|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-270 |
0e+00 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 529.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 1 KDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:PRK10653 26 KDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHKFNVLASQ 160
Cdd:PRK10653 106 ANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIAKKLGEGAKVIQLEGIAGTSAARERGEGFKQAVAAHKFNVLASQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQI 240
Cdd:PRK10653 186 PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQI 265
|
250 260 270
....*....|....*....|....*....|
1DRK_A 241 GAKGVETADKVLKGEKVQAKYPVDLKLVVK 270
Cdd:PRK10653 266 GAIGVETADKVLKGEKVEAKIPVDLKLVTK 295
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
3-269 |
9.60e-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: 406.30 E-value: 9.60e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQP 161
Cdd:cd06323 81 IPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAKYpKINVVASQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 162 ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIG 241
Cdd:cd06323 161 ADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQPEEMG 240
|
250 260
....*....|....*....|....*...
1DRK_A 242 AKGVETADKVLKGEKVQAKYPVDLKLVV 269
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 ... |
3-267 |
2.11e-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: 2.11e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQAT-KGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQ 160
Cdd:cd01536 81 IPVVAVDTDIDgGGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYpDIEIVAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQ 239
Cdd:cd01536 161 PANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTgDIKIVGVDGTPEALKAIKDGELDATVAQDPYL 240
|
250 260
....*....|....*....|....*...
1DRK_A 240 IGAKGVETADKVLKGEKVQAKYPVDLKL 267
Cdd:cd01536 241 QGYLAVEAAVKLLNGEKVPKEILTPVTL 268
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
1-270 |
2.40e-91 |
|
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: 272.57 E-value: 2.40e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 1 KDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:COG1879 33 GKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLAS 159
Cdd:COG1879 113 AGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANERTDGFKEALKEYpGIKVVAE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPD 238
Cdd:COG1879 193 QYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKgDVKVVGFDGSPEALQAIKDGTIDATVAQDPY 272
|
250 260 270
....*....|....*....|....*....|..
1DRK_A 239 QIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 270
Cdd:COG1879 273 LQGYLAVDAALKLLKGKEVPKEILTPPVLVTK 304
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
3-268 |
8.56e-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: 241.68 E-value: 8.56e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADK-LGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKyPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQ 160
Cdd:cd06308 81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYpGIKIVASQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPD-GEKAVNDGKLAATIaqLPD 238
Cdd:cd06308 161 DGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGLPEaGEKAVKDGILAATF--LYP 238
|
250 260 270
....*....|....*....|....*....|
1DRK_A 239 QIGAKGVETADKVLKGEKVQAKYPVDLKLV 268
Cdd:cd06308 239 TGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
3-268 |
1.12e-77 |
|
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: 236.73 E-value: 1.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQAT---KGEVVSHIASDNVLGGKIAGDYIAKKAGEG-AKVIELQGTAATSAARERGEGFQQAVAAH-KFNVL 157
Cdd:cd06309 81 IPVILVDRTIDgedGSLYVTFIGSDFVEEGRRAAEWLVKNYKGGkGNVVELQGTAGSSVAIDRSKGFREVIKKHpNIKIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 158 ASQPADFDRIKGLNVMQNLLTAHP-DVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKAVNDGKLAATI 233
Cdd:cd06309 161 ASQSGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLKpgkDVLVVGIDGQKDALEAIKAGELNATV 240
|
250 260 270
....*....|....*....|....*....|....*
1DRK_A 234 AQLPDQiGAKGVETADKVLKGEKVQAKYPVDLKLV 268
Cdd:cd06309 241 ECNPLF-GPTAFDTIAKLLAGEKVPKLIIVEERLF 274
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
3-268 |
1.21e-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: 228.75 E-value: 1.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQ-ATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQ 160
Cdd:cd19967 81 IPVFLIDREiNAEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQYpELKMVAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQ 239
Cdd:cd19967 161 SADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRAgDVIIVGFDGSNDVRDAIKEGKISATVLQPAKL 240
|
250 260 270
....*....|....*....|....*....|.
1DRK_A 240 IGAKGVETADKVLKGEK--VQAKYPVDLKLV 268
Cdd:cd19967 241 IARLAVEQADQYLKGGStgKEEKQLFDCVLI 271
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
3-267 |
1.11e-73 |
|
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: 225.93 E-value: 1.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGE-VVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSaARERGEGFQQAVAAH-KFNVLASQ 160
Cdd:cd19971 81 IPVINVDTPVKDTDlVDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLDHPTAES-CVDRIDGFLDAIKKNpKFEVVAQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQ 239
Cdd:cd19971 160 DGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKlGDILVYGVDGSPDAKAAIKDGKMTATAAQSPIE 239
|
250 260
....*....|....*....|....*...
1DRK_A 240 IGAKGVETADKVLKGEKVQAKYPVDLKL 267
Cdd:cd19971 240 IGKKAVETAYKILNGEKVEKEIVVPTFL 267
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
3-269 |
9.69e-73 |
|
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: 223.69 E-value: 9.69e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQP 161
Cdd:cd06322 81 IPVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKALLGGGGKIAIIDYPEVESVVLRVNGFKEAIKKYpNIEIVAEQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 162 ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVN-DGKLAATIAQLPDQ 239
Cdd:cd06322 161 GDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDkIKVIGFDGNPEAIKAIAkGGKIKADIAQQPDK 240
|
250 260 270
....*....|....*....|....*....|
1DRK_A 240 IGAKGVETADKVLKGEKVQAKYPVDLKLVV 269
Cdd:cd06322 241 IGQETVEAIVKYLAGETVEKEILIPPKLYT 270
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
3-268 |
4.57e-72 |
|
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: 222.26 E-value: 4.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQP 161
Cdd:cd19968 81 IPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAAGpKIKVVFEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 162 ADFDRIKGLNVMQNLLTAHP-DVQAVFAQNDEMALGALRALQTAG--KSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPD 238
Cdd:cd19968 161 GNFERDEGLTVMENILTSLPgPPDAIICANDDMALGAIEAMRAAGldLKKVKVIGFDAVPDALQAIKDGELYATVEQPPG 240
|
250 260 270
....*....|....*....|....*....|
1DRK_A 239 QIGAKGVETADKVLKGEKVQAKYPVDLKLV 268
Cdd:cd19968 241 GQARTALRILVDYLKDKKAPKKVNLKPKLI 270
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
4-271 |
1.58e-68 |
|
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: 213.28 E-value: 1.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 4 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQaaPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLD-------RQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAA-HK 153
Cdd:cd06320 82 GIPVINLDdavdadaLKKAGGKVTSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKKaPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 154 FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAAT 232
Cdd:cd06320 162 LKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTgKVLVVGTDGIPEAKKSIKAGELTAT 241
|
250 260 270
....*....|....*....|....*....|....*....
1DRK_A 233 IAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVKQ 271
Cdd:cd06320 242 VAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKD 280
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
3-271 |
7.75e-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: 209.05 E-value: 7.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQP 161
Cdd:cd06313 81 IPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYpDIKVLAEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 162 ADFDRIKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQI 240
Cdd:cd06313 161 ANWSRDEAMSLMENWLQAYGDeIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDALQAVKSGELIATVLQDAEAQ 240
|
250 260 270
....*....|....*....|....*....|.
1DRK_A 241 GAKGVETADKVLKGEKVQAKYPVDLKLVVKQ 271
Cdd:cd06313 241 GKGAVEVAVDAVKGEGVEKKYYIPFVLVTKD 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
3-271 |
3.77e-64 |
|
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: 202.21 E-value: 3.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGE----GAKVIELQGTAATSAARERGEGFQQAVAAHKFNVLA 158
Cdd:cd06319 81 IPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKEngwgGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 159 S-QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQL 236
Cdd:cd06319 161 LrQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTgDILVVGFDGDPEALDLIKDGKLDGTVAQQ 240
|
250 260 270
....*....|....*....|....*....|....*.
1DRK_A 237 PDQIGAKGVETADKVLKGEKVQAK-YPVDLKLVVKQ 271
Cdd:cd06319 241 PFGMGARAVELAIQALNGDNTVEKeIYLPVLLVTSE 276
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
3-267 |
4.33e-64 |
|
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: 201.71 E-value: 4.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADK-LGYNLVV--LDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMAN 79
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEaNGYELLVkgIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVITLD------RQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHK 153
Cdd:cd19970 81 DAGIAVINIDnrldadALKEGGINVPFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 154 FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAAT 232
Cdd:cd19970 161 MKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKMLAT 240
|
250 260 270
....*....|....*....|....*....|....*
1DRK_A 233 IAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKL 267
Cdd:cd19970 241 IDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPVEL 275
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
3-268 |
7.36e-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: 201.31 E-value: 7.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADK-LGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQ-ATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLAS 159
Cdd:cd06301 82 GIPLVYVNREpDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYpGMKIVAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIAQLPD 238
Cdd:cd06301 162 QTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDdILVAGIDATPDALKAMKAGRLDATVFQDAA 241
|
250 260 270
....*....|....*....|....*....|
1DRK_A 239 QIGAKGVETADKVLKGEKVQAKYPVDLKLV 268
Cdd:cd06301 242 GQGETAVDVAVKAAKGEEVESDIWIPFELV 271
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
3-257 |
2.11e-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: 195.32 E-value: 2.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQ-ATKGEVVSHIASDNVLGGKIAGDYIAKKAG-EGAKVIELQGTAATSAARERGEGFQQAV--------AAH 152
Cdd:cd06318 81 IPVITVDSAlDPSANVATQVGRDNKQNGVLVGKEAAKALGgDPGKIIELSGDKGNEVSRDRRDGFLAGVneyqlrkyGKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 153 KFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVM-VVGFDGTPDGEKAVNDGKLAA 231
Cdd:cd06318 161 NIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVkVAGADGQKEALKLIKDGKYVA 240
|
250 260
....*....|....*....|....*.
1DRK_A 232 TIAQLPDQIGAKGVETADKVLKGEKV 257
Cdd:cd06318 241 TGLNDPDLLGKTAVDTAAKVVKGEES 266
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
3-268 |
2.98e-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: 194.58 E-value: 2.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVA-AHKFNVLASQP 161
Cdd:cd19972 81 IPVIAVDRNPEDAPGDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAeAPGIKVVAEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 162 ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQI 240
Cdd:cd19972 161 ADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDhKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKM 240
|
250 260
....*....|....*....|....*...
1DRK_A 241 GAKGVETADKVLKGEKVQAKYPVDLKLV 268
Cdd:cd19972 241 GRLAVDSAIDLLNGKAVPKEQLQDAVLT 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
3-268 |
6.11e-61 |
|
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: 193.66 E-value: 6.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYN--LVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGakVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQAtKGeVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAaTSAARERGEGFQQAVAAHK-FNVLAS 159
Cdd:cd06321 81 AGIIVVAVDVAA-EG-ADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPP-VSAVIDRVNGCKEALAEYPgIKLVDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVND--GKLAATIAQLP 237
Cdd:cd06321 158 QNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSVDGSPEAVAALKRegSPFIATAAQDP 237
|
250 260 270
....*....|....*....|....*....|..
1DRK_A 238 DQIGAKGVETADKVLKGEKVQAK-YPVDLKLV 268
Cdd:cd06321 238 YDMARKAVELALKILNGQEPAPElVLIPSTLV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
3-261 |
1.59e-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: 179.85 E-value: 1.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVgpESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH--KFNVLA 158
Cdd:cd06310 81 KGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHpgGIKVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 159 SQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIAQLP 237
Cdd:cd06310 161 SQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGqIKIVGFDSQEELLDALKNGKIDALVVQNP 240
|
250 260
....*....|....*....|....
1DRK_A 238 DQIGAKGVETADKVLKGEKVQAKY 261
Cdd:cd06310 241 YEIGYEGIKLALKLLKGEEVPKNI 264
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
4-256 |
1.72e-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: 176.73 E-value: 1.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 4 IALVVSTLNNPFFVSLKDGAQKEADKLGYN-LVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEvIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH--KFNVLAS- 159
Cdd:pfam13407 81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKypGIKVVAEv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPADFDRIKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIAQLP 237
Cdd:pfam13407 161 EGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGkVVVTGFDATPEALEAIKDGTIDATVLQDP 240
|
250
....*....|....*....
1DRK_A 238 DQIGAKGVETADKVLKGEK 256
Cdd:pfam13407 241 YGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
3-264 |
1.11e-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: 172.42 E-value: 1.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL-DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQgPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLD-RQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAA-HKFNVLAS 159
Cdd:cd20007 81 GIKVVTVDtTLGDPSFVLSQIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMKKyPGIKVLGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIAQLPD 238
Cdd:cd20007 161 QYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGkVKVVGFDASPAQVEQLKAGTIDALIAQKPA 240
|
250 260
....*....|....*....|....*.
1DRK_A 239 QIGAKGVETADKVLKGEKVQAKYPVD 264
Cdd:cd20007 241 EIGYLAVEQAVAALTGKPVPKDILTP 266
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
3-261 |
4.92e-50 |
|
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: 165.87 E-value: 4.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANq 80
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLgpATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAK----KAGEGAKVIELQGTAATSAARERGEGFQQAVAAH--KF 154
Cdd:cd20008 80 AGIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAEllkaSGGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKypDI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 155 NVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATI 233
Cdd:cd20008 160 EIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAgKIVLVGFDSSPDEVALLKSGVIKALV 239
|
250 260
....*....|....*....|....*...
1DRK_A 234 AQLPDQIGAKGVETADKVLKGEKVQAKY 261
Cdd:cd20008 240 VQDPYQMGYEGVKTAVKALKGEEIVEKN 267
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
4-270 |
5.77e-48 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 161.58 E-value: 5.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 4 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:PRK09701 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFasPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDR-------QATKGEVVSHIASDNVLGGKIAGDYIAKKAG-EGAKVIELQGTAATSAARERGEGFQQA-VAAH 152
Cdd:PRK09701 107 GIYLVNLDEkidmdnlKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGaEGGEVAIIEGKAGNASGEARRNGATEAfKKAS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 153 KFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKAVNDGKLAA 231
Cdd:PRK09701 187 QIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKtGKVLVVGTDGIPEARKMVEAGQMTA 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
1DRK_A 232 TIAQLPDQIGAKGV------ETADKVLKGEKVQAKYPVDLKLVVK 270
Cdd:PRK09701 267 TVAQNPADIGATGLklmvdaEKSGKVIPLDKAPEFKLVDSILVTQ 311
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
3-260 |
2.86e-46 |
|
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: 155.82 E-value: 2.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQN-NPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQ 160
Cdd:cd06314 81 GIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKGSpGIEIVDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQ 239
Cdd:cd06314 161 SDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKvGKVKIVGFDTLPETLQGIKDGVIAATVGQRPYE 240
|
250 260
....*....|....*....|.
1DRK_A 240 IGAKGVETADKVLKGEKVQAK 260
Cdd:cd06314 241 MGYLSVKLLYKLLKGGKPVPD 261
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
3-260 |
3.13e-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: 155.75 E-value: 3.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAvgNAVKMANQAN 82
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDD--ELLEELLAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQAtKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIE-LQGTAATSAARERGEGFQQAVAAHKFNVLAS-- 159
Cdd:cd06267 79 IPVVLIDRRL-DGLGVDSVVVDNYAGAYLATEHLIEL---GHRRIAfIGGPLDLSTSRERLEGYRDALAEAGLPVDPElv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndgkLAA----- 231
Cdd:cd06267 155 VEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRvpeDISVVGFDDIP----------LAAlltpp 224
|
250 260 270
....*....|....*....|....*....|.
1DRK_A 232 --TIAQLPDQIGAKGVETADKVLKGEKVQAK 260
Cdd:cd06267 225 ltTVRQPAYEMGRAAAELLLERIEGEEEPPR 255
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
3-271 |
6.08e-46 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 156.90 E-value: 6.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGtkILLINPTDSDAvgnAVKMAN 79
Cdd:COG1609 63 TIGVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLsrrVDG--LILAGSRLDDA---RLERLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVITLDRQaTKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVI-ELQGTAATSAARERGEGFQQAVAAHKFNVLA 158
Cdd:COG1609 138 EAGIPVVLIDRP-LPDPGVPSVGVDNRAGARLATEHLIEL---GHRRIaFIGGPADSSSARERLAGYREALAEAGLPPDP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 159 SQ--PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEkaVNDGKLaATI 233
Cdd:COG1609 214 ELvvEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRvpeDVSVVGFDDIPLAR--YLTPPL-TTV 290
|
250 260 270 280
....*....|....*....|....*....|....*....|
1DRK_A 234 AQLPDQIGAKGVETADKVLKGEKVQAKyPVDL--KLVVKQ 271
Cdd:COG1609 291 RQPIEEMGRRAAELLLDRIEGPDAPPE-RVLLppELVVRE 329
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
3-269 |
6.94e-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: 152.29 E-value: 6.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGtkILLInpTDSDAVGNAVKman 79
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKrnkVDG--IILG--SHSLDIEEYKK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 qANIPVITLDRQATKGevVSHIASDNVLGGKIAGDYIAKKageGAK-VIELQGTAATSAARERGEGFQQAVAAH--KFNV 156
Cdd:cd06291 74 -LNIPIVSIDRYLSEG--IPSVSSDNYQGGRLAAEHLIEK---GCKkILHIGGPSNNSPANERYRGFEDALKEAgiEYEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 157 LASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKAVNdgKLaATI 233
Cdd:cd06291 148 IEIDENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRvpeDVQIIGFDGIEISELLYP--EL-TTI 224
|
250 260 270
....*....|....*....|....*....|....*..
1DRK_A 234 AQLPDQIGAKGVETADKVLKGEKVQAK-YPVDLKLVV 269
Cdd:cd06291 225 RQPIEEMAKEAVELLLKLIEGEEIEESrIVLPVELIE 261
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
3-270 |
1.36e-43 |
|
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: 148.92 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRgpSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH--KFNVLA 158
Cdd:cd20004 81 QGIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAKGSASTTDRERGFLEALKKLapGLKVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 159 SQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLP 237
Cdd:cd20004 161 DQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLAgKVKFIGFDASDLLLDALRAGEISALVVQDP 240
|
250 260 270
....*....|....*....|....*....|...
1DRK_A 238 DQIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 270
Cdd:cd20004 241 YRMGYLGVKTAVAALRGKPVPKRIDTGVVLVTK 273
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
4-264 |
1.26e-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: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 4 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANI 83
Cdd:cd19992 2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 84 PVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIeLQGTAATSAARERGEGF----QQAVAAHKFNVLAS 159
Cdd:cd19992 82 PVISYDRLILNADVDLYVGRDNYKVGQLQAEYALEAVPKGNYVI-LSGDPGDNNAQLITAGAmdvlQPAIDSGDIKIVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPAD-FDRIKGLNVMQNLLTA-HPDVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQL 236
Cdd:cd19992 161 QYVKgWSPDEAMKLVENALTAnNNNIDAVLAPNDGMAGGAIQALKAQGlAGKVFVTGQDAELAALKRIVEGTQTMTVWKD 240
|
250 260
....*....|....*....|....*...
1DRK_A 237 PDQIGAKGVETADKVLKGEKVQAKYPVD 264
Cdd:cd19992 241 LKELARAAADAAVKLAKGEKPQTTDETI 268
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
3-261 |
3.26e-41 |
|
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: 143.54 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYN---LVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMAN 79
Cdd:cd19996 1 TIGFSNAGLGNSWRVQMIAEFEAEAAKLKKLikeLIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHK-FNVLA 158
Cdd:cd19996 81 AAGIPVVLFDSGVGSDKYTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYPgIKIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 159 SQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGE--KAVNDGKLAATIaqL 236
Cdd:cd19996 161 EVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTGEDNNGFLKawKELPGFKSIAPS--Y 238
|
250 260
....*....|....*....|....*
1DRK_A 237 PDQIGAKGVETADKVLKGEKVQAKY 261
Cdd:cd19996 239 PPWLGATALDAALAALEGEPVPKYV 263
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
3-270 |
7.23e-40 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 139.82 E-value: 7.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAG----DYIAKKAGEGAKvIELQGTAATSAARERGEGFQQAVAAH-KFNVL 157
Cdd:cd06317 81 IPVIAYDAVIPSDFQAAQVGVDNLEGGKEIGkyaaDYIKAELGGQAK-IGVVGALSSLIQNQRQKGFEEALKANpGVEIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 158 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPD-GEKAVNDGKLAATIAQ 235
Cdd:cd06317 160 ATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQgKIKVFGWDLTKQaIFLGIDEGVLQAVVQQ 239
|
250 260 270
....*....|....*....|....*....|....*
1DRK_A 236 LPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 270
Cdd:cd06317 240 DPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
3-234 |
3.05e-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: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVV-STLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKI--LLINPTDSDAVGnAVKMAN 79
Cdd:cd06324 1 RVVFINpGKEDEPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARPPKPdyLILVNEKGVAPE-LLELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVITLDRQATKGEV-------------VSHIASDNVLGG-KIAGDYIA----KKAGEGAKVIELQGTAATSAARER 141
Cdd:cd06324 80 QAKIPVFLINNDLTDEERallgkprekfkywLGSIVPDNEQAGyLLAKALIKaarkKSDDGKIRVLAISGDKSTPASILR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 142 GEGFQQAVAAH-KFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGT 217
Cdd:cd06324 160 EQGLRDALAEHpDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLkpgKDVLVGGIDWS 239
|
250
....*....|....*..
1DRK_A 218 PDGEKAVNDGKLAATIA 234
Cdd:cd06324 240 PEALQAVKDGELTASVG 256
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
3-265 |
3.05e-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: 132.49 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQP 161
Cdd:cd06311 81 IPVVNFDRGLNVLIYDLYVAGDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNpGIKILAMQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 162 ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDV-MVVGFDGTPDGEKAVNDGK--LAATIAQLPD 238
Cdd:cd06311 161 GDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIkVMTGGGGSQEYFKRIMDGDpiWPASATYSPA 240
|
250 260 270
....*....|....*....|....*....|
1DRK_A 239 QIgAKGVETADKVLKGEK---VQAKYPVDL 265
Cdd:cd06311 241 MI-ADAIKLAVLILKGGKtveKEVIIPSTL 269
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
3-260 |
6.84e-37 |
|
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: 131.60 E-value: 6.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:cd20005 1 YIAVISKGFQHQFWKAVKKGAEQAAKELGVKITFEgpDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHKFN--VLA 158
Cdd:cd20005 81 KGIPVVTFDSGVPSDLPLATVATDNYAAGALAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDikVVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 159 SQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKAVNDGKLAATIAQLP 237
Cdd:cd20005 161 VQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKlGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNP 240
|
250 260
....*....|....*....|...
1DRK_A 238 DQIGAKGVETADKVLKGEKVQAK 260
Cdd:cd20005 241 YGMGYKTVKAAVKALKGEEVEKL 263
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
3-253 |
7.44e-37 |
|
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: 7.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:cd19973 1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAagKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATKGEVV-SHIASDNVLGGKIAGDYIAKKAGEG-AKVIELQGTAATSAARERGEGF-----------QQ 147
Cdd:cd19973 81 AGVLVIALDTPTDPIDAAdATFATDNFKAGVLIGEWAKAALGAKdAKIATLDLTPGHTVGVLRHQGFlkgfgidekdpES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 148 AVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKAVND 226
Cdd:cd19973 161 NEDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKeKGVLIVSVDGGCPGVKDVKD 240
|
250 260
....*....|....*....|....*..
1DRK_A 227 GKLAATIAQLPDQIGAKGVETADKVLK 253
Cdd:cd19973 241 GIIGATSQQYPLRMAALGVEAIAAFAK 267
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
3-247 |
1.46e-34 |
|
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: 125.45 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVgNAVKMANQAN 82
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDD-DAELLAALRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAKKageGAKVIE-LQGTAATSAARERGEGFQQAVAAHKFNVLAS-- 159
Cdd:cd06275 80 IPVVVLDREIAGDNADA-VLDDSFQGGYLATRHLIEL---GHRRIGcITGPLEHSVSRERLAGFRRALAEAGIEVPPSwi 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDGTPdgekavndgkLAA----- 231
Cdd:cd06275 156 VEGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGlrvPQDISIIGYDDIE----------LARyfspa 225
|
250
....*....|....*...
1DRK_A 232 --TIAQLPDQIGAKGVET 247
Cdd:cd06275 226 ltTIHQPKDELGELAVEL 243
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
20-259 |
4.44e-34 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 125.25 E-value: 4.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 20 KDGA--QKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEV 97
Cdd:COG4213 19 RDGDnfKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVIAYDRLILNSDV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 98 VSHIASDNVLGGKIAGDYIAKKAGEGAK-VIELQGTAATSA-ARERGEGF----QQAVAAHKFNVLASQPA-DFDRIKGL 170
Cdd:COG4213 99 DYYVSFDNVKVGELQGQYLVDGLPLKGKgNIELFGGSPTDNnATLFFEGAmsvlQPYIDSGKLVVVSGQWTlGWDPETAQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 171 NVMQNLLTAHP-DVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETA 248
Cdd:COG4213 179 KRMENLLTANGnKVDAVLAPNDGLAGGIIQALKAQGLAgKVVVTGQDAELAAVQRILAGTQYMTVYKDTRELAEAAAELA 258
|
250
....*....|.
1DRK_A 249 DKVLKGEKVQA 259
Cdd:COG4213 259 VALAKGEKPEV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
3-270 |
1.11e-33 |
|
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: 123.09 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVV--STLNNPFFVSLKDGAQKEADKLGYNLVVL--DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMA 78
Cdd:cd20006 1 KIALILksSDPNSDFWQTVKSGAEAAAKEYGVDLEFLgpESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 79 NQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHKF-NVL 157
Cdd:cd20006 81 KKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQALAEYPNiKIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 158 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQL 236
Cdd:cd20006 161 ETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGlGGKVKVVGFDSSVEEIQLLEEGIIDALVVQN 240
|
250 260 270
....*....|....*....|....*....|....
1DRK_A 237 PDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 270
Cdd:cd20006 241 PFNMGYLSVQAAVDLLNGKKIPKRIDTGSVVITK 274
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
3-218 |
1.69e-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: 122.64 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYN--LVVLDSQNNPAKELANVQDLTVRGtkILLINPTDSDAVgnaVKMANQ 80
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRplLFNVDDEDDVDDALRQLLQYRVDG--VIVTSATLSSEL---AEECAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATkGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIE-LQGTAATSAARERGEGFQQAVAAHKFNVLAS 159
Cdd:cd06278 76 RGIPVVLFNRVVE-DPGVDSVSCDNRAGGRLAADLLLAA---GHRRIAfLGGPEGTSTSRERERGFRAALAELGLPPPAV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
1DRK_A 160 QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS----DVMVVGFDGTP 218
Cdd:cd06278 152 EAGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGLvvpeDISVVGFDDIP 214
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
3-235 |
5.92e-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: 121.92 E-value: 5.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLG-YNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGkIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQATKGEV--------VSHIASDN-VLGGKIAGDYIAK-----KAGEGakVIE---LQGTAATSAARERGEG 144
Cdd:cd01539 82 NIPVIFFNREPSREDLksydkayyVGTDAEESgIMQGEIIADYWKAnpeidKNGDG--KIQyvmLKGEPGHQDAIARTKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 145 FQQAVAAH--KFNVLASQPADFDRIKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAG------KSDVMVVGFD 215
Cdd:cd01539 160 SVKTLNDAgiKTEQLAEDTANWDRAQAKDKMDAWLSKYGDkIELVIANNDDMALGAIEALKAAGyntgdgDKYIPVFGVD 239
|
250 260
....*....|....*....|
1DRK_A 216 GTPDGEKAVNDGKLAATIAQ 235
Cdd:cd01539 240 ATPEALEAIKEGKMLGTVLN 259
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
3-256 |
5.37e-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: 5.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPT--DSDAVGNAVKmanq 80
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSagPSRELKRLLK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAKKageGAKVIEL-QGTAATSAARERGEGFQQAVAAHKFNVLAS 159
Cdd:cd06280 77 HGIPIVLIDREVEGLELDL-VAGDNREGAYKAVKHLIEL---GHRRIGLiTGPLEISTTRERLAGYREALAEAGIPVDES 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 --QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEkaVNDGKLAAtIA 234
Cdd:cd06280 153 liFEGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEipqDISVVGFDDSDWFE--IVDPPLTV-VA 229
|
250 260
....*....|....*....|..
1DRK_A 235 QLPDQIGAKGVETADKVLKGEK 256
Cdd:cd06280 230 QPAYEIGRIAAQLLLERIEGQG 251
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
3-257 |
1.03e-31 |
|
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: 118.07 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQ--NNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGgyTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGA-KVIELQGTAATSAARERGEGFQQAVAAHKFNVLAS 159
Cdd:cd06306 81 AGIPVIDLVNGIDSPKVAARVLVDFYDMGYLAGEYLVEHHPGKPvKVAWFPGPAGAGWAEDREKGFKEALAGSNVEIVAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPADFDRIKGLNVMQNLLTAHPDVQAVFAqNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPD 238
Cdd:cd06306 161 KYGDTGKAVQLNLVEDALQAHPDIDYIVG-NAVAAEAAVGALREAGLTgKVKVVSTYLTPGVYRGIKRGKILAAPSDQPV 239
|
250
....*....|....*....
1DRK_A 239 QIGAKGVETADKVLKGEKV 257
Cdd:cd06306 240 LQGRIAVDQAVRALEGKPV 258
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
3-256 |
3.57e-31 |
|
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: 116.58 E-value: 3.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDavGNAVKMANQ-A 81
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNIS--DEAIIKLLKeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAKKAGEgaKVIELQGTAATSAARERGEGFQQAVAAHKFNVLASQ- 160
Cdd:cd19976 79 KIPVVVLDRYIEDNDSDS-VGVDDYRGGYEATKYLIELGHT--RIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWi 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKAvnDGKLaATIAQLP 237
Cdd:cd19976 156 YSGESSLEGGYKAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKipeDLSVIGFDNIILSEYI--TPAL-TTIAQPI 232
|
250
....*....|....*....
1DRK_A 238 DQIGAKGVETADKVLKGEK 256
Cdd:cd19976 233 FEMGQEAAKLLLKIIKNPA 251
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
3-261 |
1.39e-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: 115.09 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVsHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAAReRGEGFQQAVAAHK--FNVLASQ 160
Cdd:cd06305 81 IPVVTFDTDSQVPGVN-NITQDDYALGTLSLGQLVKDLNGEGNIAVFNVFGVPPLDK-RYDIYKAVLKANPgiKKIVAEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 PADFDrikglNVMQN-------LLTAHPD--VQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAV--NDGKL 229
Cdd:cd06305 159 GDVTP-----NTAADaqtqveaLLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISNQDLELMadEGSPW 233
|
250 260 270
....*....|....*....|....*....|..
1DRK_A 230 AATIAQLPDQIGAKGVETADKVLKGEKVQAKY 261
Cdd:cd06305 234 VATAAQDPALIGTVAVRNVARKLAGEDLPDKY 265
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
21-256 |
2.48e-30 |
|
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: 115.11 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 21 DGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDrQATKGEVVSH 100
Cdd:cd06300 24 DAAQSGQKGLVKELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFD-GAVTSPDAYN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 101 IASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQPADFDRIKGLNVMQNLLTA 179
Cdd:cd06300 103 VSNDQVEWGRLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEALAEYpGIKVVGEVFGGWDEATAQTAMLDFLAT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DRK_A 180 HPDVQAVFAQNDEmALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGK--LAATIAQLPDQIGAKGVETADKVLKGEK 256
Cdd:cd06300 183 HPQVDGVWTQGGE-DTGVLQAFQQAGRPPVPIVGGDENGFAKQWWKHPKkgLTGAAVWPPPAIGAAGLEVALRLLEGQG 260
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
3-269 |
7.93e-30 |
|
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: 113.02 E-value: 7.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKE---LANVQDLTVRGtkILLINPTDSdavgNAVKMAN 79
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREddlLDMLRSRRVDG--VILLSGRLD----AELLSEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVItldrQA---TKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIEL-QGTAATSAARERGEGFQQAVAAHK-- 153
Cdd:cd06284 75 SKRYPIV----QCceyIPDSGVPSVSIDNEAAAYDATEYLISL---GHRRIAHiNGPLDNVYARERLEGYRRALAEAGlp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 154 FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTpdgekavndgKLA 230
Cdd:cd06284 148 VDEDLIIEGDFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRvpeDVSVIGFDDI----------EFA 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
1DRK_A 231 A-------TIAQLPDQIGAKGVET-ADKVLKGEKVQAKYPVDLKLVV 269
Cdd:cd06284 218 EmfspsltTIRQPRYEIGETAAELlLEKIEGEGVPPEHIILPHELIV 264
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
3-246 |
9.32e-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: 380516 [Multi-domain] Cd Length: 270 Bit Score: 112.75 E-value: 9.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPtdSDAVGNAVKMANQAN 82
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTP--SDDDLSHLARLRARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQAtKGEVVSHIASDNVLGGKIAGDYIakkAGEGAKVIE-LQGTAATSAARERGEGFQQAVAAHKFN----VL 157
Cdd:cd06293 79 TAVVLLDRPA-PGPAGCSVSVDDVQGGALAVDHL---LELGHRRIAfVSGPLRTRQVAERLAGARAAVAEAGLDpdevVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 158 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndgkLAA--- 231
Cdd:cd06293 155 ELSAPDANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRvpdDVSVVGYDDLP----------FAAaan 224
|
250
....*....|....*....
1DRK_A 232 ----TIAQLPDQIGAKGVE 246
Cdd:cd06293 225 ppltTVRQPSYELGRAAAD 243
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
3-257 |
1.87e-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: 380513 [Multi-domain] Cd Length: 267 Bit Score: 111.94 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTK--ILLINPTDSDAVgNAVKManq 80
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDgiIVVGGFGDEELL-KLLAE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 aNIPVITLDRQaTKGEVVSHIASDNVLGGKIAGDYIAKKageGA-KVIELQGTAATSAARERGEGFQQAVAAH--KFNVL 157
Cdd:cd06290 77 -GIPVVLVDRE-LEGLNLPVVNVDNEQGGYNATNHLIDL---GHrRIVHISGPEDHPDAQERYAGYRRALEDAglEVDPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 158 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGE-----------KA 223
Cdd:cd06290 152 LIVEGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRvpdDVSVIGFDDLPFSKyttpplttvrqPL 231
|
250 260 270
....*....|....*....|....*....|....
1DRK_A 224 VNDGKLAATIaqLPDQIGAKGVETADKVLKGEKV 257
Cdd:cd06290 232 YEMGKTAAEI--LLELIEGKGRPPRRIILPTELV 263
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
3-258 |
5.81e-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: 110.72 E-value: 5.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGtkILLINPTDSDAVGNAVKman 79
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKekrVDG--IIFASGTLTEENKQLLK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAKKageGAKVIELQGTAAT--SAARERGEGFQQAVAAH--KFN 155
Cdd:cd19975 76 NMNIPVVLVSTESEDPDIPS-VKIDDYQAAYDATNYLIKK---GHRKIAMISGPLDdpNAGYPRYEGYKKALKDAglPIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 156 VLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDGTPDGEKAVNdgKLaAT 232
Cdd:cd19975 152 ENLIVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGirvPEDISVIGFDNTEIAEMSIP--PL-TT 228
|
250 260
....*....|....*....|....*.
1DRK_A 233 IAQLPDQIGAKGVETADKVLKGEKVQ 258
Cdd:cd19975 229 VSQPFYEMGKKAVELLLDLIKNEKKE 254
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
3-243 |
9.84e-29 |
|
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: 109.96 E-value: 9.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINP---TDSDAVgnavKMAN 79
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPaagTTAELL----RRLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVITLDRQATkGEVVSHIASDNVLGGKIAGDYIAkkaGEGAKVIE-LQGTAATSAARERGEGFQQAVAAHKFNVLA 158
Cdd:cd06289 77 AWGIPVVLALRDVP-GSDLDYVGIDNRLGAQLATEHLI---ALGHRRIAfLGGLSDSSTRRERLAGFRAALAEAGLPLDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 159 SQ--PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGTPdgEKAVNDGKLaATI 233
Cdd:cd06289 153 SLivPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLepgRDIAVVGFDDVP--EAALWTPPL-TTV 229
|
250
....*....|
1DRK_A 234 AQLPDQIGAK 243
Cdd:cd06289 230 SVHPREIGRR 239
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
3-247 |
2.95e-28 |
|
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: 108.85 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAvGNAVKMANqAN 82
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDA-PDLQELAA-RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVShIASDNVLGGKIAGDYIakkAGEG-AKVIELQGTAATSAARERGEGFQQAVAAHKFNVLASQ- 160
Cdd:cd06285 79 VPVVLVDRRIGDTALPS-VTVDNELGGRLATRHL---LELGhRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERi 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 -PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndgkLAA----- 231
Cdd:cd06285 155 vPGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRvpeDLSVVGFDDIP----------LAAflppp 224
|
250
....*....|....*...
1DRK_A 232 --TIAQLPDQIGAKGVET 247
Cdd:cd06285 225 ltTVRQPKYEMGRRAAEL 242
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
3-215 |
6.20e-28 |
|
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: 107.99 E-value: 6.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTK-ILLINPTDSDAvgnAVKMANQA 81
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDaIILHSRALSDE---ELILIAEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQATKgevVSH--IASDNVLGGKIAGDYIAKKageGAKVIE-LQGTAATSAARERGEGFQQAVAAH--KFNV 156
Cdd:cd06270 78 IPPLVVINRYIPG---LADrcVWLDNEQGGRLAAEHLLDL---GHRRIAcITGPLDIPDARERLAGYRDALAEAgiPLDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
1DRK_A 157 LASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFD 215
Cdd:cd06270 152 SLIIEGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKvpeDVSVIGFD 213
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
4-248 |
3.03e-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: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 4 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQaNI 83
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQ-NV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 84 PVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEgaKVIELQGTAATSAARERGEGFQQAV--AAHKFNVLASQP 161
Cdd:cd01537 81 PVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHI--QIVLLKGPLGHPDAEARLAGVIKELndKGIKTEQLQLDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 162 ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGTPDGEKAvndGKLAATIAQLPD 238
Cdd:cd01537 159 GDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLrvpSDISVFGYDALPEALKS---GPLLTTILQDAN 235
|
250
....*....|
1DRK_A 239 QIGAKGVETA 248
Cdd:cd01537 236 NLGKTTFDLL 245
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
3-218 |
3.31e-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: 106.07 E-value: 3.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAvGNAVKMANQaN 82
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNE-DLIEKLVKS-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRqATKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIE-LQGTAATSAARERGEGFQQAVAAHKfnvlasQP 161
Cdd:cd19977 79 IPVVFVDR-YIPGLDVDTVVVDNFKGAYQATEHLIEL---GHKRIAfITYPLELSTRQERLEGYKAALADHG------LP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1DRK_A 162 ADFDRIKGLNVMQN-------LLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGTP 218
Cdd:cd19977 149 VDEELIKHVDRQDDvrkaiseLLKLEKPPDAIFAANNLITLEVLKAIKELGLripDDIALIGFDDIP 215
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
3-271 |
5.55e-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: 105.32 E-value: 5.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLN-NPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGtkILLINPTdSDAVGNAVKMA 78
Cdd:cd06288 1 TIGLITDDIAtTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLsrrVDG--IIYASMH-HREVTLPPELT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 79 NqanIPVITLDRQATKGEVVSHIAsDNVLGGKIAGDYIAKKageGAKVIE-LQGTAATSAARERGEGFQQAVAAHKFNVL 157
Cdd:cd06288 78 D---IPLVLLNCFDDDPSLPSVVP-DDEQGGYLATRHLIEA---GHRRIAfIGGPEDSLATRLRLAGYRAALAEAGIPYD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 158 AS--QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDgtpdgekavnDGKLAA- 231
Cdd:cd06288 151 PSlvVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRvpeDLSVVGFD----------NQELAAy 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
1DRK_A 232 -----TIAQLP-DQIGAKGVETA-DKVLKGEKVQAKYPVDLKLVVKQ 271
Cdd:cd06288 221 lrpplTTVALPyYEMGRRAAELLlDGIEGEPPEPGVIRVPCPLIERE 267
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
3-247 |
4.37e-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: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAvgNAVKMANQAN 82
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENS--EGLQALIAQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIelQGTAATSAARERGEGFQQAVAAHKFNV--LASQ 160
Cdd:cd06299 79 LPVVFVDREVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYI--SGPLSTSTGRERLAAFRAALTAAGIPIdeELVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDGTPDGEkaVNDGKLAAtIAQLP 237
Cdd:cd06299 157 FGDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGlriGDDVSLISFDDVPWFE--LLSPPLTV-IAQPV 233
|
250
....*....|
1DRK_A 238 DQIGAKGVET 247
Cdd:cd06299 234 ERIGRRAVEL 243
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
33-257 |
5.40e-26 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380654 [Multi-domain] Cd Length: 313 Bit Score: 103.93 E-value: 5.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 33 NLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVShIASDNVLGGKIA 112
Cdd:cd19999 36 DLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPVSSPDAIN-VVIDQYKWAAIQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 113 GDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHK-FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQnD 191
Cdd:cd19999 115 AQWLAEQLGGKGNIVAINGVAGNPANEARVKAADDVFAKYPgIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLTQ-D 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DRK_A 192 EMALGALRALQTAGKSDVMVVGfDGTPDGEKAVNDGKLAA--TIAQL-PDQIGAKGVETADKVLKGEKV 257
Cdd:cd19999 194 GMAEGVLRAFQAAGKDPPVMTG-DYRKGFLRKWKELDLPDfeSIGVVnPPGIGATALRIAVRLLQGKEL 261
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
3-256 |
1.50e-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: 102.12 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIeLQGTAATSAARERGEGFQQ----AVAAHKFNVLA 158
Cdd:cd01538 81 IKVIAYDRLILNADVDYYISFDNEKVGELQAQALLDAKPEGNYVL-IGGSPTDNNAKLFRDGQMKvlqpAIDSGKIKVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 159 SQPAD-FDRIKGLNVMQNLLTAH-PDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIAQ 235
Cdd:cd01538 160 DQWVDdWLPANAQQIMENALTANgNNVDAVVASNDGTAGGAIAALKAQGLSGgVPVSGQDADLAAIKRILAGTQTMTVYK 239
|
250 260
....*....|....*....|.
1DRK_A 236 LPDQIGAKGVETADKVLKGEK 256
Cdd:cd01538 240 DIRLLADAAAEVAVALMRGEK 260
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
3-257 |
2.66e-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: 101.55 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLV-VLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd06316 1 KVAIAMHTTGSDWSRLQVAGIKDTFEELGIEVVaVTDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQAT----KGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHKFNVL 157
Cdd:cd06316 81 GIKLVFMDNVPDgleaGKDYVSVVSSDNRGNGQIAAELLAEAIGGKGKVGIIYHDADFYATNQRDKAFKDTLKEKYPDIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 158 ASQPADFDRI-KGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFD-GTPDGEKAVNDGKLAATIAQ 235
Cdd:cd06316 161 IVAEQGFADPnDAEEVASAMLTANPDIDGIYVSWDTPALGVISALRAAGRSDIKITTVDlGTEIALDMAKGGNVKGIGAQ 240
|
250 260
....*....|....*....|..
1DRK_A 236 LPDQIGAKGVETADKVLKGEKV 257
Cdd:cd06316 241 RPYDQGVAEALAAALALLGKEV 262
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
25-259 |
1.89e-24 |
|
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: 98.85 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 25 KEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASD 104
Cdd:cd19991 23 KKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNADVDLYVSFD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 105 NVLGGKIAGDYIAKKAGEGAKVIeLQGTAATSAARERGEG----FQQAVAAHKFNVLASQ-PADFDRIKGLNVMQNLLTA 179
Cdd:cd19991 103 NEKVGELQAEALVKAKPKGNYVL-LGGSPTDNNAKLFREGqmkvLQPLIDSGDIKVVGDQwVDDWDPEEALKIMENALTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 180 H-PDVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKV 257
Cdd:cd19991 182 NnNKIDAVIASNDGTAGGAIQALAEQGlAGKVAVSGQDADLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKN 261
|
..
1DRK_A 258 QA 259
Cdd:cd19991 262 EA 263
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
3-264 |
1.92e-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: 99.24 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVL-DSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd06302 1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQATKG--EVVSHIASDNVLGGKIAgDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH--KFNVL 157
Cdd:cd06302 81 GIKVITWDSDAPPSarDYFVNQADDEGLGEALV-DSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKypDIELV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 158 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFdGTP-DGEKAVNDGKLAATIAQ 235
Cdd:cd06302 160 DTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGkVAVTGI-GLPnTARPYLKDGSVKEGVLW 238
|
250 260
....*....|....*....|....*....
1DRK_A 236 LPDQIGAKGVETADKVLKGEKVQAKYPVD 264
Cdd:cd06302 239 DPAKLGYLTVYAAYQLLKGKGFTEDSDDV 267
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
4-271 |
2.94e-24 |
|
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: 98.52 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 4 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTD---SDAVgnaVKMANQ 80
Cdd:cd01540 2 IGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDqklGPAI---AAKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQ---ATKGEVVSHIASD-NVLG---GKIAGDYiAKKAG--EGAKVIELQGTAAT-SAARERGEGFQQAVA 150
Cdd:cd01540 79 AGIPVIAVDDQlvdADPMKIVPFVGIDaYKIGeavGEWLAKE-MKKRGwdDVKEVGVLAITMDTlSVCVDRTDGAKDALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 151 AHKF---NVLASQPADFDRIKGLNVMQNLLTAHPDVQ--AVFAQNDEMALGALRALQTAG--KSDVMVVGFDG--TPDGE 221
Cdd:cd01540 158 AAGFpedQIFQAPYKGTDTEGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAGfdAEDIIGVGIGGylAADEE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
1DRK_A 222 KAVNDGKLAATIAQLPDQIGAKGVET-ADKVLKGEKVQAKYPVDLKLVVKQ 271
Cdd:cd01540 238 FKKQPTGFKASLYISPDKHGYIAAEElYNWITDGKPPPAETLTDGVIVTRD 288
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
4-263 |
7.73e-24 |
|
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: 97.34 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 4 IALVVSTLN---NPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKmANQ 80
Cdd:cd01391 2 IGVVTSSLHqirEQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNL-AQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLD------RQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIElqgTAATSAARERGEGFQQAVAAHKF 154
Cdd:cd01391 81 FDIPQLALDatsqdlSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIH---GEGLNSGELRMAGFKELAKQEGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 155 NVLASQPADFDRI-KGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-SDVMVVGFDGTPDGEKA--VNDGKLA 230
Cdd:cd01391 158 CIVASDKADWNAGeKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLvGDVSVIGSDGWADRDEVgyEVEANGL 237
|
250 260 270
....*....|....*....|....*....|...
1DRK_A 231 ATIAQLPDQIGAKGVETADKVLKGEKVQAKYPV 263
Cdd:cd01391 238 TTIKQQKMGFGITAIKAMADGSQNMHEEVWFDE 270
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
25-265 |
1.30e-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: 96.78 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 25 KEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRqATKGEVVSHIASD 104
Cdd:cd19993 23 KALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDR-LIENPIAFYISFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 105 NVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERG---EGFQQAVAAHKFNVLASQPAD-FDRIKGLNVMQNLLTAH 180
Cdd:cd19993 102 NVEVGRMQARGVLKAKPEGNYVFIKGSPTDPNADFLRAgqmEVLQPAIDSGKIKIVGEQYTDgWKPANAQKNMEQILTAN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 181 P-DVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQ 258
Cdd:cd19993 182 NnKVDAVVASNDGTAGGAVAALAAQGlAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKGTKIE 261
|
....*..
1DRK_A 259 AKYPVDL 265
Cdd:cd19993 262 AIKGAAL 268
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
3-247 |
1.36e-23 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 97.46 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVkMANQAN 82
Cdd:PRK10423 58 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREI-MQRYPS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGevVSHIASDN-VLGGKIAGDYIAKKageGAKVIE-LQGTAATSAARERGEGFQQAVAAHKFNVLASQ 160
Cdd:PRK10423 137 VPTVMMDWAPFDG--DSDLIQDNsLLGGDLATQYLIDK---GYTRIAcITGPLDKTPARLRLEGYRAAMKRAGLNIPDGY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 161 P--ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDgtpdgekavnDGKLA----- 230
Cdd:PRK10423 212 EvtGDFEFNGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLSvpqDIAVIGYD----------DIELArymtp 281
|
250
....*....|....*....
1DRK_A 231 --ATIAQLPDQIGAKGVET 247
Cdd:PRK10423 282 plTTIHQPKDELGELAIDV 300
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
1-252 |
1.48e-23 |
|
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: 96.43 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 1 KDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINP--TDSDAVgnaVKMA 78
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTpaPSGDDI---TAKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 79 NQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIaKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHKFNVLA 158
Cdd:pfam00532 78 EGYGIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYL-IAEGHKRPIAVMAGPASALTARERVQGFMAALAAAGREVKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 159 SQPA--DFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG----KSDVM-----VVGFDGTPDGEKAVNDG 227
Cdd:pfam00532 157 YHVAtgDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrvkiPDIVGiginsVVGFDGLSKAQDTGLYL 236
|
250 260
....*....|....*....|....*
1DRK_A 228 KLAATIaQLPDQIgaKGVETADKVL 252
Cdd:pfam00532 237 SPLTVI-QLPRQL--LGIKASDMVY 258
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
3-237 |
5.00e-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: 94.99 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVV-STLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELA-NVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:cd06312 1 TIYVIShGSPSDPFWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQArLIEQAIAAKPDGIIVTIPDPDALEPALKRAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITL----DRQATKGEVVSHIASDNVLGGKIAGDYIAKKageGAK----VIELQGTAATSAareRGEGFQQAVAAH 152
Cdd:cd06312 81 AGIPVIAInsgdDRSKERLGALTYVGQDEYLAGQAAGERALEA---GPKnalcVNHEPGNPGLEA---RCKGFADAFKGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 153 KFNVLASQPADfDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAA 231
Cdd:cd06312 155 GILVELLDVGG-DPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGlKGKVKIGTFDLSPETLEAIKDGKILF 233
|
....*.
1DRK_A 232 TIAQLP 237
Cdd:cd06312 234 AIDQQP 239
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
4-237 |
6.42e-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: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 4 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQN-NPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd19965 2 FVFVTHVTTNPFFQPVKKGMDDACELLGAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGE--VVSHIASDNVLGGKIAGDYIAKKAG-EGAKVIELQGTAATSAARERGEGFQQAVAAHK----FN 155
Cdd:cd19965 82 IPVVAFNVDAPGGEnaRLAFVGQDLYPAGYVLGKRIAEKFKpGGGHVLLGISTPGQSALEQRLDGIKQALKEYGrgitYD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 156 VLASQPadfDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGEKAVNDGKLAATIA 234
Cdd:cd19965 162 VIDTGT---DLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGkVLVGGFDLVPEVLQGIKAGYIDFTID 238
|
...
1DRK_A 235 QLP 237
Cdd:cd19965 239 QQP 241
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
3-271 |
3.57e-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: 92.57 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTK-ILLINPTDSDAVgnaVKMANQA 81
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDgLILVGSDHDPEL---FELLEQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDrQATKGEVVSHIASDNVLGGKIAGDYiakkagegakVIEL---------QGTAATSAARERGEGFQQAVAAH 152
Cdd:cd06273 78 QVPYVLTW-SYDEDSPHPSIGFDNRAAAARAAQH----------LLDLghrriavisGPTAGNDRARARLAGIRDALAER 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 153 KFNVLASQ--PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndg 227
Cdd:cd06273 147 GLELPEERvvEAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISvpeDLSITGFDDLE--------- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
1DRK_A 228 kLAA-------TIAQLPDQIgakGVETADKV---LKGEKVQAKYPVDLKLVVKQ 271
Cdd:cd06273 218 -LAAhlsppltTVRVPAREI---GELAARYLlalLEGGPPPKSVELETELIVRE 267
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
3-252 |
5.47e-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: 380505 [Multi-domain] Cd Length: 267 Bit Score: 91.96 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDavGNAV-KMANQA 81
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQ--GSEAlELLEEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQaTKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIE-LQGTAATS-AARERGEGFQQAVAAHKFN---- 155
Cdd:cd06282 79 GVPYVLLFNQ-TENSSHPFVSVDNRLASYDVAEYLIAL---GHRRIAmVAGDFSASdRARLRYQGYRDALKEAGLKpipi 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 156 --VLASQPADFDRIKglnvmqNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEkaVNDGKLa 230
Cdd:cd06282 155 veVDFPTNGLEEALT------SLLSGPNPPTALFCSNDLLALSVISALRRLGIRvpdDVSVIGFDGIAIGE--LLTPTL- 225
|
250 260
....*....|....*....|..
1DRK_A 231 ATIAQLPDQIgakGVETADKVL 252
Cdd:cd06282 226 ATVVQPSRDM---GRAAADLLL 244
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
3-221 |
8.90e-22 |
|
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: 91.49 E-value: 8.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD-SQNNPAKELANVQDLT---VRGtkILLINPTDSDAvgNAVKMA 78
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATvDEDDPASVREALDRLLsqrVDG--IIVIAPDEAVL--EALRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 79 NqANIPVITLDrqATKGEVVSHIASDNVLGGKIAGDYIAkkaGEGAKVI-ELQGTAATSAARERGEGFQQAVAAHKFNVL 157
Cdd:cd01574 77 P-PGLPVVIVG--SGPSPGVPTVSIDQEEGARLATRHLL---ELGHRRIaHIAGPLDWVDARARLRGWREALEEAGLPPP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1DRK_A 158 ASQPADFDRIKGLNVMQNLLtAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGE 221
Cdd:cd01574 151 PVVEGDWSAASGYRAGRRLL-DDGPVTAVFAANDQMALGALRALHERGLRvpeDVSVVGFDDIPEAA 216
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
33-260 |
1.18e-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: 91.58 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 33 NLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIA 112
Cdd:cd19995 34 KVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPADYYVSFDNVAVGEAQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 113 GDYIAK----KAGEGAKVIELQGTAATSAARERGEG----FQQAVAAHKFNVLASQPA-DFDRIKGLNVMQNLLTAHP-D 182
Cdd:cd19995 114 AQSLVDhlkaIGKKGVNIVMINGSPTDNNAGLFKKGahevLDPLGDSGELKLVCEYDTpDWDPANAQTAMEQALTKLGnN 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DRK_A 183 VQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQAK 260
Cdd:cd19995 194 IDGVLSANDGLAGGAIAALKAQGlAGKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGETPPSD 272
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
3-257 |
1.41e-21 |
|
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380649 [Multi-domain] Cd Length: 304 Bit Score: 91.54 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd19994 1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKGEVVSHIAS-DNVLGGKIAGDYIAKKA----GEGAKVIEL-QGTAATSAARERGEG----FQQAVAAH 152
Cdd:cd19994 81 IPVIAYDRLIMNTDAVDYYVTfDNEKVGELQGQYLVDKLglkdGKGPFNIELfAGSPDDNNAQLFFKGamevLQPYIDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 153 KFnVLASQPADFDRI--------KGLNVMQNLLTAHP----DVQAVFAQNDEMALGALRALQTAGK-SDVM--VVGFDGT 217
Cdd:cd19994 161 TL-VVRSGQTTFEQVatpdwdteTAQARMETLLSAYYtggkKLDAVLSPNDGIARGVIEALKAAGYdTGPWpvVTGQDAE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
1DRK_A 218 PDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKV 257
Cdd:cd19994 240 DASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEV 279
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
3-261 |
3.03e-21 |
|
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: 89.92 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAvgNAVKMANQAN 82
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNN--DAYLELAQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQaTKGEVVSHIASDNVLGGKIAGDYIAKKAGEgaKVIELQGTAATSAAR-ERGEGFQQAVAAHKFN--VLAS 159
Cdd:cd06283 79 LPVVLVDRQ-IEPLNWDTVVTDNYDATYEATEHLKEQGYE--RIVFVTEPIKGISTRrERLQGFLDALARYNIEgdVYVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPADFDRIKglNVMQNLLTAHPDVQ-AVFAQNDEMALGALRALQTAGKS---DVMVVGFDgTPDGEKAVNDGklAATIAQ 235
Cdd:cd06283 156 EIEDTEDLQ--QALAAFLSQHDGGKtAIFAANGVVLLRVLRALKALGIRipdDVGLCGFD-DWDWADLIGPG--ITTIRQ 230
|
250 260
....*....|....*....|....*.
1DRK_A 236 LPDQIGAKGVETADKVLKGEKVQAKY 261
Cdd:cd06283 231 PTYEIGKAAAEILLERIEGDSGEPKE 256
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
3-218 |
3.45e-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: 89.86 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDL---TVRGtkILLINPTDSDAvgnAVKMAN 79
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALlsrRPAG--LILTGTEHTPA---TRKLLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVI-TLDRQATKGEVVshIASDNVLGGKIAGDYIAKKageGAKVIELQGTAATSA--ARERGEGFQQAVAAHKFN- 155
Cdd:cd01575 76 AAGIPVVeTWDLPDDPIDMA--VGFSNFAAGRAMARHLIER---GYRRIAFVGARLDGDsrARQRLEGFRDALAEAGLPl 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DRK_A 156 ---VLASQPADFDRikGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTP 218
Cdd:cd01575 151 plvLLVELPSSFAL--GREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRvpgDIAIAGFGDLD 217
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
3-270 |
2.41e-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: 87.61 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKE---LANVQDLTVRGtkiLLINPTDSdavgnAVKMAN 79
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEreiLESLLDQNVDG---LIIEPTKS-----ALPNPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 --------QANIPVITLDRqATKGEVVSHIASDNVLGGKIAGDYIA----KKAGEGAKVIELQGtaatsaaRERGEGFQQ 147
Cdd:cd01541 73 ldlyeelqKKGIPVVFINS-YYPELDAPSVSLDDEKGGYLATKHLIdlghRRIAGIFKSDDLQG-------VERYQGFIK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 148 AVAAHKF-----NVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPD 219
Cdd:cd01541 145 ALREAGLpidddRILWYSTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRvpeDLSVVGFDDSYL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
1DRK_A 220 GEKAvnDGKLaATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVK 270
Cdd:cd01541 225 ASLS--EPPL-TSVVHPKEELGRKAAELLLRMIEEGRKPESVIFPPELIER 272
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
61-241 |
2.59e-20 |
|
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 87.78 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 61 LLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAArE 140
Cdd:cd19969 60 IAVSAIDPEALTPTINKAVDAGIPVVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQPNHE-E 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 141 RGEGFQQAVAAHK-FNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTP 218
Cdd:cd19969 139 RVEGFKEAFAEYPgIEVVAVGDDNDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTgKVKIVAFDDDP 218
|
170 180
....*....|....*....|...
1DRK_A 219 DGEKAVNDGKLAATIAQLPDQIG 241
Cdd:cd19969 219 ETLDLIKDGVIDASIAQRPWMMG 241
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
13-261 |
3.49e-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: 87.25 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 13 NPFFVSLKDGAQKEADKLGYNLVvLDSQNNPAKELANVQDLtVRGTKI---LLINPTDSDAVgnaVKMANQANIPVITLD 89
Cdd:cd06294 16 NPFFSEVLRGISQVANENGYSLL-LATGNTEEELLEEVKRM-VRGRRVdgfILLYSKEDDPL---IEYLKEEGFPFVVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 90 RQATKGEVvSHIASDNVLGGKIAGDYIAKKageGAKVIE-LQGTAATSAARERGEGFQQAVAAHKFNVLASQ--PADFDR 166
Cdd:cd06294 91 KPLDDNDV-LYVDNDNVQAGYEATEYLIDK---GHKRIAfIGGDKNLVVSIDRLQGYKQALKEAGLPLDDDYilLLDFSE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 167 IKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKAVNdgkLAATIAQLPDQIGAK 243
Cdd:cd06294 167 EDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRvpeDVSIISFNNSPLAELASP---PLTSVDINPYELGRE 243
|
250
....*....|....*...
1DRK_A 244 GVETADKVLKGEKVQAKY 261
Cdd:cd06294 244 AAKLLINLLEGPESLPKN 261
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
3-271 |
4.05e-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: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVV-------STLNNPFFVSLKDGAQKEADKLGYNLVVLdsqnNPAKELANVQDLTVRGTK---ILLINPTDSDAVg 72
Cdd:cd06295 5 TIAVVVpmdphgdQSITDPFFLELLGGISEALTDRGYDMLLS----TQDEDANQLARLLDSGRAdglIVLGQGLDHDAL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 73 naVKMANQaNIPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAKKageGAKVIELQGTAATSAARERGEGFQQAVAAH 152
Cdd:cd06295 80 --RELAQQ-GLPMVVWGAPEDGQSYCS-VGSDNVKGGALATEHLIEI---GRRRIAFLGDPPHPEVADRLQGYRDALAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 153 KFNVLASQ--PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndg 227
Cdd:cd06295 153 GLEADPSLllSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISvpgDVAVVGYDDIP--------- 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
1DRK_A 228 kLAA-------TIAQLPDQIGAKGVETADKVLKGEKVQAKyPVDLKLVVKQ 271
Cdd:cd06295 224 -LAAyfrppltTVRQDLALAGRLLVEKLLALIAGEPVTSS-MLPVELVVRE 272
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
3-269 |
5.15e-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: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGTKILLINPTDSDavgnaVKMAN 79
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVargSAGVVLVTSDPTSRQ-----LRLLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVITLD-RQATKGEVVShIASDNVLGGKIAGDYIAkkaGEGAKVIE-LQGTAATSAARERGEGFQQAVAAH----- 152
Cdd:cd06296 76 SAGIPFVLIDpVGEPDPDLPS-VGATNWAGGRLATEHLL---DLGHRRIAvITGPPRSVSGRARLAGYRAALAEAgiavd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 153 KFNVLASqpaDFDRIKGLNVMQNLLtAHPDV-QAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKAVndgK 228
Cdd:cd06296 152 PDLVREG---DFTYEAGYRAARELL-ELPDPpTAVFAGNDEQALGVYRAARALGLRvpdDLSVIGFDDTPPARWTS---P 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
1DRK_A 229 LAATIAQLPDQIGAKGVETADKVLKGEKVQAKyPVDL--KLVV 269
Cdd:cd06296 225 PLTTVHQPLREMGAVAVRLLLRLLEGGPPDAR-RIELatELVV 266
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
3-217 |
2.12e-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: 84.98 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTK--ILLINPTDSDAVGNAVkmaNQ 80
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDglILTPGDEDDPELAAAL---AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQAtkGEVVSHIASDNVLGGKIAGDYIakkAGEGAKVIEL-QGTAATSAARERGEGFQQAVAAHKFNV--- 156
Cdd:cd06281 78 LDIPVVLIDRDL--PGDIDSVLVDHRSGVRQATEYL---LSLGHRRIALlTGGPDIRPGRERIAGFKAAFAAAGLPPdpd 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1DRK_A 157 ---LASQPADFdrikGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGT 217
Cdd:cd06281 153 lvrLGSFSADS----GFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRipgDLSVVSIGDS 215
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
3-271 |
2.31e-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: 84.91 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVV--LDSQNNPAKE--LANVQDLTVRGtkILLINP-TDSDAVgnaVKM 77
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVepCDSDDEDLADrlRRFLSRSRPDG--VILTPPlSDDPAL---LDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 78 ANQANIPVITLDRqATKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIEL-QGTAATSAARERGEGFQQAVAAH--KF 154
Cdd:cd01545 76 LDELGIPYVRIAP-GTDDDRSPSVRIDDRAAAREMTRHLIAL---GHRRIGFiAGPPDHGASAERLEGFRDALAEAglPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 155 NVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavndgkLAA 231
Cdd:cd01545 152 DPDLVVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRvpdDLSVAGFDDSP----------IAR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
1DRK_A 232 -------TIAQLPDQIGAKGVET-ADKVLKGEKVQAKYPVDLKLVVKQ 271
Cdd:cd01545 222 lvwppltTVRQPIAEMARRAVELlIAAIRGAPAGPERETLPHELVIRE 269
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
4-262 |
2.70e-19 |
|
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: 84.92 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 4 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD----SQNNPAKELANVQDLTvRGTKILLINPTDSDAVGNAVKMAN 79
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRihfvDSLDPEALAAALRRLA-AGCDGVALVAPDHPLVRAAIDELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAK-KAGEGAKVIELQGTAATSAARERGEGFQQAVAAH--KFNV 156
Cdd:cd06307 81 ARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRfLGRRPGKVLVILGSHRFRGHEEREAGFRSVLRERfpDLTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 157 LASQPADFDRIKGLNVMQNLLTAHPDVQAVF---AQNDemalGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAAT 232
Cdd:cd06307 161 LEVLEGLDDDELAYELLRELLARHPDLVGIYnagGGNE----GIARALREAGRArRVVFIGHELTPETRRLLRDGTIDAV 236
|
250 260 270
....*....|....*....|....*....|
1DRK_A 233 IAQLPDQIGAKGVETADKVLKGEKVQAKYP 262
Cdd:cd06307 237 IDQDPELQARRAIEVLLAHLGGKGPAPPQP 266
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
23-268 |
3.49e-19 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380653 [Multi-domain] Cd Length: 302 Bit Score: 85.03 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 23 AQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATkGEVVSHIA 102
Cdd:cd19998 25 AKQPPYADKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVVD-EPCAYNVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 103 SDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNVLASQPADFDRIKGLNVMQNLLTAHP 181
Cdd:cd19998 104 TDQAKAGEQTAQWLVDKLGGKGNILMVRGVPGTSVDRDRYEGAKEVFKKYpDIKVVAEYYGNWDDGTAQKAVADALAAHP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 182 DVQAVFAQNDEMalGALRALQTAGKsDVMVVGFDGTPDGEKAVND---GKLAATIAQLPDQIGAKGVETADKVLKGEKVQ 258
Cdd:cd19998 184 DVDGVWTQGGET--GVIKALQAAGH-PLVPVGGEAENGFRKAMLEplaNGLPGISAGSPPALSAVALKLAVAVLEGEKEP 260
|
250
....*....|
1DRK_A 259 AKYPVDLKLV 268
Cdd:cd19998 261 KTIELPLPWV 270
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
14-237 |
3.03e-18 |
|
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: 81.99 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 14 PFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQD-LTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQA 92
Cdd:cd19966 13 PFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEaIAAKPDGIAIMGHPGDGAYTPLIEAAKKAGIIVTSFNTDL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 93 TKGEVVS----HIASDNVLGGKIAGDYIAKKAG--EGAKVIELQGTAATSAARERGEGFQQAVAAH--KFNVLASQPADF 164
Cdd:cd19966 93 PKLEYGDcglgYVGADLYAAGYTLAKELVKRGGlkTGDRVFVPGLLPGQPYRVLRTKGVIDALKEAgiKVDYLEISLEPN 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1DRK_A 165 DRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK--SDVMVVGFDGTPDGEKAVNDGKLAATIAQLP 237
Cdd:cd19966 173 KPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKkpGEIPVAGFDLSPATVQAIKSGYVNATIDQQP 247
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
3-264 |
4.03e-18 |
|
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: 81.94 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNlVVLD--SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:cd20003 1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVD-VTYDgpTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 ANIPVITLDRQATKG--EVVSHIASDNVLGgKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH--KFNV 156
Cdd:cd20003 80 KGIKVVTWDSDVNPDarDFFVNQATPEGIG-KTLVDMVAEQTGEKGKVAIVTSSPTATNQNAWIKAMKAYIAEKypDMKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 157 LASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQnDEMAL-GALRALQTAGKS-DVMVVGFdGTPDGEKA-VNDGKLAATI 233
Cdd:cd20003 159 VTTQYGQEDPAKSLQVAENILKAYPDLKAIIAP-DSVALpGAAEAVEQLGRTgKVAVTGL-STPNVMRPyVKDGTVKSVV 236
|
250 260 270
....*....|....*....|....*....|.
1DRK_A 234 AQLPDQIGAKGVETADKVLKGEKVQAKYPVD 264
Cdd:cd20003 237 LWDVVDLGYLAVYVARALADGTLLKVGDFFV 267
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
3-268 |
5.33e-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: 81.00 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTK-ILLINPTDSDAvgnAVKMANQA 81
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDgIILFATEITDE---HRKALKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQATKGEVVSHiasDNVLGGKIAGDYIAKKageGAKVIELQGTAAT--SAARERGEGFQQAVAAHKFNVLAS 159
Cdd:cd01542 78 KIPVVVLGQEHEGFSCVYH---DDYGAGKLLGEYLLKK---GHKNIAYIGVDEEdiAVGVARKQGYLDALKEHGIDEVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 160 QPADFDRIKGLNVMQNLLTAHPDvQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEkaVNDGKLaATIAQL 236
Cdd:cd01542 152 VETDFSMESGYEAAKELLKENKP-DAIICATDNIALGAIKALRELGIKipeDISVAGFGGYDLSE--FVSPSL-TTVKFD 227
|
250 260 270
....*....|....*....|....*....|..
1DRK_A 237 PDQIGAKGVETADKVLKGEKVQAKYPVDLKLV 268
Cdd:cd01542 228 YEEAGEKAAELLLDMIEGEKVPKKQKLPYELI 259
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
11-223 |
6.76e-18 |
|
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: 81.10 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 11 LNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAkELANVQDLTVRGtkILLINPTDSDAVgnaVKMANQANIPVITLDR 90
Cdd:cd06279 14 FSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGS-AAAAVRNAAVDG--FIVYGLSDDDPA---VAALRRRGLPLVVVDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 91 QATKGevVSHIASDNVLGGKIAGDY-----------IAKKAGEGAKVIELQG----TAATSAARERGEGFQQAVAAHKFN 155
Cdd:cd06279 88 PAPPG--IPSVGIDDRAAARAAARHlldlghrriaiLSLRLDRGRERGPVSAerlaAATNSVARERLAGYRDALEEAGLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1DRK_A 156 VLASQP---ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEKA 223
Cdd:cd06279 166 LDDVPVveaPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRvpeDLSVTGFDDIPEAAAA 239
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
3-220 |
1.14e-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: 80.29 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVST----LNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAkELANVQDLtVRGTK---ILLINPTDSDAvgnAV 75
Cdd:cd20010 1 AIGLVLPLdpgdLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGED-ELATYRRL-VERGRvdgFILARTRVNDP---RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 76 KMANQANIPVITLDRQATKGEVvSHIASDNVLGGKIAgdyIAKKAGEGAKVIEL-QGTAATSAARERGEGFQQAVAAHKF 154
Cdd:cd20010 76 AYLLERGIPFVVHGRSESGAPY-AWVDIDNEGAFRRA---TRRLLALGHRRIALlNGPEELNFAHQRRDGYRAALAEAGL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1DRK_A 155 NVLAS--QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDG 220
Cdd:cd20010 152 PVDPAlvREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSpgkDVSVIGHDDLLPA 222
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
3-247 |
2.29e-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: 79.62 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLN----NPFFVSLKDGAQKEADKLGYNlVVLDSQNNPAKELANVQDLT----VRGtkILLINPTDSDAVGNA 74
Cdd:cd06292 1 LIGYVVPELPggfsDPFFDEFLAALGHAAAARGYD-VLLFTASGDEDEIDYYRDLVrsrrVDG--FVLASTRHDDPRVRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 75 VKmanQANIPVITLDRQATKGEVvSHIASDNVLGGKIAGDYIAKKageGAKVIEL-QGTAATSAARERGEGFQQAVAAHK 153
Cdd:cd06292 78 LH---EAGVPFVAFGRANPDLDF-PWVDVDGAAGMRQAVRHLIAL---GHRRIGLiGGPEGSVPSDDRLAGYRAALEEAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 154 fnvLASQPA-----DFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgekavn 225
Cdd:cd06292 151 ---LPFDPGlvvegENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRvgrDVSVVGFDDSP------- 220
|
250 260
....*....|....*....|....*....
1DRK_A 226 dgkLAA-------TIAQLPDQIGAKGVET 247
Cdd:cd06292 221 ---LAAfthppltTVRQPIDEIGRAVVDL 246
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
100-271 |
4.56e-17 |
|
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: 79.34 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 100 HIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATsAARERGEGFQQAVAAH-KFNVLASQPADFDRIKGLNVMQNLLT 178
Cdd:cd06303 136 YVGFDHAEGSRMLAKHFIKIFPEEGKYAILYLTEGY-VSDQRGDTFIDEVARHsNLELVSAYYTDFDRESAREAARALLA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 179 AHPDVQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQigaKGVETADKV---LKG 254
Cdd:cd06303 215 RHPDLDFIYACSTDIALGAIDALQELGREtDIMINGWGGGSAELDALQKGGLDVTVMRMNDD---NGIAMAEAIkldLEG 291
|
170
....*....|....*..
1DRK_A 255 EKVQAKYPVDLKLVVKQ 271
Cdd:cd06303 292 REVPTVYAGDFELVTKG 308
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
12-215 |
1.49e-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: 77.28 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 12 NNPFFVSLKDGAQKEADKLGYNL--VVLDSQNNPAKELANVQDLTVRGTkILLINPTDSDAVgnavKMANQANIPVITLD 89
Cdd:cd06277 17 ETPFFSELIDGIEREARKYGYNLliSSVDIGDDFDEILKELTDDQSSGI-ILLGTELEEKQI----KLFQDVSIPVVVVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 90 RQAtkgEVVS--HIASDNVLGGKIAGDYIAKKageGAKVIE-LQGTAATSAARERGEGFQQAVAAHKFnvlasqPADFDR 166
Cdd:cd06277 92 NYF---EDLNfdCVVIDNEDGAYEAVKYLVEL---GHTRIGyLASSYRIKNFEERRRGFRKAMRELGL------SEDPEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1DRK_A 167 IKGLNV--------MQNLLTAHPDV-QAVFAQNDEMALGALRALQTAGKS---DVMVVGFD 215
Cdd:cd06277 160 EFVVSVgpegaykdMKALLDTGPKLpTAFFAENDIIALGCIKALQEAGIRvpeDVSVIGFD 220
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
3-246 |
3.18e-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: 76.35 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVV--LDSQNNPAKELANVqdLTVRGTKILLINPTDSDAVGNAVKMANQ 80
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIfpLLSEYRLEKYLRNS--TLAYQCDGLVMASLDLTELFEEVIVPTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 81 AniPVITLDRQAtkgEVVSHIASDNVLGGKIAGDYIAKKaGEG---AKVIELQGTAATSAARERGEGFQQAVAAHKFNVL 157
Cdd:cd06297 79 K--PVVLIDANS---MGYDCVYVDNVKGGFMATEYLAGL-GEReyvFFGIEEDTVFTETVFREREQGFLEALNKAGRPIS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 158 ASQP--ADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGTPDGEKAVndgklAAT 232
Cdd:cd06297 153 SSRMfrIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLrvgEDVAVIGFDGQPWAASPG-----LTT 227
|
250
....*....|....
1DRK_A 233 IAQLPDQIGAKGVE 246
Cdd:cd06297 228 VRQPVEEMGEAAAK 241
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
3-270 |
9.44e-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: 74.89 E-value: 9.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTvrgTKIL--LI-----NPTDsdavgnaV 75
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLK---TKQIdgLIitsreNDWE-------V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 76 KMANQANIPVITLDRqaTKGEVVSHIASDNVLGGKIAGDYIAKKageGAK--VIELQGTAATSA-ARERGEGFQQAVAAH 152
Cdd:cd06286 71 IEPYAKYGPIVLCEE--TDSPDIPSVYIDRYEAYLEALEYLKEK---GHRkiGYCLGRPESSSAsTQARLKAYQDVLGEH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 153 KfnvLASQPAD-FDRIK----GLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDGEkAV 224
Cdd:cd06286 146 G---LSLREEWiFTNCHtiedGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRvpeDLAVIGFDNQPISE-LL 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
1DRK_A 225 NdgklAATIAQLPDQIGAKGVETADKVLKGEKVQaKYPVDLKLVVK 270
Cdd:cd06286 222 N----LTTIDQPLEEMGKEAFELLLSQLESKEPT-KKELPSKLIER 262
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
18-257 |
1.41e-15 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 75.37 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 18 SLKD--------GAQKEADKLGYNLVVLD--SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMAnQANIPVIT 87
Cdd:PRK10936 55 HLKDsywlsvnyGMVEEAKRLGVDLKVLEagGYYNLAKQQQQLEQCVAWGADAILLGAVTPDGLNPDLELQ-AANIPVIA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 88 LDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEG---AKVIELQGTAATSAARERGEGFQQAVAAHKFNVLASQPADF 164
Cdd:PRK10936 134 LVNGIDSPQVTTRVGVSWYQMGYQAGRYLAQWHPKGskpLNVALLPGPEGAGGSKAVEQGFRAAIAGSDVRIVDIAYGDN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 165 DRIKGLNVMQNLLTAHPDVQAVF--AQNDEMALGALRALQTAGKsdVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGA 242
Cdd:PRK10936 214 DKELQRNLLQELLERHPDIDYIAgsAVAAEAAIGELRGRNLTDK--IKLVSFYLSHQVYRGLKRGKVLAAPSDQMVLQGR 291
|
250
....*....|....*
1DRK_A 243 KGVETADKVLKGEKV 257
Cdd:PRK10936 292 LAIDQAVRQLEGAPV 306
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
3-218 |
6.95e-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: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVST-----LNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANvqdlTVRGtkILLINPTDSDAVgNAVKM 77
Cdd:cd01544 1 TIGIIQWYseeeeLEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLESLLE----KVDG--IIAIGKFSKEEI-EKLKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 78 ANQ-----------ANIPVITLD-RQATKgEVVSHIASdnvLG-GKIAgdYIakkageGAKVIELQGTAATSAARERGeg 144
Cdd:cd01544 74 LNPnivfvdsnpdpDGFDSVVPDfEQAVR-QALDYLIE---LGhRRIG--FI------GGKEYTSDDGEEIEDPRLRA-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 145 FQQAVAAH----KFNVLAsqpADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGT 217
Cdd:cd01544 140 FREYMKEKglynEEYIYI---GEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKvpeDISIISFNDI 216
|
.
1DRK_A 218 P 218
Cdd:cd01544 217 E 217
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
27-271 |
1.73e-14 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 72.33 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 27 ADKLGYNLVV--LDSQNNPAKELAnVQDLTVRGTKILLIN-PTDSDavgNAVKMANQ-ANIPVITLDRQATKgeVVSHIA 102
Cdd:PRK09526 89 ADQLGYSVVIsmVERSGVEACQAA-VNELLAQRVSGVIINvPLEDA---DAEKIVADcADVPCLFLDVSPQS--PVNSVS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 103 SDNVLGGKIAGDYIAkkAGEGAKVIELQGTAATSAARERGEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPD 182
Cdd:PRK09526 163 FDPEDGTRLGVEHLV--ELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQPIAVREGDWSAMSGYQQTLQMLREGPV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 183 VQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPDgeKAVNDGKLaATIAQLPDQIGAKGVETADKVLKGEKVQA 259
Cdd:PRK09526 241 PSAILVANDQMALGVLRALHESGLRvpgQISVIGYDDTED--SSYFIPPL-TTIKQDFRLLGKEAVDRLLALSQGQAVKG 317
|
250
....*....|..
1DRK_A 260 KYPVDLKLVVKQ 271
Cdd:PRK09526 318 SQLLPTSLVVRK 329
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
126-259 |
8.76e-14 |
|
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: 67.36 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 126 VIELQGTAATSAARERGEGFQQAVAAHKFNVLASQ--PADFDRIKGLNVMQNLLTAHPDvqAVFAQNDEMALGALRALQT 203
Cdd:pfam13377 12 LIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLyaGDDEAEAAAARERLRWLGALPT--AVFVANDEVALGVLQALRE 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
1DRK_A 204 AGKS---DVMVVGFDGTPDGEKAVNDgklAATIAQLPDQIGAKGVETADKVLKGEKVQA 259
Cdd:pfam13377 90 AGLRvpeDLSVIGFDDSPLAALVSPP---LTTVRVDAEELGRAAAELLLDLLNGEPAPP 145
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
3-215 |
4.87e-13 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 67.83 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLI----NPTDSDAVgnavkMA 78
Cdd:PRK10703 61 SIGLLATSSEAPYFAEIIEAVEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVmcseYPEPLLAM-----LE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 79 NQANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIElqGTAATSAARERGEGFQQAVAAHKFNVLA 158
Cdd:PRK10703 136 EYRHIPMVVMDWGEAKADFTDAIIDNAFEGGYLAGRYLIERGHRDIGVIP--GPLERNTGAGRLAGFMKAMEEANIKVPE 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
1DRK_A 159 S--QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFD 215
Cdd:PRK10703 214 EwiVQGDFEPESGYEAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGlrvPQDISVIGYD 275
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
3-202 |
8.15e-13 |
|
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: 66.46 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLI----NPTDSDAVGNAvkma 78
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVapstPPDDIYYLCQA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 79 nqANIPVITLDRQATKGEVVShIASDNVLGGKIAGDYIAkkAGEGAKVIELQGTAATSAARERGEGFQQAVAAHKF---- 154
Cdd:cd06274 77 --AGLPVVFLDRPFSGSDAPS-VVSDNRAGARALTEKLL--AAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGItegd 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
1DRK_A 155 -NVLASqpaDFDRIKGLNVMQNLLTAHPDV-QAVFAQNDEMALGALRALQ 202
Cdd:cd06274 152 dWILAE---GYDRESGYQLMAELLARLGGLpQALFTSSLTLLEGVLRFLR 198
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
3-257 |
1.57e-12 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380652 [Multi-domain] Cd Length: 305 Bit Score: 66.16 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEA-----DKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKM 77
Cdd:cd19997 1 VIALSNSYAGNTWRQQMVDAFEEAAkkakaDGLIADYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 78 ANQANIPVITLDRQATKgEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAH-KFNV 156
Cdd:cd19997 81 ACDAGIKVVVFDSGVTE-PCAYILNNDFEDYGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKKYpDLKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 157 LASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEmALGALRALQTAGKsDVMVVGFDGTPDGEK---AVNDGKLAATI 233
Cdd:cd19997 160 VAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGD-GYGAAQAFEAAGR-PLPIIIGGNRGEFLKwwqEEYAKNGYETV 237
|
250 260
....*....|....*....|....*
1DRK_A 234 AQLPDQ-IGAKGVETADKVLKGEKV 257
Cdd:cd19997 238 SVSTDPgQGSAAFWVALDILNGKDV 262
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
25-259 |
7.93e-12 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 64.38 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 25 KEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSHIASD 104
Cdd:PRK10355 49 KKAESLGAKVFVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDFYISFD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 105 NVLGGKIAGDYIAKKAGEGAKVIeLQGTAATSAARERGEG----FQQAVAAHKFNVLASQPAD-FDRIKGLNVMQNLLTA 179
Cdd:PRK10355 129 NEKVGELQAKALVDKVPQGNYFL-MGGSPVDNNAKLFRAGqmkvLKPYIDSGKIKVVGDQWVDgWLPENALKIMENALTA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 180 HPD-VQAVFAQNDEMALGALRALQTAGKS-DVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKV 257
Cdd:PRK10355 208 NNNkIDAVVASNDATAGGAIQALSAQGLSgKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEP 287
|
..
1DRK_A 258 QA 259
Cdd:PRK10355 288 KA 289
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
3-247 |
8.16e-11 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380629 [Multi-domain] Cd Length: 270 Bit Score: 61.03 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVS---TLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKEL---ANVQDLTVRGtkILLINPTDSDAVgnavK 76
Cdd:cd19974 1 NIAVLIPerfFGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELnlpSIISEEKVDG--IIILGEISKEYL----E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 77 MANQANIPVITLDRQATKGEVvSHIASDNVLGGKIAGDYIAKKageGAKVIELQGT-AATSAARERGEGFQQAVAAHKfn 155
Cdd:cd19974 75 KLKELGIPVVLVDHYDEELNA-DSVLSDNYYGAYKLTSYLIEK---GHKKIGFVGDiNYTSSFMDRYLGYRKALLEAG-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 156 vLASQPADF---DRIKGLNVMQNLLTA----HPDvqAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTPdgEKAVN 225
Cdd:cd19974 149 -LPPEKEEWlleDRDDGYGLTEEIELPlklmLPT--AFVCANDSIAIQLIKALKEKGYRvpeDISVVGFDNIE--LAELS 223
|
250 260
....*....|....*....|..
1DRK_A 226 DGKLaATIAQLPDQIGAKGVET 247
Cdd:cd19974 224 TPPL-TTVEVDKEAMGRRAVEQ 244
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
3-218 |
3.32e-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: 59.23 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDL---TVRGtkILLINPTDSDavgNAVKMAN 79
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMlskQVDG--IIFMGDELTE---EIREEFK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVI---TLDRQATkgevvshIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAA--RERGEGFQQAV--AAH 152
Cdd:cd06298 76 RSPVPVVlagTVDSDHE-------IPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYInnDKKLQGYKRALeeAGL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1DRK_A 153 KFN---VLAsqpADFDRIKGLNVMQNLLTA-HPDvqAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTP 218
Cdd:cd06298 149 EFNeplIFE---GDYDYDSGYELYEELLESgEPD--AAIVVRDEIAVGLLNAAQDRGLKvpeDLEIIGFDNTR 216
|
|
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
24-233 |
1.32e-09 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 57.82 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 24 QKEADKL-GYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSH-- 100
Cdd:PRK15395 47 EKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYdk 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 101 ---IASDNVLGGKIAGDYIAK--KAGEGakvIELQGTAATSAARERGE-GFQQAVAAHKFNV------------LASQPA 162
Cdd:PRK15395 127 ayyVGTDSKESGIIQGDLIAKhwKANPA---WDLNKDGKIQYVLLKGEpGHPDAEARTTYVIkelndkgikteqLQLDTA 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1DRK_A 163 DFDRIKGLNVMQNLLTAHP--DVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATI 233
Cdd:PRK15395 204 MWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTV 276
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
4-221 |
5.68e-09 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 55.87 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 4 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQaNI 83
Cdd:PRK10014 67 IGLIVRDLSAPFYAELTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMAEEK-GI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 84 PVITLDRqATKGEVVSHIASDNVLGGKIAGDYIAKKageGAKVIELQGTAATSAAR-ERGEGF-----QQAVAAHKFNVL 157
Cdd:PRK10014 146 PVVFASR-ASYLDDVDTVRPDNMQAAQLLTEHLIRN---GHQRIAWLGGQSSSLTRaERVGGYcatllKFGLPFHSEWVL 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DRK_A 158 ---ASQPADFDrikglnVMQNLLTAHPDVQAVFAQNDEMALGA----LRALQTAGKSD--------VMVVGFDGTPDGE 221
Cdd:PRK10014 222 ectSSQKQAAE------AITALLRHNPTISAVVCYNETIAMGAwfglLRAGRQSGESGvdryfeqqVALAAFTDVPEAE 294
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
3-255 |
7.99e-09 |
|
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: 55.34 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD-SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd20000 1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGpTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQATKGEVVSHIASDNVLG-GKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHKF---NVL 157
Cdd:cd20000 81 GIKVVTFDSDVAPEARDLFVNQADADGiGRAQVDMMAELIGGEGEFAILSATPTATNQNAWIDAMKKELASPEYagmKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 158 ASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFdGTPDGEKA-VNDGKLAATIAQ 235
Cdd:cd20000 161 KVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGkVKVTGL-GLPSEMAKyVKDGTVPAFALW 239
|
250 260
....*....|....*....|
1DRK_A 236 LPDQIGAKGVETADKVLKGE 255
Cdd:cd20000 240 NPIDLGYLAAYAAAALAQGE 259
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
3-257 |
1.40e-08 |
|
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: 54.59 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD-SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd20001 1 TIAVVVKVTGIAWFDRMETGVEQFAKDTGVNVYQIGpATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITldrqatkgevvsHIAS------------DNVLGGKIAGDYIAKKAGEGAKVIELQG--TAATSAARERGE-GFQ 146
Cdd:cd20001 81 GIVVIT------------HEASnlknvdydveafDNAAYGAFIMDKLAEAMGGKGKYVTFVGslTSTSHMEWANAAvAYQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 147 QAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFdGTPDGEKA-V 224
Cdd:cd20001 149 KANYPDMLLVTDRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGkIAVVGT-GLPSVAGEyL 227
|
250 260 270
....*....|....*....|....*....|...
1DRK_A 225 NDGKLAATIAQLPDQIGAKGVETADKVLKGEKV 257
Cdd:cd20001 228 EDGTIDYIQFWDPADAGYAMNALAVMVLEGEKI 260
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
3-256 |
1.65e-08 |
|
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: 54.25 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLD-SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQA 81
Cdd:cd20002 1 TIVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVGpADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHKFN---VLA 158
Cdd:cd20002 81 GIVVITHESPGQKGADWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKYPNmkqVTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 159 SQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG-KSDVMVVGFDGTPDGEKAVNDGKLAATIAQLP 237
Cdd:cd20002 161 RIPGGEDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGlKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDP 240
|
250
....*....|....*....
1DRK_A 238 DQIGAKGVETADKVLKGEK 256
Cdd:cd20002 241 ADAGYAMVYIAKMLLDGKR 259
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
33-205 |
5.94e-08 |
|
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: 52.63 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 33 NLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVIT-------LDRQATKGEVVSHIASDN 105
Cdd:COG0683 46 ELVVEDDASDPDTAVAAARKLIDQDKVDAIVGPLSSGVALAVAPVAEEAGVPLISpsatapaLTGPECSPYVFRTAPSDA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 106 VLgGKIAGDYIAKKAGeGAKVIELqgTAATSAARERGEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVqA 185
Cdd:COG0683 126 QQ-AEALADYLAKKLG-AKKVALL--YDDYAYGQGLAAAFKAALKAAGGEVVGEEYYPPGTTDFSAQLTKIKAAGPDA-V 200
|
170 180
....*....|....*....|
1DRK_A 186 VFAQNDEMALGALRALQTAG 205
Cdd:COG0683 201 FLAGYGGDAALFIKQAREAG 220
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
3-219 |
5.08e-07 |
|
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: 49.73 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVS---TLNNPFFVSLKDGAQKEADKLGYNLVVLDSQnnPAKELANVQDLT----VRGTKILLINPTDSdavgnAV 75
Cdd:cd06271 1 VIALVFPvteTELNGTVSE*VSGITEEAGTTGYHLLVWPFE--EAES*VPIRDLVetgsADGVILSEIEPNDP-----RV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 76 KMANQANIPVITLDRQATkGEVVSHIASDNVLGGKIAGDYIAkkaGEGAKVIELQGTAAT-SAARERGEGFQQAVAAHKF 154
Cdd:cd06271 74 QFLTKQNFPFVAHGRSD*-PIGHAWVDIDNEAGAYEAVERLA---GLGHRRIAFIVPPARySPHDRRLQGYVRA*RDAGL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1DRK_A 155 NVLAsQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDGTPD 219
Cdd:cd06271 150 TGYP-LDADTTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGlkiGEDVSIIGKDSAPF 216
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
3-188 |
3.60e-06 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 47.57 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLIN---PTDSDAVgnaVKMAN 79
Cdd:PRK11303 63 SIGLIIPDLENTSYARIAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVStslPPEHPFY---QRLQN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QAnIPVITLDRqATKGEVVSHIASDNVLGGKIAGDYIAKKAgegAKVIELQGT-AATSAARERGEGFQQAVAAHKFNVLA 158
Cdd:PRK11303 140 DG-LPIIALDR-ALDREHFTSVVSDDQDDAEMLAESLLKFP---AESILLLGAlPELSVSFEREQGFRQALKDDPREVHY 214
|
170 180 190
....*....|....*....|....*....|
1DRK_A 159 SQPADFDRIKGLNVMQNLLTAHPDVQAVFA 188
Cdd:PRK11303 215 LYANSFEREAGAQLFEKWLETHPMPDALFT 244
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-258 |
1.02e-05 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 45.87 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 61 LLINPTDSDAvgnAVKMANQANIPVITLDRQATKGEVVSHIasdNVLGGKIAGDYIAKKAGEGAKVIEL-QGTAATSAAR 139
Cdd:cd06287 61 IVVEPTVEDP---ILARLRQRGVPVVSIGRAPGTDEPVPYV---DLQSAATARLLLEHLHGAGARQVALlTGSSRRNSSL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 140 ERGEGFQQAVAAHKFN-VLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVgfd 215
Cdd:cd06287 135 ESEAAYLRFAQEYGTTpVVYKVPESEGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSvpeDLMVV--- 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....
1DRK_A 216 GTPDGEKA-VNDGKLAATIAQLpDQIGAKGVETADKVLKGEKVQ 258
Cdd:cd06287 212 TRYDGIRArTADPPLTAVDLHL-DRVARTAIDLLFASLSGEERS 254
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
2-218 |
1.28e-05 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 45.92 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 2 DTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINptdSDAVGNAVKMANQA 81
Cdd:PRK10401 60 DTIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVH---SKALSDDELAQFMD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 82 NIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKkagEGAKVIelqGTAATSAARE----RGEGFQQAVAAHKFNVL 157
Cdd:PRK10401 137 QIPGMVLINRVVPGYAHRCVCLDNVSGARMATRMLLN---NGHQRI---GYLSSSHGIEddamRRAGWMSALKEQGIIPP 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1DRK_A 158 ASQPA--DFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTP 218
Cdd:PRK10401 211 ESWIGtgTPDMQGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAiplHLSIIGFDDIP 276
|
|
| PRK15408 |
PRK15408 |
autoinducer 2 ABC transporter substrate-binding protein LsrB; |
2-266 |
2.20e-05 |
|
autoinducer 2 ABC transporter substrate-binding protein LsrB;
Pssm-ID: 237961 Cd Length: 336 Bit Score: 45.17 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 2 DTIALVVSTLNNPFFVSLKDGAQKEADKLGYNlVVLDSQNNP--AKELANVQDLTVRGTKILLINPTDSDAVGNAVKMAN 79
Cdd:PRK15408 24 ERIAFIPKLVGVGFFTSGGNGAKEAGKELGVD-VTYDGPTEPsvSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 80 QANIPVITLDRQaTKGEVVSHIASD---NVLGG---KIAGDYIAKKAgegAKVIELQGTAATSAARERGEGFQQAVAAH- 152
Cdd:PRK15408 103 QRGVKVLTWDSD-TKPECRSYYINQgtpEQLGSmlvEMAAKQVGKDK---AKVAFFYSSPTVTDQNQWVKEAKAKIAKEh 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 153 -KFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDgTPDGEKA-VNDGkla 230
Cdd:PRK15408 179 pGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRDKVAIVGFS-TPNVMRPyVKRG--- 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
1DRK_A 231 aTIAQ--LPD--QIGAKGVETADKVLKGEKVQAKYPVDLK 266
Cdd:PRK15408 255 -TVKEfgLWDvvQQGKISVYVANELLKKGKLNVGDSLDVP 293
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
78-215 |
2.77e-05 |
|
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: 44.50 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 78 ANQANIPVITLDRqATKGEVVSHIASDNVLGGKIAGDYIakkagegakvIELQ-------GTAATSAARERGEGFQQAVA 150
Cdd:cd01543 67 LRRLGIPVVNVSG-SRPEPGFPRVTTDNEAIGRMAAEHL----------LERGfrhfafcGFRNAAWSRERGEGFREALR 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1DRK_A 151 AHKFNVLASQPADFDRIKGLNVMQNLLTA------HPdVqAVFAQNDEMALGALRALQTAGKS---DVMVVGFD 215
Cdd:cd01543 136 EAGYECHVYESPPSGSSRSWEEEREELADwlkslpKP-V-GIFACNDDRARQVLEACREAGIRvpeEVAVLGVD 207
|
|
| PBP1_ABC_transporter_LIVBP-like |
cd06268 |
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ... |
3-230 |
3.65e-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: 44.24 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVV--STLNNPFFVSLKDG---AQKEADKLG------YNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAV 71
Cdd:cd06268 1 KIGVVVplTGPYADYGEEILRGvalAVEEINAAGgingrkLELVIADDQGDPETAVAVARKLVDDDKVLAVVGHYSSSVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 72 GNAVKMANQANIPVITL-----DRQATKGEVVSHIASDNVLGGKIAGDYIAKKaGEGAKVIELqgTAATSAARERGEGFQ 146
Cdd:cd06268 81 LAAAPIYQEAGIPLISPgstapELTEGGGPYVFRTVPSDAMQAAALADYLAKK-LKGKKVAIL--YDDYDYGKSLADAFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 147 QAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALgALRALQTAGKsDVMVVGFDGTPDGEKAVND 226
Cdd:cd06268 158 KALKALGGEIVAEEDFPLGTTDFSAQLTKIKAAGPDVLFLAGYGADAAN-ALKQARELGL-KLPILGGDGLYSPELLKLG 235
|
....
1DRK_A 227 GKLA 230
Cdd:cd06268 236 GEAA 239
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
34-205 |
5.53e-05 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 43.80 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 34 LVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVIT---LDRQATKGEVVSHIASDNVLgGK 110
Cdd:pfam13458 45 LVVADDQGDPDVAAAAARRLVDQDGVDAIVGGVSSAVALAVAEVLAKKGVPVIGpaaLTGEKCSPYVFSLGPTYSAQ-AT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 111 IAGDYIAKKAGeGAKVIELqgTAATSAARERGEGFQQAVAAHKFNVLASQPADFDRIKGLNVMQNLLTAHPDVqaVFAQN 190
Cdd:pfam13458 124 ALGRYLAKELG-GKKVALI--GADYAFGRALAAAAKAAAKAAGGEVVGEVRYPLGTTDFSSQVLQIKASGADA--VLLAN 198
|
170
....*....|....*.
1DRK_A 191 D-EMALGALRALQTAG 205
Cdd:pfam13458 199 AgADTVNLLKQAREAG 214
|
|
| PBP1_ABC_sugar_binding-like |
cd06315 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
3-257 |
6.46e-05 |
|
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: 43.49 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQAN 82
Cdd:cd06315 2 TIAYVASDLRNGGVLGVGRGVKEAAAALGWKVDVLDGGGTVTGRLAALNQALALKPDGIILGGDDAVELQEPLKKAVKAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 83 IPVITLDRQATKG-----EVVSHIASDNVLGGKIAGDY-IAKKAGEGAKVIELQGTAATsaARERGEGFQQAV-AAHKFN 155
Cdd:cd06315 82 IPVVGWHAAASPGpipelGLFTNITTDPREVAETAAALvIAQSGGKAGVVIFTDSRYAI--ATAKANAMKKAIeACSGCK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 156 VLASQPADFDRIKGL--NVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAGK--SDVMVVGFDGTPDGEKAVNDGKL- 229
Cdd:cd06315 160 VLEYVDIPIADTAQRmpKLIRSLLQRYGDrWTHTLAINDLYFDFAAPALRAAGVeaDPVNISAGDGSPSAYDRIRAGEYq 239
|
250 260
....*....|....*....|....*...
1DRK_A 230 AATIAQLPDQIGAKGVETADKVLKGEKV 257
Cdd:cd06315 240 VATVAEPLTLQGWQLVDELNRALAGEPP 267
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
3-218 |
2.96e-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: 41.21 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVS-LKDGAQKEADKLGYNLVVLDSQNNP-----AKELANvqDLTVRGtkILLINPTDSDAVGNAVk 76
Cdd:cd06272 1 TIGLYWPSVGERVALTrLLSGINEAISKQGYNINLSICPYKVghlctAKGLFS--ENRFDG--VIVFGISDSDIEYLNK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 77 maNQANIPVITLDRQATKgevVSHIASDNVLGGKIAGDYIAKKageGAKVIELQGTAAT-SAARERGEGFQQAVAAHKFN 155
Cdd:cd06272 76 --NKPKIPIVLYNRESPK---YSTVNVDNEKAGRLAVLLLIQK---GHKSIAYIGNPNSnRNQTLRGKGFIETCEKHGIH 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1DRK_A 156 VLAS--QPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---DVMVVGFDGTP 218
Cdd:cd06272 148 LSDSiiDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISipeDISIVSYDNIP 215
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
3-271 |
4.19e-04 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 41.14 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVqDLTVrgTK----ILLIN---PTDsdavgnaV 75
Cdd:PRK11041 37 TILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFV-NLII--TKqidgMLLLGsrlPFD-------A 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 76 KMANQANIPVITLDRQ-ATKGEVVS-HIasDNVLGGKIAGDYIAKKageGAKVI-ELQGTAATSAARERGEGFQQAVAAH 152
Cdd:PRK11041 107 SKEEQRNLPPMVMANEfAPELELPTvHI--DNLTAAFEAVNYLHEL---GHKRIaCIAGPEEMPLCHYRLQGYVQALRRC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 153 KFNVLASQPA--DFDRIKGLNVMQNLLtAHPDV-QAVFAQNDEMALGALRALQTAG---KSDVMVVGFDgtpdgekavnD 226
Cdd:PRK11041 182 GITVDPQYIArgDFTFEAGAKALKQLL-DLPQPpTAVFCHSDVMALGALSQAKRMGlrvPQDLSIIGFD----------D 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
1DRK_A 227 GKLA-------ATIAQLPDQIGAKGVETADKVLKGEKVQA-KYPVDLKLVVKQ 271
Cdd:PRK11041 251 IDLAqycdpplTTVAQPRYEIGREAMLLLLEQLQGHHVSSgSRLLDCELIIRG 303
|
|
| PBP1_ABC_ligand_binding-like |
cd06343 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
33-230 |
6.02e-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: 40.63 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 33 NLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKGEVVSH-----IASDNVL 107
Cdd:cd06343 49 ELIVEDDGYDPARAVAAVRKLVEQDKVFAIVGGLGTPTNLAVRPYLNEAGVPQLFPATGASALSPPPKpytfgVQPSYED 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 108 GGKIAGDYIAKKAGeGAKVIEL-QGTAatsAARERGEGFQQAVAAHKFNVLASQP-----ADFDrikglNVMQNLLTAHP 181
Cdd:cd06343 129 EGRILADYIVETLP-AAKVAVLyQNDD---FGKDGLEGLKEALKAYGLEVVAEETyepgdTDFS-----SQVLKLKAAGA 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
1DRK_A 182 DVQAVFAQNDEmALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLA 230
Cdd:cd06343 200 DVVVLGTLPKE-AAAALKEAAKLGWKPTFLGSSVSADPTTLAKAGGDAA 247
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
3-118 |
2.44e-03 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 38.74 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DRK_A 3 TIALVVSTlNNPFFVSLKDGAQKEADKLGYNLVVLDSQNnpAKELANVQDLTVRGTKILLInPTDSDAVGNA---VKMAN 79
Cdd:COG2984 134 RIGVLYNP-SEANSVAQVEELKKAAKKLGLELVEATVTS--SNEIQQALQSLAGKVDAIYV-PTDNTVVSALeaiAKVAA 209
|
90 100 110
....*....|....*....|....*....|....*....
1DRK_A 80 QANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAK 118
Cdd:COG2984 210 RAKIPVFGGDDSSVKAGALAGYGIDYYELGRQAAEMALR 248
|
|
| |
