|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-295 |
0e+00 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 575.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 1 MKMKKLATLASAIALSATLSANAMAKDTIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMV 80
Cdd:PRK10653 1 MNMKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 81 RAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGT 160
Cdd:PRK10653 81 RGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIAKKLGEGAKVIQLEGIAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 161 SAARERGEGFKQSLDQNKFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDVIVVGFD 240
Cdd:PRK10653 161 SAARERGEGFKQAVAAHKFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 727170941 241 GTADGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:PRK10653 241 GTPDGIKAVNRGKLAATIAQQPDQIGAIGVETADKVLKGEKVEAKIPVDLKLVTK 295
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
28-294 |
1.43e-141 |
|
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: 399.36 E-value: 1.43e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLASQP 186
Cdd:cd06323 81 IPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAKYpKINVVASQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 187 ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDVIVVGFDGTADGVKAVEGGKLAATVAQRPDQIG 266
Cdd:cd06323 161 ADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQPEEMG 240
|
250 260
....*....|....*....|....*...
gi 727170941 267 VIGVETADKVLKGEKVPATIPVDLKLVT 294
Cdd:cd06323 241 AKAVETADKYLKGEKVPKKIPVPLKLVT 268
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
4-295 |
9.02e-97 |
|
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: 287.21 E-value: 9.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 4 KKLATLASAIALSATLSANAM----------AKDTIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELA 73
Cdd:COG1879 1 KRLALLAAVLALALALAACGSaaaeaaaaaaKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 74 NVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQ 153
Cdd:COG1879 81 QIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 154 LEGIAGTSAARERGEGFKQSLDQN-KFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT 232
Cdd:COG1879 161 LTGSPGAPAANERTDGFKEALKEYpGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727170941 233 -DVIVVGFDGTADGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:COG1879 241 gDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTK 304
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
28-292 |
3.27e-96 |
|
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: 284.46 E-value: 3.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDR-VASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLASQ 185
Cdd:cd01536 81 IPVVAVDTdIDGGGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYpDIEIVAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 186 PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLAATVAQRPDQ 264
Cdd:cd01536 161 PANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTgDIKIVGVDGTPEALKAIKDGELDATVAQDPYL 240
|
250 260
....*....|....*....|....*...
gi 727170941 265 IGVIGVETADKVLKGEKVPATIPVDLKL 292
Cdd:cd01536 241 QGYLAVEAAVKLLNGEKVPKEILTPVTL 268
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
28-293 |
1.11e-77 |
|
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: 237.06 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANK-LGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKyPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLASQ 185
Cdd:cd06308 81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYpGIKIVASQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 186 PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-TDVIVVGFDG-TADGVKAVEGGKLAATVaqRPD 263
Cdd:cd06308 161 DGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGlPEAGEKAVKDGILAATF--LYP 238
|
250 260 270
....*....|....*....|....*....|
gi 727170941 264 QIGVIGVETADKVLKGEKVPATIPVDLKLV 293
Cdd:cd06308 239 TGGKEAIEAALKILNGEKVPKEIVLPTPLI 268
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
28-294 |
1.12e-77 |
|
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: 237.22 E-value: 1.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDR-VASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLASQ 185
Cdd:cd19967 81 IPVFLIDReINAEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQYpELKMVAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 186 PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-TDVIVVGFDGTADGVKAVEGGKLAATVAQRPDQ 264
Cdd:cd19967 161 SADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRaGDVIIVGFDGSNDVRDAIKEGKISATVLQPAKL 240
|
250 260 270
....*....|....*....|....*....|..
gi 727170941 265 IGVIGVETADKVLKGEK--VPATIPVDLKLVT 294
Cdd:cd19967 241 IARLAVEQADQYLKGGStgKEEKQLFDCVLIT 272
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
28-295 |
3.04e-76 |
|
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: 234.04 E-value: 3.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDR---VASKGEVVSHIASDNRVGGKMAGDFIAKKVGAD-AKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLL 182
Cdd:cd06309 81 IPVILVDRtidGEDGSLYVTFIGSDFVEEGRRAAEWLVKNYKGGkGNVVELQGTAGSSVAIDRSKGFREVIKKHpNIKIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 183 ASQPADFDRTKGLNVMQNLLTAHP-DVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTADGVKAVEGGKLAATV 258
Cdd:cd06309 161 ASQSGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLKpgkDVLVVGIDGQKDALEAIKAGELNATV 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 727170941 259 AQRPDQiGVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd06309 241 ECNPLF-GPTAFDTIAKLLAGEKVPKLIIVEERLFDK 276
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
29-295 |
8.02e-76 |
|
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: 232.92 E-value: 8.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 29 IALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVL--DSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQaaPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDRV-------ASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-K 178
Cdd:cd06320 82 GIPVINLDDAvdadalkKAGGKVTSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKKApG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 179 FKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLAAT 257
Cdd:cd06320 162 LKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTgKVLVVGTDGIPEAKKSIKAGELTAT 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 727170941 258 VAQRPDQIGVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd06320 242 VAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITK 279
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-294 |
1.52e-71 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380545 [Multi-domain] Cd Length: 270 Bit Score: 221.77 E-value: 1.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLASQP 186
Cdd:cd06322 81 IPVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKALLGGGGKIAIIDYPEVESVVLRVNGFKEAIKKYpNIEIVAEQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 187 ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTD-VIVVGFDGTADGVKAV-EGGKLAATVAQRPDQ 264
Cdd:cd06322 161 GDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDkIKVIGFDGNPEAIKAIaKGGKIKADIAQQPDK 240
|
250 260 270
....*....|....*....|....*....|
gi 727170941 265 IGVIGVETADKVLKGEKVPATIPVDLKLVT 294
Cdd:cd06322 241 IGQETVEAIVKYLAGETVEKEILIPPKLYT 270
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
28-294 |
1.43e-69 |
|
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: 216.48 E-value: 1.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLASQP 186
Cdd:cd19968 81 IPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAAGpKIKVVFEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 187 ADFDRTKGLNVMQNLLTAHP-DVQAVFAQNDEMALGALRALQTAG--KTDVIVVGFDGTADGVKAVEGGKLAATVAQRPD 263
Cdd:cd19968 161 GNFERDEGLTVMENILTSLPgPPDAIICANDDMALGAIEAMRAAGldLKKVKVIGFDAVPDALQAIKDGELYATVEQPPG 240
|
250 260 270
....*....|....*....|....*....|.
gi 727170941 264 QIGVIGVETADKVLKGEKVPATIPVDLKLVT 294
Cdd:cd19968 241 GQARTALRILVDYLKDKKAPKKVNLKPKLIT 271
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-292 |
7.90e-68 |
|
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: 212.11 E-value: 7.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQ-EANKLGYNLVV--LDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMAN 104
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKhAKEANGYELLVkgIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLD------RVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQNK 178
Cdd:cd19970 81 DAGIAVINIDnrldadALKEGGINVPFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 179 FKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTD-VIVVGFDGTADGVKAVEGGKLAAT 257
Cdd:cd19970 161 MKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKMLAT 240
|
250 260 270
....*....|....*....|....*....|....*
gi 727170941 258 VAQRPDQIGVIGVETADKVLKGEKVPATIPVDLKL 292
Cdd:cd19970 241 IDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPVEL 275
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
28-295 |
7.70e-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: 209.82 E-value: 7.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLASQP 186
Cdd:cd06313 81 IPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYpDIKVLAEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 187 ADFDRTKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAGKTDVIVVGFDGTADGVKAVEGGKLAATVAQRPDQI 265
Cdd:cd06313 161 ANWSRDEAMSLMENWLQAYGDeIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDALQAVKSGELIATVLQDAEAQ 240
|
250 260 270
....*....|....*....|....*....|
gi 727170941 266 GVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd06313 241 GKGAVEVAVDAVKGEGVEKKYYIPFVLVTK 270
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-295 |
1.08e-66 |
|
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: 209.52 E-value: 1.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGA----DAKVIQLEGIAGTSAARERGEGFKQSLDQNKFKLLA 183
Cdd:cd06319 81 IPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKEngwgGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 184 -SQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLAATVAQR 261
Cdd:cd06319 161 lRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTgDILVVGFDGDPEALDLIKDGKLDGTVAQQ 240
|
250 260 270
....*....|....*....|....*....|....*
gi 727170941 262 PDQIGVIGVETADKVLKGEKVPA-TIPVDLKLVTK 295
Cdd:cd06319 241 PFGMGARAVELAIQALNGDNTVEkEIYLPVLLVTS 275
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
28-294 |
9.35e-66 |
|
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: 206.70 E-value: 9.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEA-NKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAkEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDR-VASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLAS 184
Cdd:cd06301 82 GIPLVYVNRePDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYpGMKIVAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 185 QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTD-VIVVGFDGTADGVKAVEGGKLAATVAQRPD 263
Cdd:cd06301 162 QTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDdILVAGIDATPDALKAMKAGRLDATVFQDAA 241
|
250 260 270
....*....|....*....|....*....|.
gi 727170941 264 QIGVIGVETADKVLKGEKVPATIPVDLKLVT 294
Cdd:cd06301 242 GQGETAVDVAVKAAKGEEVESDIWIPFELVT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-292 |
3.14e-65 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380626 [Multi-domain] Cd Length: 267 Bit Score: 205.51 E-value: 3.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLD-RVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSaARERGEGFKQSL-DQNKFKLLASQ 185
Cdd:cd19971 81 IPVINVDtPVKDTDLVDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLDHPTAES-CVDRIDGFLDAIkKNPKFEVVAQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 186 PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLAATVAQRPDQ 264
Cdd:cd19971 160 DGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKLgDILVYGVDGSPDAKAAIKDGKMTATAAQSPIE 239
|
250 260
....*....|....*....|....*...
gi 727170941 265 IGVIGVETADKVLKGEKVPATIPVDLKL 292
Cdd:cd19971 240 IGKKAVETAYKILNGEKVEKEIVVPTFL 267
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
28-295 |
9.41e-64 |
|
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: 202.26 E-value: 9.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDR-VASKGEVVSHIASDNRVGGKMAGDFIAKKVG-ADAKVIQLEGIAGTSAARERGEGFKQSLDQ--------N 177
Cdd:cd06318 81 IPVITVDSaLDPSANVATQVGRDNKQNGVLVGKEAAKALGgDPGKIIELSGDKGNEVSRDRRDGFLAGVNEyqlrkygkS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 178 KFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTD-VIVVGFDGTADGVKAVEGGKLAA 256
Cdd:cd06318 161 NIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDkVKVAGADGQKEALKLIKDGKYVA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 727170941 257 TVAQRPDQIGVIGVETADKVLKGE-KVPATIPVDLKLVTK 295
Cdd:cd06318 241 TGLNDPDLLGKTAVDTAAKVVKGEeSFPEFTYTPTALITK 280
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-294 |
5.80e-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: 5.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLASQP 186
Cdd:cd19972 81 IPVIAVDRNPEDAPGDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAEApGIKVVAEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 187 ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-TDVIVVGFDGTADGVKAVEGGKLAATVAQRPDQI 265
Cdd:cd19972 161 ADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLdHKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKM 240
|
250 260
....*....|....*....|....*....
gi 727170941 266 GVIGVETADKVLKGEKVPATIPVDLKLVT 294
Cdd:cd19972 241 GRLAVDSAIDLLNGKAVPKEQLQDAVLTT 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-294 |
1.04e-60 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380544 [Multi-domain] Cd Length: 270 Bit Score: 194.04 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYN--LVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQ 105
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGakVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDrVASKGeVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAgTSAARERGEGFKQSLDQNK-FKLLAS 184
Cdd:cd06321 81 AGIIVVAVD-VAAEG-ADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPP-VSAVIDRVNGCKEALAEYPgIKLVDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 185 QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDVIVVGFDGTADGVKAV--EGGKLAATVAQRP 262
Cdd:cd06321 158 QNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSVDGSPEAVAALkrEGSPFIATAAQDP 237
|
250 260 270
....*....|....*....|....*....|...
gi 727170941 263 DQIGVIGVETADKVLKGEKV-PATIPVDLKLVT 294
Cdd:cd06321 238 YDMARKAVELALKILNGQEPaPELVLIPSTLVT 270
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-294 |
6.20e-57 |
|
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: 184.47 E-value: 6.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVL--DSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQ 105
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVgpESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN--KFKLLA 183
Cdd:cd06310 81 KGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHpgGIKVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 184 SQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDVI-VVGFDGTADGVKAVEGGKLAATVAQRP 262
Cdd:cd06310 161 SQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIkIVGFDSQEELLDALKNGKIDALVVQNP 240
|
250 260 270
....*....|....*....|....*....|..
gi 727170941 263 DQIGVIGVETADKVLKGEKVPATIPVDLKLVT 294
Cdd:cd06310 241 YEIGYEGIKLALKLLKGEEVPKNIDTGAELIT 272
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
29-281 |
3.88e-56 |
|
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: 181.74 E-value: 3.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 29 IALVVSTLNNPFFVSMKDGAQQEANKLGYN-LVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEvIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN--KFKLLAS- 184
Cdd:pfam13407 81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKypGIKVVAEv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 185 QPADFDRTKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAGKTD-VIVVGFDGTADGVKAVEGGKLAATVAQRP 262
Cdd:pfam13407 161 EGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGkVVVTGFDATPEALEAIKDGTIDATVLQDP 240
|
250
....*....|....*....
gi 727170941 263 DQIGVIGVETADKVLKGEK 281
Cdd:pfam13407 241 YGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-294 |
4.93e-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: 380662 [Multi-domain] Cd Length: 271 Bit Score: 179.36 E-value: 4.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVL-DSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQgPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLD-RVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLAS 184
Cdd:cd20007 81 GIKVVTVDtTLGDPSFVLSQIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMKKYpGIKVLGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 185 QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDVI-VVGFDGTADGVKAVEGGKLAATVAQRPD 263
Cdd:cd20007 161 QYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGKVkVVGFDASPAQVEQLKAGTIDALIAQKPA 240
|
250 260 270
....*....|....*....|....*....|.
gi 727170941 264 QIGVIGVETADKVLKGEKVPATIPVDLKLVT 294
Cdd:cd20007 241 EIGYLAVEQAVAALTGKPVPKDILTPFVVIT 271
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
3-295 |
1.88e-52 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 173.91 E-value: 1.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 3 MKKLATLASAIALSATLSANAMAKDTIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVL--DSQNNPAKELANVQDLMV 80
Cdd:PRK09701 1 MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFasPSEGDFQSQLQLFEDLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 81 RAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDR-------VASKGEVVSHIASDNRVGGKMAGDFIAKKVGADA-KVI 152
Cdd:PRK09701 81 KNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEkidmdnlKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGgEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 153 QLEGIAGTSAARERGEGFKQS-LDQNKFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK 231
Cdd:PRK09701 161 IIEGKAGNASGEARRNGATEAfKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727170941 232 T-DVIVVGFDGTADGVKAVEGGKLAATVAQRPDQIGVIGV------ETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:PRK09701 241 TgKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLklmvdaEKSGKVIPLDKAPEFKLVDSILVTQ 311
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-283 |
9.23e-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: 9.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVL--DSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANq 105
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLgpATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGA----DAKVIQLEGIAGTSAARERGEGFKQSLDQN--KF 179
Cdd:cd20008 80 AGIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAELLKAsgggKGKVAIISFQAGSQTLVDREEGFRDYIKEKypDI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 180 KLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLAATV 258
Cdd:cd20008 160 EIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAgKIVLVGFDSSPDEVALLKSGVIKALV 239
|
250 260
....*....|....*....|....*
gi 727170941 259 AQRPDQIGVIGVETADKVLKGEKVP 283
Cdd:cd20008 240 VQDPYQMGYEGVKTAVKALKGEEIV 264
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-295 |
2.04e-46 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 157.01 E-value: 2.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVL--DSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQ 105
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRgpSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSL--DQNKFKLLA 183
Cdd:cd20004 81 QGIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAKGSASTTDRERGFLEALkkLAPGLKVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 184 SQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-TDVIVVGFDGTADGVKAVEGGKLAATVAQRP 262
Cdd:cd20004 161 DQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLaGKVKFIGFDASDLLLDALRAGEISALVVQDP 240
|
250 260 270
....*....|....*....|....*....|...
gi 727170941 263 DQIGVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd20004 241 YRMGYLGVKTAVAALRGKPVPKRIDTGVVLVTK 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
28-294 |
5.77e-46 |
|
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: 157.02 E-value: 5.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYN---LVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMAN 104
Cdd:cd19996 1 TIGFSNAGLGNSWRVQMIAEFEAEAAKLKKLikeLIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQNK-FKLLA 183
Cdd:cd19996 81 AAGIPVVLFDSGVGSDKYTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYPgIKIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 184 SQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDVIVVGFD--GTADGVKAVEGGKLAATVAqr 261
Cdd:cd19996 161 EVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTGEDnnGFLKAWKELPGFKSIAPSY-- 238
|
250 260 270
....*....|....*....|....*....|...
gi 727170941 262 PDQIGVIGVETADKVLKGEKVPATIPVDLKLVT 294
Cdd:cd19996 239 PPWLGATALDAALAALEGEPVPKYVYIPLPVIT 271
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
28-294 |
1.34e-43 |
|
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: 149.65 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQN-NPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSL-DQNKFKLLASQ 185
Cdd:cd06314 81 GIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALkGSPGIEIVDPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 186 PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLAATVAQRPDQ 264
Cdd:cd06314 161 SDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVgKVKIVGFDTLPETLQGIKDGVIAATVGQRPYE 240
|
250 260 270
....*....|....*....|....*....|.
gi 727170941 265 IGVIGVETADKVLKGEK-VPATIPVDLKLVT 294
Cdd:cd06314 241 MGYLSVKLLYKLLKGGKpVPDVIDTGVDVVT 271
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
22-290 |
8.04e-43 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 149.58 E-value: 8.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 22 NAMAK-------DTIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPK-LLLINPTDS 93
Cdd:COG1609 50 NAAARslrtgrtRTIGVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDgLILAGSRLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 94 DAvgnAIKMANQAKIPVITLDRVASkGEVVSHIASDNRVGGKMAGDFIAKKvGADaKVIQLEGIAGTSAARERGEGFKQS 173
Cdd:COG1609 130 DA---RLERLAEAGIPVVLIDRPLP-DPGVPSVGVDNRAGARLATEHLIEL-GHR-RIAFIGGPADSSSARERLAGYREA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 174 LDQNKFKLLASQ--PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTAdgvka 248
Cdd:COG1609 204 LAEAGLPPDPELvvEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRvpeDVSVVGFDDIP----- 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 727170941 249 veggkLAA-------TVAQRPDQIGVIGVETADKVLKGEKVPAT---IPVDL 290
Cdd:COG1609 279 -----LARyltppltTVRQPIEEMGRRAAELLLDRIEGPDAPPErvlLPPEL 325
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
28-290 |
1.41e-42 |
|
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: 146.89 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAvgNAIKMANQAK 107
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDD--ELLEELLAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVaSKGEVVSHIASDNRVGGKMAGDFIA----KKVGAdakviqLEGIAGTSAARERGEGFKQSLDQNKFKLLA 183
Cdd:cd06267 79 IPVVLIDRR-LDGLGVDSVVVDNYAGAYLATEHLIelghRRIAF------IGGPLDLSTSRERLEGYRDALAEAGLPVDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 184 S--QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTAdgvkaveggkLAA-- 256
Cdd:cd06267 152 ElvVEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRvpeDISVVGFDDIP----------LAAll 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 727170941 257 -----TVAQRPDQIGVIGVETADKVLKGEKVPA---TIPVDL 290
Cdd:cd06267 222 tppltTVRQPAYEMGRAAAELLLERIEGEEEPPrriVLPTEL 263
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-295 |
2.21e-42 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 146.62 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVL--DSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQ 105
Cdd:cd20005 1 YIAVISKGFQHQFWKAVKKGAEQAAKELGVKITFEgpDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN--KFKLLA 183
Cdd:cd20005 81 KGIPVVTFDSGVPSDLPLATVATDNYAAGALAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKypDIKVVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 184 SQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLAATVAQRP 262
Cdd:cd20005 161 VQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLgKIKVVGFDSGEAQIDAIKNGVIAGSVTQNP 240
|
250 260 270
....*....|....*....|....*....|...
gi 727170941 263 DQIGVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd20005 241 YGMGYKTVKAAVKALKGEEVEKLIDTGAKWYDK 273
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-295 |
6.76e-42 |
|
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: 145.60 E-value: 6.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAG----DFIAKKVGADAKViqleGIAGTSAA---RERGEGFKQSLDQN-KF 179
Cdd:cd06317 81 IPVIAYDAVIPSDFQAAQVGVDNLEGGKEIGkyaaDYIKAELGGQAKI----GVVGALSSliqNQRQKGFEEALKANpGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 180 KLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKA-VEGGKLAAT 257
Cdd:cd06317 157 EIVATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQgKIKVFGWDLTKQAIFLgIDEGVLQAV 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 727170941 258 VAQRPDQIGVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd06317 237 VQQDPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-295 |
2.54e-41 |
|
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: 144.04 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLLASQP 186
Cdd:cd06311 81 IPVVNFDRGLNVLIYDLYVAGDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNpGIKILAMQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 187 ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDV-IVVGFDGTADGVKAVEGGK--LAATVAQRPD 263
Cdd:cd06311 161 GDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIkVMTGGGGSQEYFKRIMDGDpiWPASATYSPA 240
|
250 260 270
....*....|....*....|....*....|..
gi 727170941 264 QIGViGVETADKVLKGEKvpaTIPVDLKLVTK 295
Cdd:cd06311 241 MIAD-AIKLAVLILKGGK---TVEKEVIIPST 268
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
28-290 |
1.40e-40 |
|
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380514 [Multi-domain] Cd Length: 264 Bit Score: 141.89 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQdlMVRAPK---LLLInpTDSDAVGNAIKman 104
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLE--MLKRNKvdgIILG--SHSLDIEEYKK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 qAKIPVITLDRVASKGevVSHIASDNRVGGKMAGDFIAKKvGADaKVIQLEGIAGTSAARERGEGFKQSLDQNKFK---L 181
Cdd:cd06291 74 -LNIPIVSIDRYLSEG--IPSVSSDNYQGGRLAAEHLIEK-GCK-KILHIGGPSNNSPANERYRGFEDALKEAGIEyeiI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 182 LASQPaDFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTadgvkaveggKLA--- 255
Cdd:cd06291 149 EIDEN-DFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRvpeDVQIIGFDGI----------EISell 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 727170941 256 ----ATVAQRPDQIGVIGVETADKVLKGEKVPA---TIPVDL 290
Cdd:cd06291 218 ypelTTIRQPIEEMAKEAVELLLKLIEGEEIEEsriVLPVEL 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-259 |
1.18e-39 |
|
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: 140.82 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVV-STLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPK--LLLINPTDSDAVGnAIKMAN 104
Cdd:cd06324 1 RVVFINpGKEDEPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARPPKpdYLILVNEKGVAPE-LLELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLDRVASKGEV-------------VSHIASDN-RVGGKMAGDFI--AKKVGADAK--VIQLEGIAGTSAARER 166
Cdd:cd06324 80 QAKIPVFLINNDLTDEERallgkprekfkywLGSIVPDNeQAGYLLAKALIkaARKKSDDGKirVLAISGDKSTPASILR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 167 GEGFKQSL-DQNKFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGT 242
Cdd:cd06324 160 EQGLRDALaEHPDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKpgkDVLVGGIDWS 239
|
250
....*....|....*..
gi 727170941 243 ADGVKAVEGGKLAATVA 259
Cdd:cd06324 240 PEALQAVKDGELTASVG 256
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
29-285 |
2.41e-38 |
|
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: 136.56 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 29 IALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAKI 108
Cdd:cd19992 2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 109 PVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGaDAKVIQLEGIAGTSAARERGEGFKQSL----DQNKFKLLAS 184
Cdd:cd19992 82 PVISYDRLILNADVDLYVGRDNYKVGQLQAEYALEAVP-KGNYVILSGDPGDNNAQLITAGAMDVLqpaiDSGDIKIVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 185 QPAD-FDRTKGLNVMQNLLTA-HPDVQAVFAQNDEMALGALRALQTAG-KTDVIVVGFDGTADGVKAVEGGKLAATVAQR 261
Cdd:cd19992 161 QYVKgWSPDEAMKLVENALTAnNNNIDAVLAPNDGMAGGAIQALKAQGlAGKVFVTGQDAELAALKRIVEGTQTMTVWKD 240
|
250 260
....*....|....*....|....
gi 727170941 262 PDQIGVIGVETADKVLKGEKVPAT 285
Cdd:cd19992 241 LKELARAAADAAVKLAKGEKPQTT 264
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
28-295 |
2.21e-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: 380661 [Multi-domain] Cd Length: 274 Bit Score: 133.49 E-value: 2.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVV--STLNNPFFVSMKDGAQQEANKLGYNLVVL--DSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMA 103
Cdd:cd20006 1 KIALILksSDPNSDFWQTVKSGAEAAAKEYGVDLEFLgpESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 104 NQAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQNKF-KLL 182
Cdd:cd20006 81 KKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQALAEYPNiKIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 183 ASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG-KTDVIVVGFDGTADGVKAVEGGKLAATVAQR 261
Cdd:cd20006 161 ETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGlGGKVKVVGFDSSVEEIQLLEEGIIDALVVQN 240
|
250 260 270
....*....|....*....|....*....|....
gi 727170941 262 PDQIGVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd20006 241 PFNMGYLSVQAAVDLLNGKKIPKRIDTGSVVITK 274
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
28-285 |
2.83e-37 |
|
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: 134.25 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLG-YNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGkIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDR-----VASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAK-------VIQ---LEGIAGTSAARERGEGFK 171
Cdd:cd01539 82 NIPVIFFNRepsreDLKSYDKAYYVGTDAEESGIMQGEIIADYWKANPEidkngdgKIQyvmLKGEPGHQDAIARTKYSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 172 QSLDQNKFKL--LASQPADFDRTKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAGKTD------VIVVGFDGT 242
Cdd:cd01539 162 KTLNDAGIKTeqLAEDTANWDRAQAKDKMDAWLSKYGDkIELVIANNDDMALGAIEALKAAGYNTgdgdkyIPVFGVDAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 727170941 243 ADGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEKVPAT 285
Cdd:cd01539 242 PEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLET 284
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-289 |
4.85e-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: 132.98 E-value: 4.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVL--DSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQ 105
Cdd:cd19973 1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAagKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDRVASKGEVV-SHIASDNRVGGKMAGDFIAKKVGA-DAKVIQLEGIAGTSAARERGEGF-----------KQ 172
Cdd:cd19973 81 AGVLVIALDTPTDPIDAAdATFATDNFKAGVLIGEWAKAALGAkDAKIATLDLTPGHTVGVLRHQGFlkgfgidekdpES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 173 SLDQNKFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK-TDVIVVGFDGTADGVKAVEG 251
Cdd:cd19973 161 NEDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKeKGVLIVSVDGGCPGVKDVKD 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 727170941 252 GKLAATVAQRPDQIGVIGVETADKVLKGEKVPATIPVD 289
Cdd:cd19973 241 GIIGATSQQYPLRMAALGVEAIAAFAKTGGTKGSGFTD 278
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-295 |
1.90e-35 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380539 [Multi-domain] Cd Length: 294 Bit Score: 129.28 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLV-VLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd06316 1 KVAIAMHTTGSDWSRLQVAGIKDTFEELGIEVVaVTDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDRVAS----KGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN--KFK 180
Cdd:cd06316 81 GIKLVFMDNVPDgleaGKDYVSVVSSDNRGNGQIAAELLAEAIGGKGKVGIIYHDADFYATNQRDKAFKDTLKEKypDIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 181 LLASQPADfDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDVIVVGFD-GTADGVKAVEGGKLAATVA 259
Cdd:cd06316 161 IVAEQGFA-DPNDAEEVASAMLTANPDIDGIYVSWDTPALGVISALRAAGRSDIKITTVDlGTEIALDMAKGGNVKGIGA 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 727170941 260 QRPDQIGVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd06316 240 QRPYDQGVAEALAAALALLGKEVPPFIGVPPLAVTK 275
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
28-286 |
1.04e-34 |
|
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380528 [Multi-domain] Cd Length: 273 Bit Score: 126.64 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDrVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGiAGTSAARERGEGFKQSLDQNK--FKLLASQ 185
Cdd:cd06305 81 IPVVTFD-TDSQVPGVNNITQDDYALGTLSLGQLVKDLNGEGNIAVFNV-FGVPPLDKRYDIYKAVLKANPgiKKIVAEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 186 PADFDRTKG--LNVMQNLLTAHPD--VQAVFAQNDEMALGALRALQTAGKTDVIVVGFDGTADGVKAV--EGGKLAATVA 259
Cdd:cd06305 159 GDVTPNTAAdaQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISNQDLELMadEGSPWVATAA 238
|
250 260
....*....|....*....|....*..
gi 727170941 260 QRPDQIGVIGVETADKVLKGEKVPATI 286
Cdd:cd06305 239 QDPALIGTVAVRNVARKLAGEDLPDKY 265
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
28-286 |
2.34e-32 |
|
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.
Pssm-ID: 380529 [Multi-domain] Cd Length: 269 Bit Score: 120.38 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQ--NNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQ 105
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGgyTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITL-DRVASKGeVVSHIASDNRVGGKMAGDFIAKKV-GADAKVIQLEGIAGTSAARERGEGFKQSLDQNKFKLLA 183
Cdd:cd06306 81 AGIPVIDLvNGIDSPK-VAARVLVDFYDMGYLAGEYLVEHHpGKPVKVAWFPGPAGAGWAEDREKGFKEALAGSNVEIVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 184 SQPADFDRTKGLNVMQNLLTAHPDVQAVFAqNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLAATVAQRP 262
Cdd:cd06306 160 TKYGDTGKAVQLNLVEDALQAHPDIDYIVG-NAVAAEAAVGALREAGLTgKVKVVSTYLTPGVYRGIKRGKILAAPSDQP 238
|
250 260
....*....|....*....|....
gi 727170941 263 DQIGVIGVETADKVLKGEKVPATI 286
Cdd:cd06306 239 VLQGRIAVDQAVRALEGKPVPKHV 262
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
28-294 |
2.60e-32 |
|
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380523 [Multi-domain] Cd Length: 302 Bit Score: 120.89 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGY-----NLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKM 102
Cdd:cd06300 1 TIGLSNTYAGNSWREQMIASLKADAAQSGQkglvkELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 103 ANQAKIPVITLD-RVASKGEVvsHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFK 180
Cdd:cd06300 81 AADAGIPVVAFDgAVTSPDAY--NVSNDQVEWGRLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEALAEYpGIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 181 LLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEmALGALRALQTAGKTDVIVVGFDGTADGVKAVEGGK--LAATV 258
Cdd:cd06300 159 VVGEVFGGWDEATAQTAMLDFLATHPQVDGVWTQGGE-DTGVLQAFQQAGRPPVPIVGGDENGFAKQWWKHPKkgLTGAA 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 727170941 259 AQRPDQIGVIGVETADKVLKGEK-VPATIPVDLKLVT 294
Cdd:cd06300 238 VWPPPAIGAAGLEVALRLLEGQGpKPQSVLLPPPLIT 274
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
25-285 |
7.66e-32 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 119.85 E-value: 7.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 25 AKDTIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMAN 104
Cdd:COG4213 1 GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAK--VIQLEGIAGTSAARERGEGFKQSL----DQNK 178
Cdd:COG4213 81 AAGIPVIAYDRLILNSDVDYYVSFDNVKVGELQGQYLVDGLPLKGKgnIELFGGSPTDNNATLFFEGAMSVLqpyiDSGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 179 FKLLASQPA-DFDRTKGLNVMQNLLTAHP-DVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLA 255
Cdd:COG4213 161 LVVVSGQWTlGWDPETAQKRMENLLTANGnKVDAVLAPNDGLAGGIIQALKAQGLAgKVVVTGQDAELAAVQRILAGTQY 240
|
250 260 270
....*....|....*....|....*....|
gi 727170941 256 ATVAQRPDQIGVIGVETADKVLKGEKVPAT 285
Cdd:COG4213 241 MTVYKDTRELAEAAAELAVALAKGEKPEVN 270
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-293 |
2.15e-31 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380513 [Multi-domain] Cd Length: 267 Bit Score: 117.72 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRapK---LLLINPTDSDAVGNAIKMan 104
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLAR--KvdgIIVVGGFGDEELLKLLAE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 qaKIPVITLDRvASKGEVVSHIASDNRVGGKMAGDFIAKKvGAdAKVIQLEGIAGTSAARERGEGFKQSLDQN--KFKLL 182
Cdd:cd06290 77 --GIPVVLVDR-ELEGLNLPVVNVDNEQGGYNATNHLIDL-GH-RRIVHISGPEDHPDAQERYAGYRRALEDAglEVDPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 183 ASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KTDVIVVGFDGTADGVKAVEggKLaATVA 259
Cdd:cd06290 152 LIVEGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGirvPDDVSVIGFDDLPFSKYTTP--PL-TTVR 228
|
250 260 270
....*....|....*....|....*....|....*
gi 727170941 260 QRPDQIGVIGVET-ADKVLKGEKVPATIPVDLKLV 293
Cdd:cd06290 229 QPLYEMGKTAAEIlLELIEGKGRPPRRIILPTELV 263
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
28-293 |
2.94e-31 |
|
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: 117.36 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVgNAIKMANQAK 107
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDD-DAELLAALRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVShIASDNRVGGKMAGDFIA----KKVGAdakviqLEGIAGTSAARERGEGFKQSLDQNKFKLLA 183
Cdd:cd06275 80 IPVVVLDREIAGDNADA-VLDDSFQGGYLATRHLIelghRRIGC------ITGPLEHSVSRERLAGFRRALAEAGIEVPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 184 S--QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KTDVIVVGFDGTAdgvkaveggkLAA-- 256
Cdd:cd06275 153 SwiVEGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGlrvPQDISIIGYDDIE----------LARyf 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 727170941 257 -----TVAQRPDQIGVIGVET-ADKVLKGEKVPATIPVDLKLV 293
Cdd:cd06275 223 spaltTIHQPKDELGELAVELlLDRIENKREEPQSIVLEPELI 265
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
28-293 |
1.45e-30 |
|
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380503 [Multi-domain] Cd Length: 266 Bit Score: 115.43 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDavGNAIKMANQAK 107
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGP--SRELKRLLKHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRvASKGEVVSHIASDNRVGGKMAGDFIA----KKVGAdakviqLEGIAGTSAARERGEGFKQSLDQNKFKLLA 183
Cdd:cd06280 79 IPIVLIDR-EVEGLELDLVAGDNREGAYKAVKHLIelghRRIGL------ITGPLEISTTRERLAGYREALAEAGIPVDE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 184 S--QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDgtaDGVKAVEGGKLAATV 258
Cdd:cd06280 152 SliFEGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEipqDISVVGFD---DSDWFEIVDPPLTVV 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 727170941 259 AQRPDQIGVIGVETADKVLKGE-KVPATIPVDLKLV 293
Cdd:cd06280 229 AQPAYEIGRIAAQLLLERIEGQgEEPRRIVLPTELI 264
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
58-289 |
9.50e-30 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380654 [Multi-domain] Cd Length: 313 Bit Score: 114.33 E-value: 9.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 58 NLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRVASKGEVVShIASDNRVGGKMA 137
Cdd:cd19999 36 DLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPVSSPDAIN-VVIDQYKWAAIQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 138 GDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQNK-FKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQnD 216
Cdd:cd19999 115 AQWLAEQLGGKGNIVAINGVAGNPANEARVKAADDVFAKYPgIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLTQ-D 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727170941 217 EMALGALRALQTAGKTDVIVVGfDGTADGV---KAVEGGKLAATVAQRPDQIGVIGVETADKVLKGE--KVPATIPVD 289
Cdd:cd19999 194 GMAEGVLRAFQAAGKDPPVMTG-DYRKGFLrkwKELDLPDFESIGVVNPPGIGATALRIAVRLLQGKelKEDALNPLD 270
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-243 |
1.75e-27 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 107.23 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYN--LVVLDSQNNPAKELANVQDLMVRApkLLLINPTDSDAVgnaIKMANQ 105
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRplLFNVDDEDDVDDALRQLLQYRVDG--VIVTSATLSSEL---AEECAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDRVaSKGEVVSHIASDNRVGGKMAGDFIA----KKVGAdakviqLEGIAGTSAARERGEGFKQSLDQNKFKL 181
Cdd:cd06278 76 RGIPVVLFNRV-VEDPGVDSVSCDNRAGGRLAADLLLaaghRRIAF------LGGPEGTSTSRERERGFRAALAELGLPP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727170941 182 LASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT----DVIVVGFDGTA 243
Cdd:cd06278 149 PAVEAGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGLvvpeDISVVGFDDIP 214
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
28-293 |
1.13e-25 |
|
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380507 [Multi-domain] Cd Length: 267 Bit Score: 102.62 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKE---LANVQDLMVRApkLLLINPTDSdavgNAIKMAN 104
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREddlLDMLRSRRVDG--VILLSGRLD----AELLSEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIP-VITLDRVASKGevVSHIASDNRVGGKMAGDFIA----KKVGAdakviqlegIAGTSA---ARERGEGFKQSLDQ 176
Cdd:cd06284 75 SKRYPiVQCCEYIPDSG--VPSVSIDNEAAAYDATEYLIslghRRIAH---------INGPLDnvyARERLEGYRRALAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 177 NKFKLLAS--QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTadgvkaveg 251
Cdd:cd06284 144 AGLPVDEDliIEGDFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRvpeDVSVIGFDDI--------- 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 727170941 252 gKLAA-------TVAQRPDQIGVIGVET-ADKVLKGEKVPATIPVDLKLV 293
Cdd:cd06284 215 -EFAEmfspsltTIRQPRYEIGETAAELlLEKIEGEGVPPEHIILPHELI 263
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
39-266 |
1.35e-25 |
|
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: 102.42 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 39 PFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANV-QDLMVRAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRVA 117
Cdd:cd19969 12 PYWDDVKEGFEDAGAELGVKTEYTGPATADVNEQITAiEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSDA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 118 SKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAArERGEGFKQSLDQNK-FKLLASQPADFDRTKGLN 196
Cdd:cd19969 92 PESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQPNHE-ERVEGFKEAFAEYPgIEVVAVGDDNDDPEKAAQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727170941 197 VMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLAATVAQRPDQIG 266
Cdd:cd19969 171 NTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTgKVKIVAFDDDPETLDLIKDGVIDASIAQRPWMMG 241
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
28-281 |
1.63e-25 |
|
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: 101.94 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDaVGNAIKMANQAK 107
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNIS-DEAIIKLLKEEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVShIASDNRVGGKMAGDFIAKKvgADAKVIQLEGIAGTSAARERGEGFKQSLDQNKFKLLASQ-- 185
Cdd:cd19976 80 IPVVVLDRYIEDNDSDS-VGVDDYRGGYEATKYLIEL--GHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWiy 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 186 PADFDRTKGLnVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTadgvkavEGGKLAA----TV 258
Cdd:cd19976 157 SGESSLEGGY-KAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKipeDLSVIGFDNI-------ILSEYITpaltTI 228
|
250 260
....*....|....*....|...
gi 727170941 259 AQRPDQIGVIGVETADKVLKGEK 281
Cdd:cd19976 229 AQPIFEMGQEAAKLLLKIIKNPA 251
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
29-295 |
4.18e-25 |
|
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: 101.60 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 29 IALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTD---SDAVgnaIKMANQ 105
Cdd:cd01540 2 IGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDqklGPAI---AAKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDRV---ASKGEVVSHIASDNRVGGKMAGDFIAKKV-------GADAKVIQLEgIAGTSAARERGEGFKQSLD 175
Cdd:cd01540 79 AGIPVIAVDDQlvdADPMKIVPFVGIDAYKIGEAVGEWLAKEMkkrgwddVKEVGVLAIT-MDTLSVCVDRTDGAKDALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 176 QNKFKLLASQPADFDRT---KGLNVMQNLLTAHPDVQ--AVFAQNDEMALGALRALQTAG--KTDVIVVGFDG--TADGV 246
Cdd:cd01540 158 AAGFPEDQIFQAPYKGTdteGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAGfdAEDIIGVGIGGylAADEE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 727170941 247 KAVEGGKLAATVAQRPDQIGVIGVET-ADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd01540 238 FKKQPTGFKASLYISPDKHGYIAAEElYNWITDGKPPPAETLTDGVIVTR 287
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
28-266 |
4.61e-25 |
|
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: 100.72 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINP---TDSDAVgnaiKMAN 104
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPaagTTAELL----RRLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLDRvASKGEVVSHIASDNRVGGKMAGDFIAKKvGADaKVIQLEGIAGTSAARERGEGFKQSLDQNKFKLLAS 184
Cdd:cd06289 77 AWGIPVVLALR-DVPGSDLDYVGIDNRLGAQLATEHLIAL-GHR-RIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 185 Q--PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDgtaDgvkaVEGGKLA---- 255
Cdd:cd06289 154 LivPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEpgrDIAVVGFD---D----VPEAALWtppl 226
|
250
....*....|.
gi 727170941 256 ATVAQRPDQIG 266
Cdd:cd06289 227 TTVSVHPREIG 237
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-262 |
5.43e-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: 380535 [Multi-domain] Cd Length: 272 Bit Score: 100.77 E-value: 5.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVV-STLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELA-NVQDLMVRAPKLLLINPTDSDAVGNAIKMANQ 105
Cdd:cd06312 1 TIYVIShGSPSDPFWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQArLIEQAIAAKPDGIIVTIPDPDALEPALKRAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITL----DRVASKGEVVSHIASDNRVGGKMAGD-FIAKKVGADAKVIQLEGIAGTSAareRGEGFKQSLDQNKFK 180
Cdd:cd06312 81 AGIPVIAInsgdDRSKERLGALTYVGQDEYLAGQAAGErALEAGPKNALCVNHEPGNPGLEA---RCKGFADAFKGAGIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 181 LLASQPADfDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTD-VIVVGFDGTADGVKAVEGGKLAATVA 259
Cdd:cd06312 158 VELLDVGG-DPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGkVKIGTFDLSPETLEAIKDGKILFAID 236
|
...
gi 727170941 260 QRP 262
Cdd:cd06312 237 QQP 239
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
29-292 |
6.03e-25 |
|
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: 100.40 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 29 IALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQaKI 108
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQ-NV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 109 PVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKvgADAKVIQLEGIAGTSAARERGEGFKQSLDQNKFKL--LASQP 186
Cdd:cd01537 81 PVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKH--GHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTeqLQLDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 187 ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---TDVIVVGFDGTADGVKAvegGKLAATVAQRPD 263
Cdd:cd01537 159 GDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLrvpSDISVFGYDALPEALKS---GPLLTTILQDAN 235
|
250 260 270
....*....|....*....|....*....|
gi 727170941 264 QIGVIGVETA-DKVLKGEKVPATIPVDLKL 292
Cdd:cd01537 236 NLGKTTFDLLlNLADNWKIDNKVVRVPYVL 265
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
28-284 |
3.60e-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: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVL-DSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd06302 1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDR--VASKGEVVSHIASDNRVGGKMAgDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN--KFKLL 182
Cdd:cd06302 81 GIKVITWDSdaPPSARDYFVNQADDEGLGEALV-DSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKypDIELV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 183 ASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTD-VIVVGFdGTADGVKA-VEGGKLAATVAQ 260
Cdd:cd06302 160 DTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGkVAVTGI-GLPNTARPyLKDGSVKEGVLW 238
|
250 260
....*....|....*....|....
gi 727170941 261 RPDQIGVIGVETADKVLKGEKVPA 284
Cdd:cd06302 239 DPAKLGYLTVYAAYQLLKGKGFTE 262
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
28-240 |
3.70e-24 |
|
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: 98.36 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLM---VRApkLLLINPTDSDAvgnAIKMAN 104
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLdrrCDA--IILHSRALSDE---ELILIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLDRvaskgevvsHIAS--------DNRVGGKMAGDFIakkvgadakvIQL--EGIA------GTSAARERGE 168
Cdd:cd06270 76 EKIPPLVVINR---------YIPGladrcvwlDNEQGGRLAAEHL----------LDLghRRIAcitgplDIPDARERLA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727170941 169 GFKQSLDQN--KFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KTDVIVVGFD 240
Cdd:cd06270 137 GYRDALAEAgiPLDPSLIIEGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGikvPEDVSVIGFD 213
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
28-285 |
7.98e-24 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380480 [Multi-domain] Cd Length: 283 Bit Score: 97.88 E-value: 7.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERG---EGFKQSLDQNKFKLLAS 184
Cdd:cd01538 81 IKVIAYDRLILNADVDYYISFDNEKVGELQAQALLDAKPEGNYVLIGGSPTDNNAKLFRDgqmKVLQPAIDSGKIKVVGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 185 QPAD-FDRTKGLNVMQNLLTAH-PDVQAVFAQNDEMALGALRALQTAG-KTDVIVVGFDGTADGVKAVEGGKLAATVAQR 261
Cdd:cd01538 161 QWVDdWLPANAQQIMENALTANgNNVDAVVASNDGTAGGAIAALKAQGlSGGVPVSGQDADLAAIKRILAGTQTMTVYKD 240
|
250 260
....*....|....*....|....
gi 727170941 262 PDQIGVIGVETADKVLKGEKVPAT 285
Cdd:cd01538 241 IRLLADAAAEVAVALMRGEKPPIN 264
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
29-289 |
1.05e-23 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 97.72 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 29 IALVVSTLN---NPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKmANQ 105
Cdd:cd01391 2 IGVVTSSLHqirEQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNL-AQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDRV------ASKGEVVSHIASDNRVGGKMAGDFIAKKVGAdaKVIQLEGIAGTSAaRERGEGFKQSLDQNKF 179
Cdd:cd01391 81 FDIPQLALDATsqdlsdKTLYKYFLSVVFSDTLGARLGLDIVKRKNWT--YVAAIHGEGLNSG-ELRMAGFKELAKQEGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 180 KLLASQPADFDR-TKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT-DVIVVGFDGT--ADGVKAVEGGKLA 255
Cdd:cd01391 158 CIVASDKADWNAgEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLVgDVSVIGSDGWadRDEVGYEVEANGL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 727170941 256 ATVAQRPDQIGVIGV------ETADKVLKGEKVPATIPVD 289
Cdd:cd01391 238 TTIKQQKMGFGITAIkamadgSQNMHEEVWFDEKGDALGR 277
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-272 |
1.50e-23 |
|
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: 96.91 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMAnqAK 107
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAA--RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVShIASDNRVGGKMAGDFIAKKvgADAKVIQLEGIAGTSAARERGEGFKQSLDQN--KFKLLASQ 185
Cdd:cd06285 79 VPVVLVDRRIGDTALPS-VTVDNELGGRLATRHLLEL--GHRRIAVVAGPLNASTGRDRLRGYRRALAEAglPVPDERIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 186 PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTAdgvkaveggkLAA------ 256
Cdd:cd06285 156 PGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRvpeDLSVVGFDDIP----------LAAflpppl 225
|
250
....*....|....*..
gi 727170941 257 -TVAQRPDQIGVIGVET 272
Cdd:cd06285 226 tTVRQPKYEMGRRAAEL 242
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
28-283 |
3.83e-23 |
|
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: 95.70 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLM-VRAPKLLLINPTDSDAVGNAIKMANqa 106
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKeKRVDGIIFASGTLTEENKQLLKNMN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 kIPVITLDRVaSKGEVVSHIASDNRVGGKMAGDFIAKKvgaDAKVIQLegIAG----TSAARERGEGFKQSL-DQN-KFK 180
Cdd:cd19975 79 -IPVVLVSTE-SEDPDIPSVKIDDYQAAYDATNYLIKK---GHRKIAM--ISGplddPNAGYPRYEGYKKALkDAGlPIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 181 LLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KTDVIVVGFDGTadgvkaveggKLAA- 256
Cdd:cd19975 152 ENLIVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGirvPEDISVIGFDNT----------EIAEm 221
|
250 260 270
....*....|....*....|....*....|...
gi 727170941 257 ------TVAQRPDQIGVIGVETADKVLKGEKVP 283
Cdd:cd19975 222 sippltTVSQPFYEMGKKAVELLLDLIKNEKKE 254
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
54-290 |
5.89e-23 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 95.62 E-value: 5.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 54 KLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRVAsKGEVVSHIASDNRVG 133
Cdd:cd19993 27 KAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDRLI-ENPIAFYISFDNVEV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 134 GKMAGDFIAKKVGADAKVIQLEGIAGTSAARERG---EGFKQSLDQNKFKLLASQPAD-FDRTKGLNVMQNLLTAHP-DV 208
Cdd:cd19993 106 GRMQARGVLKAKPEGNYVFIKGSPTDPNADFLRAgqmEVLQPAIDSGKIKIVGEQYTDgWKPANAQKNMEQILTANNnKV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 209 QAVFAQNDEMALGALRALQTAGKTDVI-VVGFDGTADGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEKVPATIP 287
Cdd:cd19993 186 DAVVASNDGTAGGAVAALAAQGLAGKVpVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKGTKIEAIKG 265
|
...
gi 727170941 288 VDL 290
Cdd:cd19993 266 AAL 268
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
29-262 |
1.59e-22 |
|
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: 94.26 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 29 IALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQN-NPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd19965 2 FVFVTHVTTNPFFQPVKKGMDDACELLGAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGE--VVSHIASDNRVGGKMAGDFIAKKVGAD-AKVIQLEGIAGTSAARERGEGFKQSLDQNK----FK 180
Cdd:cd19965 82 IPVVAFNVDAPGGEnaRLAFVGQDLYPAGYVLGKRIAEKFKPGgGHVLLGISTPGQSALEQRLDGIKQALKEYGrgitYD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 181 LLASQPadfDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTD-VIVVGFDGTADGVKAVEGGKLAATVA 259
Cdd:cd19965 162 VIDTGT---DLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGkVLVGGFDLVPEVLQGIKAGYIDFTID 238
|
...
gi 727170941 260 QRP 262
Cdd:cd19965 239 QQP 241
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
28-240 |
1.95e-22 |
|
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: 93.88 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAvgNAIKMANQAK 107
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENS--EGLQALIAQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQleGIAGTSAARERGEGFKQSLDQNKFK----LLA 183
Cdd:cd06299 79 LPVVFVDREVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYIS--GPLSTSTGRERLAAFRAALTAAGIPideeLVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 184 SqpADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KTDVIVVGFD 240
Cdd:cd06299 157 F--GDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGlriGDDVSLISFD 214
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
11-240 |
6.35e-22 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 93.61 E-value: 6.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 11 SAIALSATLSANamakDTIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINP 90
Cdd:PRK10423 45 SALARSLKLNQT----RTIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 91 TDSDAVGNAIkMANQAKIPVITLDrvASKGEVVSHIASDNRV-GGKMAGDFIAKKvgADAKVIQLEGIAGTSAARERGEG 169
Cdd:PRK10423 121 TETHQPSREI-MQRYPSVPTVMMD--WAPFDGDSDLIQDNSLlGGDLATQYLIDK--GYTRIACITGPLDKTPARLRLEG 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727170941 170 FKQSLDQNKFKLLASQP--ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFD 240
Cdd:PRK10423 196 YRAAMKRAGLNIPDGYEvtGDFEFNGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLSvpqDIAVIGYD 271
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-293 |
8.40e-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: 92.19 E-value: 8.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVR-APKLLLINPTDSDAVgnaIKMANQA 106
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERgVDGLILVGSDHDPEL---FELLEQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDrVASKGEVVSHIASDNRVGGKMAGDFIA----KKVGAdakviqlegIAGTSA----ARERGEGFKQSLDQNK 178
Cdd:cd06273 78 QVPYVLTW-SYDEDSPHPSIGFDNRAAAARAAQHLLdlghRRIAV---------ISGPTAgndrARARLAGIRDALAERG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 179 FKL----LASQPADFDRTKGLnvMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTAdgvkaveg 251
Cdd:cd06273 148 LELpeerVVEAPYSIEEGREA--LRRLLARPPRPTAIICGNDVLALGALAECRRLGISvpeDLSITGFDDLE-------- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 727170941 252 gkLAA-------TV---AQRpdqigvIGVETADKV---LKGEKVPATIPVDLKLV 293
Cdd:cd06273 218 --LAAhlsppltTVrvpARE------IGELAARYLlalLEGGPPPKSVELETELI 264
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
28-294 |
2.02e-21 |
|
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: 91.58 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSM----KDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMA 103
Cdd:cd19998 1 KIALSNSYSGNDWRQEMiniaKAAAKQPPYADKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 104 NQAKIPVITLDRVASkGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKLL 182
Cdd:cd19998 81 CDAGIVVVAFDNVVD-EPCAYNVNTDQAKAGEQTAQWLVDKLGGKGNILMVRGVPGTSVDRDRYEGAKEVFKKYpDIKVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 183 ASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMalGALRALQTAGKtDVIVVGFDGTADGVKAV---EGGKLAATVA 259
Cdd:cd19998 160 AEYYGNWDDGTAQKAVADALAAHPDVDGVWTQGGET--GVIKALQAAGH-PLVPVGGEAENGFRKAMlepLANGLPGISA 236
|
250 260 270
....*....|....*....|....*....|....*
gi 727170941 260 QRPDQIGVIGVETADKVLKGEKVPATIPVDLKLVT 294
Cdd:cd19998 237 GSPPALSAVALKLAVAVLEGEKEPKTIELPLPWVT 271
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
28-240 |
2.78e-21 |
|
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: 90.67 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAvgNAIKMANQAK 107
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNE--DLIEKLVKSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEvVSHIASDNRVGGKMAGDFIAKK-------VGADAKVIQLEgiagtsaarERGEGFKQSLDQNKFK 180
Cdd:cd19977 79 IPVVFVDRYIPGLD-VDTVVVDNFKGAYQATEHLIELghkriafITYPLELSTRQ---------ERLEGYKAALADHGLP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727170941 181 LLASQPADFDRTKGLNV-MQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFD 240
Cdd:cd19977 149 VDEELIKHVDRQDDVRKaISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRipdDIALIGFD 212
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
28-285 |
5.20e-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: 90.77 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd19994 1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKGEVVSHIAS-DNRVGGKMAGDFIAKKVG--ADAKVIQLEGIAGTSA---ARERGEGFKQSL----DQN 177
Cdd:cd19994 81 IPVIAYDRLIMNTDAVDYYVTfDNEKVGELQGQYLVDKLGlkDGKGPFNIELFAGSPDdnnAQLFFKGAMEVLqpyiDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 178 KFKLLASQP-------ADFDRTKGLNVMQNLLTAHP----DVQAVFAQNDEMALGALRALQTAGKTD---VIVVGFDGTA 243
Cdd:cd19994 161 TLVVRSGQTtfeqvatPDWDTETAQARMETLLSAYYtggkKLDAVLSPNDGIARGVIEALKAAGYDTgpwPVVTGQDAED 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 727170941 244 DGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEKVPAT 285
Cdd:cd19994 241 ASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVEVN 282
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
28-240 |
5.41e-21 |
|
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: 89.91 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLN-NPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANqa 106
Cdd:cd06288 1 TIGLITDDIAtTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLPPELTD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 kIPVITLDRVASKGEVVSHIAsDNRVGGKMAGDFI----AKKVGAdakviqlegIAGTS---AARERGEGFKQSLDQNKF 179
Cdd:cd06288 79 -IPLVLLNCFDDDPSLPSVVP-DDEQGGYLATRHLieagHRRIAF---------IGGPEdslATRLRLAGYRAALAEAGI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727170941 180 KLLAS--QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---TDVIVVGFD 240
Cdd:cd06288 148 PYDPSlvVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLrvpEDLSVVGFD 213
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-266 |
5.74e-21 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 90.02 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPtdSDAVGNAIKMANQAK 107
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTP--SDDDLSHLARLRARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASkGEVVSHIASDNRVGGKMAGDFIakkVGADAKVIQ-LEGIAGTSAARERGEGFKQSLD----QNKFKLL 182
Cdd:cd06293 79 TAVVLLDRPAP-GPAGCSVSVDDVQGGALAVDHL---LELGHRRIAfVSGPLRTRQVAERLAGARAAVAeaglDPDEVVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 183 ASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KTDVIVVGFDGtadgvkaVEGGKLAA--- 256
Cdd:cd06293 155 ELSAPDANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGlrvPDDVSVVGYDD-------LPFAAAANppl 227
|
250
....*....|.
gi 727170941 257 -TVAQRPDQIG 266
Cdd:cd06293 228 tTVRQPSYELG 238
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-292 |
1.18e-20 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 88.88 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDavGNAI-KMANQA 106
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQ--GSEAlELLEEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDRVaSKGEVVSHIASDNRVGGKMAGDFIAKK-------VGADakviqlegIAGTSAARERGEGFKQSLDQNKF 179
Cdd:cd06282 79 GVPYVLLFNQ-TENSSHPFVSVDNRLASYDVAEYLIALghrriamVAGD--------FSASDRARLRYQGYRDALKEAGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 180 KLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGtadgvkaVEGGKLA- 255
Cdd:cd06282 150 KPIPIVEVDFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRvpdDVSVIGFDG-------IAIGELLt 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 727170941 256 ---ATVAQRPDQIGVIGVETADKVLKGEKVPATIPVDLKL 292
Cdd:cd06282 223 ptlATVVQPSRDMGRAAADLLLAEIEGESPPTSIRLPHHL 262
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
38-286 |
1.34e-20 |
|
ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380517 [Multi-domain] Cd Length: 269 Bit Score: 88.79 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 38 NPFFVSMKDGAQQEANKLGYNLVvLDSQNNPAKELANVQDlMVRAPK---LLLINPTDSDAVgnaIKMANQAKIPVITLD 114
Cdd:cd06294 16 NPFFSEVLRGISQVANENGYSLL-LATGNTEEELLEEVKR-MVRGRRvdgFILLYSKEDDPL---IEYLKEEGFPFVVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 115 RVASKGEVvSHIASDNRVGGKMAGDFIAKK-------VGADAKVIqlegiagtsAARERGEGFKQSLDQNKFKLLASQ-- 185
Cdd:cd06294 91 KPLDDNDV-LYVDNDNVQAGYEATEYLIDKghkriafIGGDKNLV---------VSIDRLQGYKQALKEAGLPLDDDYil 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 186 PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---TDVIVVGFDgtaDGVKAVEGGKLAATVAQRP 262
Cdd:cd06294 161 LLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLrvpEDVSIISFN---NSPLAELASPPLTSVDINP 237
|
250 260 270
....*....|....*....|....*....|.
gi 727170941 263 DQIGVIGVETADKVLKGEK-------VPATI 286
Cdd:cd06294 238 YELGREAAKLLINLLEGPEslpknviVPHEL 268
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
26-291 |
1.49e-20 |
|
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).
Pssm-ID: 395423 [Multi-domain] Cd Length: 281 Bit Score: 89.11 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 26 KDTIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLInpTDSDAVGNAI-KMAN 104
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIII--TTPAPSGDDItAKAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIaKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQNKFKLLAS 184
Cdd:pfam00532 79 GYGIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYL-IAEGHKRPIAVMAGPASALTARERVQGFMAALAAAGREVKIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 185 QPA--DFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDVI---------VVGFDGTAD-GVKAVEGG 252
Cdd:pfam00532 158 HVAtgDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRVKIPdivgiginsVVGFDGLSKaQDTGLYLS 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 727170941 253 KLaaTVAQRPDQIgvIGVETADKVL----KGEKVPAT--IPVDLK 291
Cdd:pfam00532 238 PL--TVIQLPRQL--LGIKASDMVYqwipKFREHPRVllIPRDFF 278
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
28-290 |
2.17e-20 |
|
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: 88.32 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTD-SDAvgnAIKMANQA 106
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEhTPA---TRKLLRAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVI-TLDRVASKGEVVshIASDNRVGGKMAGDFIAKK-------VGADakviqlegIAGTSAARERGEGFKQSLDQNK 178
Cdd:cd01575 78 GIPVVeTWDLPDDPIDMA--VGFSNFAAGRAMARHLIERgyrriafVGAR--------LDGDSRARQRLEGFRDALAEAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 179 FK----LLASQPADFDRtkGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTaDGVKAVEG 251
Cdd:cd01575 148 LPlplvLLVELPSSFAL--GREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRvpgDIAIAGFGDL-DIAAALPP 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 727170941 252 GklAATVAQRPDQIGVIGVETADKVLKGEKVPATIpVDL 290
Cdd:cd01575 225 A--LTTVRVPRYEIGRKAAELLLARLEGEEPEPRV-VDL 260
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
58-286 |
2.41e-20 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380650 [Multi-domain] Cd Length: 294 Bit Score: 88.50 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 58 NLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRVASKGEVVSHIASDNRVGGKMA 137
Cdd:cd19995 34 KVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPADYYVSFDNVAVGEAQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 138 GDFIAKKVGADAK----VIQLEGIAGTSAARERGEG----FKQSLDQNKFKLLASQPA-DFDRTKGLNVMQNLLTAHPD- 207
Cdd:cd19995 114 AQSLVDHLKAIGKkgvnIVMINGSPTDNNAGLFKKGahevLDPLGDSGELKLVCEYDTpDWDPANAQTAMEQALTKLGNn 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 208 VQAVFAQNDEMALGALRALQTAGKTDVIVV-GFDGTADGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEKVPATI 286
Cdd:cd19995 194 IDGVLSANDGLAGGAIAALKAQGLAGKVPVtGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGETPPSDL 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
28-295 |
9.79e-20 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380652 [Multi-domain] Cd Length: 305 Bit Score: 86.96 E-value: 9.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDG---AQQEANKLGY--NLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKM 102
Cdd:cd19997 1 VIALSNSYAGNTWRQQMVDAfeeAAKKAKADGLiaDYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 103 ANQAKIPVITLDRVASKgEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN-KFKL 181
Cdd:cd19997 81 ACDAGIKVVVFDSGVTE-PCAYILNNDFEDYGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALKKYpDLKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 182 LASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEmALGALRALQTAGKtDVIVVGFDGTADGVK--AVEGGKLA-ATV 258
Cdd:cd19997 160 VAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGGD-GYGAAQAFEAAGR-PLPIIIGGNRGEFLKwwQEEYAKNGyETV 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 727170941 259 AQRPDQ-IGVIGVETADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd19997 238 SVSTDPgQGSAAFWVALDILNGKDVPKEMILPVVTITE 275
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
125-295 |
2.09e-19 |
|
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: 86.27 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 125 HIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTsAARERGEGFKQSLDQN-KFKLLASQPADFDRTKGLNVMQNLLT 203
Cdd:cd06303 136 YVGFDHAEGSRMLAKHFIKIFPEEGKYAILYLTEGY-VSDQRGDTFIDEVARHsNLELVSAYYTDFDRESAREAARALLA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 204 AHPDVQAVFAQNDEMALGALRALQTAGK-TDVIVVGFDGTADGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEKV 282
Cdd:cd06303 215 RHPDLDFIYACSTDIALGAIDALQELGReTDIMINGWGGGSAELDALQKGGLDVTVMRMNDDNGIAMAEAIKLDLEGREV 294
|
170
....*....|...
gi 727170941 283 PATIPVDLKLVTK 295
Cdd:cd06303 295 PTVYAGDFELVTK 307
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
50-289 |
6.71e-19 |
|
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: 84.21 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 50 QEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRVASKGEVVSHIASD 129
Cdd:cd19991 23 KKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNADVDLYVSFD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 130 NRVGGKMAGDFIAKKVGADAKVIqLEGIAGTSAARERGEGFKQSL----DQNKFKLLASQ-PADFDRTKGLNVMQNLLTA 204
Cdd:cd19991 103 NEKVGELQAEALVKAKPKGNYVL-LGGSPTDNNAKLFREGQMKVLqpliDSGDIKVVGDQwVDDWDPEEALKIMENALTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 205 H-PDVQAVFAQNDEMALGALRALQTAG-KTDVIVVGFDGTADGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEKV 282
Cdd:cd19991 182 NnNKIDAVIASNDGTAGGAIQALAEQGlAGKVAVSGQDADLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKN 261
|
....*..
gi 727170941 283 PATIPVD 289
Cdd:cd19991 262 EANRTIN 268
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
39-262 |
8.63e-19 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380621 [Multi-domain] Cd Length: 278 Bit Score: 83.91 E-value: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 39 PFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLIN-PTDSDAVGNAIKMANQAKIPVITLDRVA 117
Cdd:cd19966 13 PFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMgHPGDGAYTPLIEAAKKAGIIVTSFNTDL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 118 SKGEVVS----HIASDNRVGGKMAGDFIAK--KVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN--KFKLLASQPADF 189
Cdd:cd19966 93 PKLEYGDcglgYVGADLYAAGYTLAKELVKrgGLKTGDRVFVPGLLPGQPYRVLRTKGVIDALKEAgiKVDYLEISLEPN 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727170941 190 DRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT--DVIVVGFDGTADGVKAVEGGKLAATVAQRP 262
Cdd:cd19966 173 KPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKKpgEIPVAGFDLSPATVQAIKSGYVNATIDQQP 247
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
28-284 |
1.31e-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: 83.87 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNlVVLD--SQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQ 105
Cdd:cd20003 1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVD-VTYDgpTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDRVASKG--EVVSHIASDNRVGGKMAgDFIAKKVGADAKV----------IQLEGIAgtsAARERgegfkQS 173
Cdd:cd20003 80 KGIKVVTWDSDVNPDarDFFVNQATPEGIGKTLV-DMVAEQTGEKGKVaivtssptatNQNAWIK---AMKAY-----IA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 174 LDQNKFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQnDEMAL-GALRALQTAGKT-DVIVVGFDGTADGVKAVEG 251
Cdd:cd20003 151 EKYPDMKIVTTQYGQEDPAKSLQVAENILKAYPDLKAIIAP-DSVALpGAAEAVEQLGRTgKVAVTGLSTPNVMRPYVKD 229
|
250 260 270
....*....|....*....|....*....|...
gi 727170941 252 GKLAATVAQRPDQIGVIGVETADKVLKGEKVPA 284
Cdd:cd20003 230 GTVKSVVLWDVVDLGYLAVYVARALADGTLLKV 262
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
28-290 |
4.20e-18 |
|
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380506 [Multi-domain] Cd Length: 266 Bit Score: 81.83 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLM---VRApklLLINPTDSDAvgNAIKMAN 104
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLsqrVDG---LILQPTGNNN--DAYLELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLDRvASKGEVVSHIASDNRVGGKMAGDFIAKKvGADAKVIQLEGIAGTSAARERGEGFKQSLDQNKF--KLL 182
Cdd:cd06283 76 QKGLPVVLVDR-QIEPLNWDTVVTDNYDATYEATEHLKEQ-GYERIVFVTEPIKGISTRRERLQGFLDALARYNIegDVY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 183 ASQPADFDRTKglNVMQNLLTAHPDVQ-AVFAQNDEMALGALRALQTAGK---TDVIVVGFDGTadgvkavEGGKLAA-- 256
Cdd:cd06283 154 VIEIEDTEDLQ--QALAAFLSQHDGGKtAIFAANGVVLLRVLRALKALGIripDDVGLCGFDDW-------DWADLIGpg 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 727170941 257 --TVAQRPDQIGVIGVETADKVLKGEKVPA---TIPVDL 290
Cdd:cd06283 225 itTIRQPTYEIGKAAAEILLERIEGDSGEPkeiELPSEL 263
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
28-242 |
7.10e-18 |
|
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: 81.45 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAP--KLLLINP-TDSDAVgnaIKMAN 104
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVEPCDSDDEDLADRLRRFLSRSRpdGVILTPPlSDDPAL---LDALD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVItldRVASKGEVV--SHIASDNRVGGKMAGD-----------FIAkkvgadakviqleGIAGTSAARERGEGFK 171
Cdd:cd01545 78 ELGIPYV---RIAPGTDDDrsPSVRIDDRAAAREMTRhlialghrrigFIA-------------GPPDHGASAERLEGFR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727170941 172 QSLDQNKFKLLAS--QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGT 242
Cdd:cd01545 142 DALAEAGLPLDPDlvVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRvpdDLSVAGFDDS 217
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
28-284 |
4.63e-17 |
|
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: 78.86 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPK---LLLINPTDSDavgnaIKMAN 104
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAgvvLVTSDPTSRQ-----LRLLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIA----KKVGAdakviqLEGIAGTSAARERGEGFKQSLDQNKfk 180
Cdd:cd06296 76 SAGIPFVLIDPVGEPDPDLPSVGATNWAGGRLATEHLLdlghRRIAV------ITGPPRSVSGRARLAGYRAALAEAG-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 181 lLASQPA-----DFDRTKGLNVMQNLLtAHPDV-QAVFAQNDEMALGALRALQTAG---KTDVIVVGFDGTadgvkavEG 251
Cdd:cd06296 148 -IAVDPDlvregDFTYEAGYRAARELL-ELPDPpTAVFAGNDEQALGVYRAARALGlrvPDDLSVIGFDDT-------PP 218
|
250 260 270
....*....|....*....|....*....|....*..
gi 727170941 252 GKLAA----TVAQRPDQIGVIGVETADKVLKGEKVPA 284
Cdd:cd06296 219 ARWTSppltTVHQPLREMGAVAVRLLLRLLEGGPPDA 255
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-242 |
6.04e-17 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 78.82 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPK--LLLINPTDSDAVGNAIkmaNQ 105
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDglILTPGDEDDPELAAAL---AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 AKIPVITLDRvaSKGEVVSHIASDNRVGGKMAgdfiakkvgadakVIQLEG-----IA------GTSAARERGEGFKQSL 174
Cdd:cd06281 78 LDIPVVLIDR--DLPGDIDSVLVDHRSGVRQA-------------TEYLLSlghrrIAlltggpDIRPGRERIAGFKAAF 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727170941 175 DQNK--FKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGT 242
Cdd:cd06281 143 AAAGlpPDPDLVRLGSFSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRipgDLSVVSIGDS 215
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
28-245 |
7.19e-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: 78.36 E-value: 7.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVST----LNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAkELANVQDlMVRAPK---LLLINPTDSDAvgnAI 100
Cdd:cd20010 1 AIGLVLPLdpgdLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGED-ELATYRR-LVERGRvdgFILARTRVNDP---RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 101 KMANQAKIPVITLDRVASKGEVvSHIASDNRVGGKMAGDFIA----KKVGAdakviqLEGIAGTSAARERGEGFKQSLDQ 176
Cdd:cd20010 76 AYLLERGIPFVVHGRSESGAPY-AWVDIDNEGAFRRATRRLLalghRRIAL------LNGPEELNFAHQRRDGYRAALAE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727170941 177 NKFKLLAS--QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTADG 245
Cdd:cd20010 149 AGLPVDPAlvREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSpgkDVSVIGHDDLLPA 222
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
28-288 |
1.01e-16 |
|
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: 78.01 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLD-SQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQa 106
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATvDEDDPASVREALDRLLSQRVDGIIVIAPDEAVLEALRRLPPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 kIPVITLDrvASKGEVVSHIASDNRVGGKMAGDFIakkvgadakvIQLeG------IAGTS---AARERGEGFKQSLDQN 177
Cdd:cd01574 80 -LPVVIVG--SGPSPGVPTVSIDQEEGARLATRHL----------LEL-GhrriahIAGPLdwvDARARLRGWREALEEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 178 KFKLLASQPADFDRTKGLNVMQNLLtAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTADgvkaveggkl 254
Cdd:cd01574 146 GLPPPPVVEGDWSAASGYRAGRRLL-DDGPVTAVFAANDQMALGALRALHERGLRvpeDVSVVGFDDIPE---------- 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 727170941 255 AA-------TVAQRPDQIGVIGVETADKVLKGEKVPATIPV 288
Cdd:cd01574 215 AAyfvppltTVRQDFAELGRRAVELLLALIEGPAPPPESVL 255
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
7-286 |
1.32e-16 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 78.84 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 7 ATLASAIALSATLSANAMAKdtIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLD--SQNNPAKELANVQDLMVRAPK 84
Cdd:PRK10936 29 LAQRTSLQYSPLLKAKKAWK--LCALYPHLKDSYWLSVNYGMVEEAKRLGVDLKVLEagGYYNLAKQQQQLEQCVAWGAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 85 LLLINPTDSDAVGNAIKMAnQAKIPVITL-DRVASKgEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQL------EGI 157
Cdd:PRK10936 107 AILLGAVTPDGLNPDLELQ-AANIPVIALvNGIDSP-QVTTRVGVSWYQMGYQAGRYLAQWHPKGSKPLNVallpgpEGA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 158 AGTSAARErgeGFKQSLDQNKFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVF--AQNDEMALGALRALQTAGKTDVI 235
Cdd:PRK10936 185 GGSKAVEQ---GFRAAIAGSDVRIVDIAYGDNDKELQRNLLQELLERHPDIDYIAgsAVAAEAAIGELRGRNLTDKIKLV 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 727170941 236 VVGFD-GTADGVKAvegGKLAATVAQRPDQIGVIGVETADKVLKGEKVPATI 286
Cdd:PRK10936 262 SFYLShQVYRGLKR---GKVLAAPSDQMVLQGRLAIDQAVRQLEGAPVPGDV 310
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
29-295 |
1.46e-16 |
|
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: 77.60 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 29 IALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLD----SQNNPAKELANVQDLMVRAPKLLLInPTDSDAVGNAIKMAN 104
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRihfvDSLDPEALAAALRRLAAGCDGVALV-APDHPLVRAAIDELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGAD-AKVIQLEGIAGTSAARERGEGFKQSLDQN--KFKL 181
Cdd:cd06307 81 ARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGRRpGKVLVILGSHRFRGHEEREAGFRSVLRERfpDLTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 182 LASQPADFDRTKGLNVMQNLLTAHPDVQAVF---AQNDemalGALRALQTAGKT-DVIVVGFDGTADGVKAVEGGKLAAT 257
Cdd:cd06307 161 LEVLEGLDDDELAYELLRELLARHPDLVGIYnagGGNE----GIARALREAGRArRVVFIGHELTPETRRLLRDGTIDAV 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 727170941 258 VAQRPDQIGVIGVET-ADKVLKGEKVPATIPVDLKLVTK 295
Cdd:cd06307 237 IDQDPELQARRAIEVlLAHLGGKGPAPPQPPIPIEIITR 275
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
28-293 |
4.62e-16 |
|
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380484 [Multi-domain] Cd Length: 259 Bit Score: 75.99 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPK---LLLINPTDSDavgnaIKMAN 104
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDgiiLFATEITDEH-----RKALK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLdrvaskGEVVSHIAS---DNRVGGKMAGDFIAKK-------VGADAKVIqlegiagtSAARERGEGFKQSL 174
Cdd:cd01542 76 KLKIPVVVL------GQEHEGFSCvyhDDYGAGKLLGEYLLKKghkniayIGVDEEDI--------AVGVARKQGYLDAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 175 DQNKFKLLASQPADFDRTKGLNVMQNLLTAHPDvQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTadgvkaveg 251
Cdd:cd01542 142 KEHGIDEVEIVETDFSMESGYEAAKELLKENKP-DAIICATDNIALGAIKALRELGIKipeDISVAGFGGY--------- 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 727170941 252 gKLAA-------TVAQRPDQIGVIGVETADKVLKGEKVPATIPVDLKLV 293
Cdd:cd01542 212 -DLSEfvspsltTVKFDYEEAGEKAAELLLDMIEGEKVPKKQKLPYELI 259
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
28-293 |
6.29e-16 |
|
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: 75.75 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVV-------STLNNPFFVSMKDGAQQEANKLGYNLVV--LDSQNNPAKELANVQdlmvRAPKLLLINPTDSDAVGN 98
Cdd:cd06295 5 TIAVVVpmdphgdQSITDPFFLELLGGISEALTDRGYDMLLstQDEDANQLARLLDSG----RADGLIVLGQGLDHDALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 99 AIKMANqakIPVITLDRVASKGEVVShIASDNRVGGKMAGD-FIAkkVGAdaKVIQLEGIAGTSAARERGEGFKQSLDQ- 176
Cdd:cd06295 81 ELAQQG---LPMVVWGAPEDGQSYCS-VGSDNVKGGALATEhLIE--IGR--RRIAFLGDPPHPEVADRLQGYRDALAEa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 177 -NKFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTAdgvkavegg 252
Cdd:cd06295 153 gLEADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISvpgDVAVVGYDDIP--------- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 727170941 253 kLAA-------TVAQRPDQIGVIGVETADKVLKGEkVPATIPVDLKLV 293
Cdd:cd06295 224 -LAAyfrppltTVRQDLALAGRLLVEKLLALIAGE-PVTSSMLPVELV 269
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
28-240 |
2.06e-15 |
|
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: 74.52 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSdavgnAIKMAN--- 104
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKS-----ALPNPNldl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 -----QAKIPVITLDRVASKGEvVSHIASDNRVGGKMAGDFIA----KKVGADAKVIQLEGIagtsaarERGEGFKQSLD 175
Cdd:cd01541 76 yeelqKKGIPVVFINSYYPELD-APSVSLDDEKGGYLATKHLIdlghRRIAGIFKSDDLQGV-------ERYQGFIKALR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727170941 176 QnkfkllASQPADFDRTKGLNV-----------MQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFD 240
Cdd:cd01541 148 E------AGLPIDDDRILWYSTedledrffaeeLREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRvpeDLSVVGFD 220
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
28-293 |
5.93e-15 |
|
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: 73.07 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLN----NPFFVSMKDGAQQEANKLGYNlVVLDSQNNPAKELANVQDLM--VRAPKLLLINPTDSDAVGNAIK 101
Cdd:cd06292 1 LIGYVVPELPggfsDPFFDEFLAALGHAAAARGYD-VLLFTASGDEDEIDYYRDLVrsRRVDGFVLASTRHDDPRVRYLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 102 manQAKIPVITLDRVASKGEVvSHIASDNRVGGKMAGDFIAKKvGAdAKVIQLEGIAGTSAARERGEGFKQSLDQNKfkl 181
Cdd:cd06292 80 ---EAGVPFVAFGRANPDLDF-PWVDVDGAAGMRQAVRHLIAL-GH-RRIGLIGGPEGSVPSDDRLAGYRAALEEAG--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 182 LASQPA-----DFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTAdgvkaveggk 253
Cdd:cd06292 151 LPFDPGlvvegENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRvgrDVSVVGFDDSP---------- 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 727170941 254 LAA-------TVAQRPDQIGVIGVETADKVLKGEKV-PATIPVDLKLV 293
Cdd:cd06292 221 LAAfthppltTVRQPIDEIGRAVVDLLLAAIEGNPSePREILLQPELV 268
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
28-292 |
1.49e-14 |
|
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: 71.78 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVST-----LNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELAN---------------VQDLMVRAPKLLL 87
Cdd:cd01544 1 TIGIIQWYseeeeLEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLESLLEkvdgiiaigkfskeeIEKLKKLNPNIVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 88 I----NPTDSDAVG----NAIKMAnqakipvitLDRVASKGevVSHIAsdnrvggkmagdFIA-KKVGADAKVIQLEgia 158
Cdd:cd01544 81 VdsnpDPDGFDSVVpdfeQAVRQA---------LDYLIELG--HRRIG------------FIGgKEYTSDDGEEIED--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 159 gtsaarERGEGFKQSL-DQNKFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DV 234
Cdd:cd01544 135 ------PRLRAFREYMkEKGLYNEEYIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKvpeDI 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727170941 235 IVVGFDGTAdgvkaveggkLAA-------TVAQRPDQIGVIGVETA-DKVLKGEKVP--ATIPVDLKL 292
Cdd:cd01544 209 SIISFNDIE----------VAKyvtppltTVHIPTEEMGRTAVRLLlERINGGRTIPkkVLLPTKLIE 266
|
|
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
3-295 |
1.72e-14 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 72.45 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 3 MKKLATLAsAIALSATLSANAMAKDT-IALVVSTLNNPFFVSMKDGAQQEANKL-GYNLVVLDSQNNPAKELANVQDLMV 80
Cdd:PRK15395 1 NKKVLTLS-ALMASMLFGAAAAAADTrIGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 81 RAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRVASKGEVVSH-----IASDNRVGGKMAGDFIAKKVGADAK----- 150
Cdd:PRK15395 80 KGVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYdkayyVGTDSKESGIIQGDLIAKHWKANPAwdlnk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 151 --VIQ---LEGIAGTSAARERGEGFKQSLDQNKFKL--LASQPADFDRTKGLNVMQNLLTAHP--DVQAVFAQNDEMALG 221
Cdd:PRK15395 160 dgKIQyvlLKGEPGHPDAEARTTYVIKELNDKGIKTeqLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727170941 222 ALRALQTAGKTDVIVVGFDGTADGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEkvPATIPVDLKLVTK 295
Cdd:PRK15395 240 AVEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGK--GAAEGTNWKIENK 311
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
36-245 |
3.23e-13 |
|
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: 68.39 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 36 LNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAkELANVQDLMVRApkLLLINPTDSDAVgnaIKMANQAKIPVITLDR 115
Cdd:cd06279 14 FSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGS-AAAAVRNAAVDG--FIVYGLSDDDPA---VAALRRRGLPLVVVDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 116 VASKGevVSHIASDNRVGGKMAGDFI----AKKVG-------ADAKVIQLEGI----AGTSAARERGEGFKQSLDQNKFK 180
Cdd:cd06279 88 PAPPG--IPSVGIDDRAAARAAARHLldlgHRRIAilslrldRGRERGPVSAErlaaATNSVARERLAGYRDALEEAGLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727170941 181 LLASQP---ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDGTADG 245
Cdd:cd06279 166 LDDVPVveaPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRvpeDLSVTGFDDIPEA 236
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
52-290 |
3.48e-13 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 68.87 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 52 ANKLGYNLVV--LDSQNNPAKELAnVQDLMVRAPKLLLIN-PTDSDavgNAIKMANQ-AKIPVITLDrvASKGEVVSHIA 127
Cdd:PRK09526 89 ADQLGYSVVIsmVERSGVEACQAA-VNELLAQRVSGVIINvPLEDA---DAEKIVADcADVPCLFLD--VSPQSPVNSVS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 128 SDNRVGGKMAGDFIAKkvGADAKVIQLEGIAGTSAARERGEGFKQSLDQNKFKLLASQPADFDRTKGLNVMQNLLTAHPD 207
Cdd:PRK09526 163 FDPEDGTRLGVEHLVE--LGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQPIAVREGDWSAMSGYQQTLQMLREGPV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 208 VQAVFAQNDEMALGALRAL---QTAGKTDVIVVGFDGTADgvkaveggklAA-------TVAQRPDQIGVIGVETADKVL 277
Cdd:PRK09526 241 PSAILVANDQMALGVLRALhesGLRVPGQISVIGYDDTED----------SSyfippltTIKQDFRLLGKEAVDRLLALS 310
|
250
....*....|....*
gi 727170941 278 KGEKVPAT--IPVDL 290
Cdd:PRK09526 311 QGQAVKGSqlLPTSL 325
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
129-241 |
1.18e-12 |
|
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380520 [Multi-domain] Cd Length: 268 Bit Score: 66.72 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 129 DNRVGGKMAGDFIAKKVGAD--AKVIQLEGIAGTSAARERGEGFKQSLDQNKFKLLASQP--ADFDRTKGLNVMQNLLTA 204
Cdd:cd06297 97 DNVKGGFMATEYLAGLGEREyvFFGIEEDTVFTETVFREREQGFLEALNKAGRPISSSRMfrIDNSSKKAECLARELLKK 176
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 727170941 205 HPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFDG 241
Cdd:cd06297 177 ADNPAAFFAAADLVALGLIRAAQSLGLRvgeDVAVIGFDG 216
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
28-240 |
1.65e-12 |
|
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: 66.03 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELanvqdlmvRAPKLL-------LI-----NPTDsda 95
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKEL--------RALELLktkqidgLIitsreNDWE--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 96 vgnAIKM------------ANQAKIPVITLDRVASKGEVVSHIasdnrvggKMAGdfiAKKVGadakvIQLEGIAGTSA- 162
Cdd:cd06286 70 ---VIEPyakygpivlceeTDSPDIPSVYIDRYEAYLEALEYL--------KEKG---HRKIG-----YCLGRPESSSAs 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 163 ARERGEGFKQSLDQNKfklLASQPAD-----FDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---TDV 234
Cdd:cd06286 131 TQARLKAYQDVLGEHG---LSLREEWiftncHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIrvpEDL 207
|
....*.
gi 727170941 235 IVVGFD 240
Cdd:cd06286 208 AVIGFD 213
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
1-284 |
2.58e-12 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 66.30 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 1 MKMKKLatLASAIALSATLSANAMAKD-TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLM 79
Cdd:PRK10355 1 MKIKNI--LLTLCASLLLTSVAAHAKEvKIGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQMSQIENMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 80 VRAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGadakviqlEG--- 156
Cdd:PRK10355 79 NRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDFYISFDNEKVGELQAKALVDKVP--------QGnyf 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 157 IAGTSAARERGEGFKQS--------LDQNKFKLLASQPAD-FDRTKGLNVMQNLLTAHPD-VQAVFAQNDEMALGALRAL 226
Cdd:PRK10355 151 LMGGSPVDNNAKLFRAGqmkvlkpyIDSGKIKVVGDQWVDgWLPENALKIMENALTANNNkIDAVVASNDATAGGAIQAL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727170941 227 QT---AGKtdVIVVGFDGTADGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEKVPA 284
Cdd:PRK10355 231 SAqglSGK--VAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKA 289
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
3-240 |
4.52e-12 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 65.52 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 3 MKKLATLASAIALSatLSANAMakDTIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVqDLMV-- 80
Cdd:PRK10703 40 IKELHYSPSAVARS--LKVNHT--KSIGLLATSSEAPYFAEIIEAVEKNCYQKGYTLILCNAWNNLEKQRAYL-SMLAqk 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 81 RAPKLLLI---NPTDSDAVgnaikMANQAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIqlEGI 157
Cdd:PRK10703 115 RVDGLLVMcseYPEPLLAM-----LEEYRHIPMVVMDWGEAKADFTDAIIDNAFEGGYLAGRYLIERGHRDIGVI--PGP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 158 AGTSAARERGEGFKQSLDQNKFKLLAS--QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KT 232
Cdd:PRK10703 188 LERNTGAGRLAGFMKAMEEANIKVPEEwiVQGDFEPESGYEAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGlrvPQ 267
|
....*...
gi 727170941 233 DVIVVGFD 240
Cdd:PRK10703 268 DISVIGYD 275
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
28-227 |
4.51e-11 |
|
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: 61.84 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLI----NPTDSDAVGNAikma 103
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVapstPPDDIYYLCQA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 104 nqAKIPVITLDRVASKGEVVShIASDNRVGGKmagDFIAKKVGADAK-VIQLEGIAGTSAARERGEGFKQSLDQNKFKLL 182
Cdd:cd06274 77 --AGLPVVFLDRPFSGSDAPS-VVSDNRAGAR---ALTEKLLAAGPGeIYFLGGRPELPSTAERIRGFRAALAEAGITEG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 727170941 183 ASQ--PADFDRTKGLNVMQNLLTAHPDV-QAVFAQNDEMALGALRALQ 227
Cdd:cd06274 151 DDWilAEGYDRESGYQLMAELLARLGGLpQALFTSSLTLLEGVLRFLR 198
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
37-240 |
7.58e-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: 380500 [Multi-domain] Cd Length: 275 Bit Score: 61.49 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 37 NNPFFVSMKDGAQQEANKLGYNL--VVLDSQNNPAKELANVQDLMVRApklLLINPTDSDAVgnAIKMANQAKIPVITLD 114
Cdd:cd06277 17 ETPFFSELIDGIEREARKYGYNLliSSVDIGDDFDEILKELTDDQSSG---IILLGTELEEK--QIKLFQDVSIPVVVVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 115 RvASKGEVVSHIASDNRVGGKMAGDFIA----KKVGadakviQLEGIAGTSAARERGEGFKQSLDQNKfklLASQPAD-- 188
Cdd:cd06277 92 N-YFEDLNFDCVVIDNEDGAYEAVKYLVelghTRIG------YLASSYRIKNFEERRRGFRKAMRELG---LSEDPEPef 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727170941 189 ----------FDRTKGLNVMQNLLTAhpdvqaVFAQNDEMALGALRALQTAG---KTDVIVVGFD 240
Cdd:cd06277 162 vvsvgpegayKDMKALLDTGPKLPTA------FFAENDIIALGCIKALQEAGirvPEDVSVIGFD 220
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
28-292 |
2.10e-10 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380656 Cd Length: 296 Bit Score: 60.37 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLD-SQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd20001 1 TIAVVVKVTGIAWFDRMETGVEQFAKDTGVNVYQIGpATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDrvASKGEVVSHI--ASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQNKFKLL-- 182
Cdd:cd20001 81 GIVVITHE--ASNLKNVDYDveAFDNAAYGAFIMDKLAEAMGGKGKYVTFVGSLTSTSHMEWANAAVAYQKANYPDMLlv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 183 -ASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTD-VIVVGFDGTADGVKAVEGGKLAATVAQ 260
Cdd:cd20001 159 tDRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGkIAVVGTGLPSVAGEYLEDGTIDYIQFW 238
|
250 260 270
....*....|....*....|....*....|..
gi 727170941 261 RPDQIGVIGVETADKVLKGEKVpaTIPVDLKL 292
Cdd:cd20001 239 DPADAGYAMNALAVMVLEGEKI--TDGTDLGV 268
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
155-284 |
4.62e-10 |
|
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 57.35 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 155 EGIAGTSAARERGEGFKQSLDQNKFKLLASQ--PADFDRTKGLNVMQNLLTAHPDvqAVFAQNDEMALGALRALQTAGKT 232
Cdd:pfam13377 16 EGDRDDPYSDLRERGFREAARELGLDVEPTLyaGDDEAEAAAARERLRWLGALPT--AVFVANDEVALGVLQALREAGLR 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 727170941 233 ---DVIVVGFDGTADGVKAVEGgklAATVAQRPDQIGVIGVETADKVLKGEKVPA 284
Cdd:pfam13377 94 vpeDLSVIGFDDSPLAALVSPP---LTTVRVDAEELGRAAAELLLDLLNGEPAPP 145
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
43-239 |
2.18e-09 |
|
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: 57.25 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 43 SMKDGAQ---QEANKLGY------NLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAKIPVITL 113
Cdd:COG0683 22 PIKNGAElavEEINAAGGvlgrkiELVVEDDASDPDTAVAAARKLIDQDKVDAIVGPLSSGVALAVAPVAEEAGVPLISP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 114 D------RVASKGEVVSHIASDNRVGGKMAGDFIAKKVGAD-AKVIQLEGIAGTSAArergEGFKQSLDQNKFKLLASQP 186
Cdd:COG0683 102 SatapalTGPECSPYVFRTAPSDAQQAEALADYLAKKLGAKkVALLYDDYAYGQGLA----AAFKAALKAAGGEVVGEEY 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 727170941 187 ADFDRTKGLNVMQNLLTAHPDVqAVFAQNDEMALGALRALQTAGKTDVIVVGF 239
Cdd:COG0683 178 YPPGTTDFSAQLTKIKAAGPDA-VFLAGYGGDAALFIKQAREAGLKGPLNKAF 229
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
28-280 |
1.02e-08 |
|
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380655 Cd Length: 298 Bit Score: 55.34 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLD-SQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd20000 1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGpTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDR-VASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQNKF---KLL 182
Cdd:cd20000 81 GIKVVTFDSdVAPEARDLFVNQADADGIGRAQVDMMAELIGGEGEFAILSATPTATNQNAWIDAMKKELASPEYagmKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 183 ASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDVIVVGFDGTA-DGVKAVEGGKLAATVAQR 261
Cdd:cd20000 161 KVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGKVKVTGLGLPsEMAKYVKDGTVPAFALWN 240
|
250
....*....|....*....
gi 727170941 262 PDQIGVIGVETADKVLKGE 280
Cdd:cd20000 241 PIDLGYLAAYAAAALAQGE 259
|
|
| PBP1_ABC_transporter_LIVBP-like |
cd06268 |
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ... |
28-255 |
7.00e-08 |
|
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: 52.71 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVV--STLNNPFFVSMKDG---AQQEANKLG------YNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAV 96
Cdd:cd06268 1 KIGVVVplTGPYADYGEEILRGvalAVEEINAAGgingrkLELVIADDQGDPETAVAVARKLVDDDKVLAVVGHYSSSVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 97 GNAIKMANQAKIPVITL-----DRVASKGEVVSHIASDNRVGGKMAGDFIAKKvGADAKViqleGIAGTSAARERG--EG 169
Cdd:cd06268 81 LAAAPIYQEAGIPLISPgstapELTEGGGPYVFRTVPSDAMQAAALADYLAKK-LKGKKV----AILYDDYDYGKSlaDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 170 FKQSLDQNKFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALgALRALQTAGKtDVIVVGFDGTADGVKAV 249
Cdd:cd06268 156 FKKALKALGGEIVAEEDFPLGTTDFSAQLTKIKAAGPDVLFLAGYGADAAN-ALKQARELGL-KLPILGGDGLYSPELLK 233
|
....*.
gi 727170941 250 EGGKLA 255
Cdd:cd06268 234 LGGEAA 239
|
|
| PRK15408 |
PRK15408 |
autoinducer 2 ABC transporter substrate-binding protein LsrB; |
3-281 |
1.33e-07 |
|
autoinducer 2 ABC transporter substrate-binding protein LsrB;
Pssm-ID: 237961 Cd Length: 336 Bit Score: 52.11 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 3 MKKLATLASAIALsATLSANAMAKDTIALVVSTLNNPFFVSMKDGAQQEANKLGYNlVVLDSQNNP--AKELANVQDLMV 80
Cdd:PRK15408 1 RKKKIALVSALGI-ALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVD-VTYDGPTEPsvSGQVQLINNFVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 81 RAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRvASKGEVVSHIASDNRVG--GKMAGDFIAKKVGAD-AKVIQLEGI 157
Cdd:PRK15408 79 QGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDS-DTKPECRSYYINQGTPEqlGSMLVEMAAKQVGKDkAKVAFFYSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 158 AGTSAARERGEGFKQSLDQN--KFKLLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKTDVI 235
Cdd:PRK15408 158 PTVTDQNQWVKEAKAKIAKEhpGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRDKVA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 727170941 236 VVGFDGTADGVKAVEGGKLAATVAQRPDQIGVIGVETADKVLKGEK 281
Cdd:PRK15408 238 IVGFSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLKKGK 283
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
28-242 |
1.42e-07 |
|
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: 51.52 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVR-APKLLLINPTDSDAVGNAIKMANqa 106
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKqVDGIIFMGDELTEEIREEFKRSP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 kIPVITLDRVASKGEVVShIASDNRvggKMAGDFIAKKVGADAKVIQL-EGIAGTSAARERGE-GFKQSLDQNKFKLLAS 184
Cdd:cd06298 79 -VPVVLAGTVDSDHEIPS-VNIDYE---QAAYDATKSLIDKGHKKIAFvSGPLKEYINNDKKLqGYKRALEEAGLEFNEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727170941 185 QPADFDRT--KGLNVMQNLLTA-HPDvqAVFAQNDEMALGALRALQTAGK---TDVIVVGFDGT 242
Cdd:cd06298 154 LIFEGDYDydSGYELYEELLESgEPD--AAIVVRDEIAVGLLNAAQDRGLkvpEDLEIIGFDNT 215
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
59-255 |
3.72e-07 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 50.73 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 59 LVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAKIPVITLdrVASKGEVVS----HIASDNRVGG 134
Cdd:pfam13458 45 LVVADDQGDPDVAAAAARRLVDQDGVDAIVGGVSSAVALAVAEVLAKKGVPVIGP--AALTGEKCSpyvfSLGPTYSAQA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 135 KMAGDFIAKKVGAD-AKVIQLEGIAGTSAARergeGFKQSLDQNKFKLLASQPADFDRTKGLNVMQNLLTAHPDVqaVFA 213
Cdd:pfam13458 123 TALGRYLAKELGGKkVALIGADYAFGRALAA----AAKAAAKAAGGEVVGEVRYPLGTTDFSSQVLQIKASGADA--VLL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 727170941 214 QND-EMALGALRALQTAGKTD--VIVVGFDGTADGVKAVEGGKLA 255
Cdd:pfam13458 197 ANAgADTVNLLKQAREAGLDAkgIKLVGLGGDEPDLKALGGDAAE 241
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
28-281 |
3.73e-07 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380657 Cd Length: 295 Bit Score: 50.39 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLD-SQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQA 106
Cdd:cd20002 1 TIVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVGpADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 107 KIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGIAGTSAARERGEGFKQSLDQN--KFKLLAS 184
Cdd:cd20002 81 GIVVITHESPGQKGADWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKypNMKQVTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 185 Q-PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG-KTDVIVVGFDGTADGVKAVEGGKLAATVAQRP 262
Cdd:cd20002 161 RiPGGEDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGlKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDP 240
|
250
....*....|....*....
gi 727170941 263 DQIGVIGVETADKVLKGEK 281
Cdd:cd20002 241 ADAGYAMVYIAKMLLDGKR 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06315 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-260 |
9.73e-07 |
|
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: 49.26 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06315 2 TIAYVASDLRNGGVLGVGRGVKEAAAALGWKVDVLDGGGTVTGRLAALNQALALKPDGIILGGDDAVELQEPLKKAVKAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 108 IPVITLDRVASKG-----EVVSHIASDNRVGGKMAGDFIAKKVGADAKVIQLEGiAGTSAARERGEGFKQSLDQ-NKFKL 181
Cdd:cd06315 82 IPVVGWHAAASPGpipelGLFTNITTDPREVAETAAALVIAQSGGKAGVVIFTD-SRYAIATAKANAMKKAIEAcSGCKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 182 LASQPADFDRTKGL--NVMQNLLTAHPD-VQAVFAQNDEMALGALRALQTAGK--TDVIVVGFDGTADGVKAVEGGKL-A 255
Cdd:cd06315 161 LEYVDIPIADTAQRmpKLIRSLLQRYGDrWTHTLAINDLYFDFAAPALRAAGVeaDPVNISAGDGSPSAYDRIRAGEYqV 240
|
....*
gi 727170941 256 ATVAQ 260
Cdd:cd06315 241 ATVAE 245
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
29-232 |
1.71e-06 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 48.55 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 29 IALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAkI 108
Cdd:PRK10014 67 IGLIVRDLSAPFYAELTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMAEEKG-I 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 109 PVITLDRvASKGEVVSHIASDNRVGGKMAGDFIAKKvgaDAKVIQLEGIAGTSAAR-ERGEGFKQSLDQN--KFKLLASQ 185
Cdd:PRK10014 146 PVVFASR-ASYLDDVDTVRPDNMQAAQLLTEHLIRN---GHQRIAWLGGQSSSLTRaERVGGYCATLLKFglPFHSEWVL 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 727170941 186 PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT 232
Cdd:PRK10014 222 ECTSSQKQAAEAITALLRHNPTISAVVCYNETIAMGAWFGLLRAGRQ 268
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-242 |
2.42e-06 |
|
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: 47.93 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVS---TLNNPFFVSMKDGAQQEANKLGYNLVvldsqnnpakeLANVQDLMVRAPKL-LLINPTDSDAV------- 96
Cdd:cd19974 1 NIAVLIPerfFGDNSFYGKIYQGIEKELSELGYNLV-----------LEIISDEDEEELNLpSIISEEKVDGIiilgeis 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 97 GNAIKMANQAKIPVITLDrvaSKGEVVS--HIASDNRVGGKMAGDFIAKK-------VGAdakviqlegIAGTSAARERG 167
Cdd:cd19974 70 KEYLEKLKELGIPVVLVD---HYDEELNadSVLSDNYYGAYKLTSYLIEKghkkigfVGD---------INYTSSFMDRY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 168 EGFKQSLDQNKfklLASQPADF---DRTKGLNVMQNLLTA----HPDvqAVFAQNDEMALGALRALQTAGKT---DVIVV 237
Cdd:cd19974 138 LGYRKALLEAG---LPPEKEEWlleDRDDGYGLTEEIELPlklmLPT--AFVCANDSIAIQLIKALKEKGYRvpeDISVV 212
|
....*
gi 727170941 238 GFDGT 242
Cdd:cd19974 213 GFDNI 217
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
28-213 |
3.11e-05 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 44.87 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLIN---PTDSDAVgnaIKMAN 104
Cdd:PRK11303 63 SIGLIIPDLENTSYARIAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVStslPPEHPFY---QRLQN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 105 QAkIPVITLDRVASKGEVVShIASDNRVGGKM----AGDFIAKKVGADAKVIQLegiagtSAARERGEGFKQSLDQNKFK 180
Cdd:PRK11303 140 DG-LPIIALDRALDREHFTS-VVSDDQDDAEMlaesLLKFPAESILLLGALPEL------SVSFEREQGFRQALKDDPRE 211
|
170 180 190
....*....|....*....|....*....|...
gi 727170941 181 LLASQPADFDRTKGLNVMQNLLTAHPDVQAVFA 213
Cdd:PRK11303 212 VHYLYANSFEREAGAQLFEKWLETHPMPDALFT 244
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
103-270 |
1.78e-04 |
|
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: 42.19 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 103 ANQAKIPVITLDrVASKGEVVSHIASDNRVGGKMAGDFIakkvgadakviqLE---------GIAGTSAARERGEGFKQS 173
Cdd:cd01543 67 LRRLGIPVVNVS-GSRPEPGFPRVTTDNEAIGRMAAEHL------------LErgfrhfafcGFRNAAWSRERGEGFREA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 174 LDQNKFKLLASQPADFDRTKGLNVMQNLLTA------HPdVqAVFAQNDEMALGALRALQTAGktdvIVVgfdgtadgvk 247
Cdd:cd01543 134 LREAGYECHVYESPPSGSSRSWEEEREELADwlkslpKP-V-GIFACNDDRARQVLEACREAG----IRV---------- 197
|
170 180
....*....|....*....|...
gi 727170941 248 aveggklaatvaqrPDQIGVIGV 270
Cdd:cd01543 198 --------------PEEVAVLGV 206
|
|
| PBP1_ABC_ligand_binding-like |
cd06343 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
58-258 |
2.12e-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: 42.17 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 58 NLVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAKIPVITLDRVASKGEVVSH-----IASDNRV 132
Cdd:cd06343 49 ELIVEDDGYDPARAVAAVRKLVEQDKVFAIVGGLGTPTNLAVRPYLNEAGVPQLFPATGASALSPPPKpytfgVQPSYED 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 133 GGKMAGDFIAKKVGaDAKViqleGIAG--TSAARERGEGFKQSLDQNKFKLLASQP-----ADFDrtkglNVMQNLLTAH 205
Cdd:cd06343 129 EGRILADYIVETLP-AAKV----AVLYqnDDFGKDGLEGLKEALKAYGLEVVAEETyepgdTDFS-----SQVLKLKAAG 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 727170941 206 PDVQAVFAQNDEmALGALRALQTAGKTDVIVVGFDGTADGVKAVEGGKLAATV 258
Cdd:cd06343 199 ADVVVLGTLPKE-AAAALKEAAKLGWKPTFLGSSVSADPTTLAKAGGDAAEGV 250
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
31-288 |
5.49e-04 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 40.66 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 31 LVVSTLNNPFFVSMKDGAQQEANKLGYNL-VVLDSQN---NPAKELANVQDLMVRAPKLLLINPTDS-DAVGNAIKmanq 105
Cdd:COG2984 6 GILQISEHPALDAAREGFKDGLAEAGYGKnLKLDYQNaqgDQATAAQIAAKLVADKPDLIVAIGTPAaQAAANATK---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 106 aKIPVI---TLDRVASKGevvshIASDNRVGGKMAG-----DF-----IAKKVGADAKVIqleGI---AGTSAARERGEG 169
Cdd:COG2984 82 -DIPVVftaVTDPVGAGL-----VKSLEKPGGNVTGvsdllPIekqleLIKKLLPDAKRI---GVlynPSEANSVAQVEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 170 FKQSLDQNKFKLLASQPADFDrtkglNVMQNLLTAHPDVQAVFAQNDEMALGALRAL-QTAGKTDVIVVGFDGTAdgvka 248
Cdd:COG2984 153 LKKAAKKLGLELVEATVTSSN-----EIQQALQSLAGKVDAIYVPTDNTVVSALEAIaKVAARAKIPVFGGDDSS----- 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 727170941 249 VEGGKLAAtVAQRPDQIGVIGVETADKVLKGEKvPATIPV 288
Cdd:COG2984 223 VKAGALAG-YGIDYYELGRQAAEMALRILKGEK-PADIPV 260
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
21-240 |
2.22e-03 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 38.99 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 21 ANAMA-----KDTIALVVSTLNNPFFVSMKDGAQQEANKLGYNLVVLDSQNNPAKELANVQDLMVRAPKLLLINptdSDA 95
Cdd:PRK10401 49 ANAQAlatqvSDTIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVH---SKA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 96 VGNAIKMANQAKIPVITLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKvgADAKVIQLEGIAGTSAARERGEGFKQSLD 175
Cdd:PRK10401 126 LSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDNVSGARMATRMLLNN--GHQRIGYLSSSHGIEDDAMRRAGWMSALK 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 176 QNKFKLLASQPA--DFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVGFD 240
Cdd:PRK10401 204 EQGIIPPESWIGtgTPDMQGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAiplHLSIIGFD 273
|
|
| PBP1_ABC_ligand_binding-like |
cd06335 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
37-112 |
3.67e-03 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport 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 transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally.
Pssm-ID: 380558 [Multi-domain] Cd Length: 348 Bit Score: 38.36 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 37 NNPFFVSMKDGAQ---QEANKLGYN------LVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAK 107
Cdd:cd06335 12 SAELGESARRGVElavEEINAAGGIlgrkieLVERDDEANPTKAVQNAQELIDKEKVVAIIGPTNSGVALATIPILQEAK 91
|
....*
gi 727170941 108 IPVIT 112
Cdd:cd06335 92 IPLII 96
|
|
| PBP1_ABC_unchar_transporter |
cd06325 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems ... |
28-143 |
4.33e-03 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the 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); its ligand specificity has not been determined experimentally.
Pssm-ID: 380548 Cd Length: 282 Bit Score: 37.87 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 28 TIALVVSTlNNPFFVSMKDGAQQEANKLGYNLVVLDSQNnpAKELANVQDLMVRAPKLLLINPTDSDAVGNA---IKMAN 104
Cdd:cd06325 133 RVGVLYNP-GEPNSVAQLEELEAAAKKLGLELVEVPVSS--PADIEQAFASLAGKVADALYVPTDNTVASARpriAALAL 209
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 727170941 105 QAKIPVITLDRV-ASKGEVVShIASDNRVGGKMAGDFIAK 143
Cdd:cd06325 210 KARIPVIYSDREfVEAGALMS-YGPDYYDLGRQAARYVDR 248
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
199-283 |
5.25e-03 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 37.79 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 199 QNLLTAHPDVQAVFAQNDEMALGALRALQTAGKT---DVIVVgfdGTADGVKAVEGGKLAATVAQRPDQIGVIGVETADK 275
Cdd:cd06287 170 AALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSvpeDLMVV---TRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFA 246
|
....*...
gi 727170941 276 VLKGEKVP 283
Cdd:cd06287 247 SLSGEERS 254
|
|
| PBP1_ABC_LivK_ligand_binding-like |
cd06347 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
42-147 |
6.77e-03 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380570 [Multi-domain] Cd Length: 334 Bit Score: 37.52 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727170941 42 VSMKDGAQ---QEANK----LGYN--LVVLDSQNNPAKELANVQDLMVRAPKLLLINPTDSDAVGNAIKMANQAKIPVI- 111
Cdd:cd06347 17 QPALNGAElavDEINAaggiLGKKieLIVYDNKSDPTEAANAAQKLIDEDKVVAIIGPVTSSIALAAAPIAQKAKIPMIt 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 727170941 112 ---TLDRVASKGEVVSHIASDNRVGGKMAGDFIAKKVGA 147
Cdd:cd06347 97 psaTNPLVTKGGDYIFRACFTDPFQGAALAKFAYEELGA 135
|
|
| |
