTP 243
Cdd:cd06272 148 LSDSiiDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISipeDISIVSYDNIP 215
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
28-143 |
3.67e-03 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 38.35 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732686642 28 TIALVVSTlNNPFFVSLKDGAQKEADKLGYNLVVLDSQNnpAKELANVQDLTVRGTKILLInPTDSDAVGNA---VKMAN 104
Cdd:COG2984 134 RIGVLYNP-SEANSVAQVEELKKAAKKLGLELVEATVTS--SNEIQQALQSLAGKVDAIYV-PTDNTVVSALeaiAKVAA 209
|
90 100 110
....*....|....*....|....*....|....*....
gi 732686642 105 QANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAK 143
Cdd:COG2984 210 RAKIPVFGGDDSSVKAGALAGYGIDYYELGRQAAEMALR 248
|
|
| |
