|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
6-342 |
0e+00 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 601.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 6 LSAKATKITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITDPFYTE 85
Cdd:PRK10014 2 ATAKKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 86 VTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLETLIDSELPVVCAARSYYRDDVDF 165
Cdd:PRK10014 82 LTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMAEEKGIPVVFASRASYLDDVDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 166 IGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERTQRSAADTIAQLLHQH 245
Cdd:PRK10014 162 VRPDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVLECTSSQKQAAEAITALLRHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 246 PKVTAVLCHYPEVALGAIYGVEASGRTVGK---DNYIGQQVALLGFDDVAEAELTSPALTFVSSPAREIGRQAARRLLTR 322
Cdd:PRK10014 242 PTISAVVCYNETIAMGAWFGLLRAGRQSGEsgvDRYFEQQVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRMMQR 321
|
330 340
....*....|....*....|
gi 518276643 323 MLQPELAPNRHIITPNLQKR 342
Cdd:PRK10014 322 ITHEETHSRNLIIPPRLIAR 341
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
8-345 |
1.99e-121 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 352.96 E-value: 1.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 8 AKATKITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITDPFYTEVT 87
Cdd:COG1609 1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 88 AGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAkTLETLIDSELPVVCAARSYYRDDVDFIG 167
Cdd:COG1609 81 RGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDA-RLERLAEAGIPVVLIDRPLPDPGVPSVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 168 PDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERTQRSAADTIAQLLHQHPK 247
Cdd:COG1609 160 VDNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 248 VTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAREIGRQAARRLLTRMLQPE 327
Cdd:COG1609 240 PTAIFCANDLMALGALRALREAGLRVPED------VSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPD 313
|
330
....*....|....*...
gi 518276643 328 LAPNRHIITPNLQKRESA 345
Cdd:COG1609 314 APPERVLLPPELVVREST 331
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
70-343 |
2.04e-102 |
|
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: 302.18 E-value: 2.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLETLIDSEL 149
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTTAELLRRLKAWGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECER 229
Cdd:cd06289 81 PVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVPGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 230 TQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAR 309
Cdd:cd06289 161 TREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRD------IAVVGFDDVPEAALWTPPLTTVSVHPR 234
|
250 260 270
....*....|....*....|....*....|....
gi 518276643 310 EIGRQAARRLLTRMLQPELAPNRHIITPNLQKRE 343
Cdd:cd06289 235 EIGRRAARLLLRRIEGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
70-339 |
3.93e-81 |
|
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: 247.82 E-value: 3.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAaKTLETLIDSEL 149
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDD-ELLEELLAAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECER 229
Cdd:cd06267 80 PVVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 230 TQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAR 309
Cdd:cd06267 160 SEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPED------ISVVGFDDIPLAALLTPPLTTVRQPAY 233
|
250 260 270
....*....|....*....|....*....|
gi 518276643 310 EIGRQAARRLLTRMLQPELAPNRHIITPNL 339
Cdd:cd06267 234 EMGRAAAELLLERIEGEEEPPRRIVLPTEL 263
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
71-345 |
1.62e-62 |
|
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: 200.15 E-value: 1.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLEtLIDSELP 150
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQE-LAARGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 151 VVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERT 230
Cdd:cd06285 81 VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGGFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 231 QRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPARE 310
Cdd:cd06285 161 IEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPED------LSVVGFDDIPLAAFLPPPLTTVRQPKYE 234
|
250 260 270
....*....|....*....|....*....|....*
gi 518276643 311 IGRQAARRLLTRMLQPELAPNRHIITPNLQKRESA 345
Cdd:cd06285 235 MGRRAAELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
74-344 |
1.26e-59 |
|
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: 192.75 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 74 ILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGII-FNPVRGAAakTLETLiDSELPVV 152
Cdd:cd06284 5 LVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVIlLSGRLDAE--LLSEL-SKRYPIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 153 CAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERTQR 232
Cdd:cd06284 82 QCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGDFSFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 233 SAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAREIG 312
Cdd:cd06284 162 AGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPED------VSVIGFDDIEFAEMFSPSLTTIRQPRYEIG 235
|
250 260 270
....*....|....*....|....*....|..
gi 518276643 313 RQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06284 236 ETAAELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
71-339 |
1.62e-59 |
|
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: 192.36 E-value: 1.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKtLETLIDSELP 150
Cdd:cd19977 2 IGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDL-IEKLVKSGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 151 VVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERT 230
Cdd:cd19977 81 VVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEELIKHVDRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 231 QrSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPARE 310
Cdd:cd19977 161 D-DVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDD------IALIGFDDIPWADLFNPPLTVIAQPTYE 233
|
250 260 270
....*....|....*....|....*....|
gi 518276643 311 IGRQAARRLLTRMLQPELAPNRHII-TPNL 339
Cdd:cd19977 234 IGRKAAELLLDRIENKPKGPPRQIVlPTEL 263
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
71-344 |
3.57e-59 |
|
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: 191.72 E-value: 3.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVrGAAAKTLETLIDSELP 150
Cdd:cd06299 2 IGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPT-GENSEGLQALIAQGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 151 VVCAARSY-YRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECER 229
Cdd:cd06299 81 VVFVDREVeGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 230 TQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAR 309
Cdd:cd06299 161 RQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDD------VSLISFDDVPWFELLSPPLTVIAQPVE 234
|
250 260 270
....*....|....*....|....*....|....*
gi 518276643 310 EIGRQAARRLLTRMLQPElAPNRHIITPNLQKRES 344
Cdd:cd06299 235 RIGRRAVELLLALIENGG-RATSIRVPTELIPRES 268
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
70-344 |
5.97e-59 |
|
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: 190.92 E-value: 5.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLETLIDSEL 149
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECER 229
Cdd:cd19976 81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 230 TQRSAAdTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAR 309
Cdd:cd19976 161 SLEGGY-KAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKIPED------LSVIGFDNIILSEYITPALTTIAQPIF 233
|
250 260 270
....*....|....*....|....*....|....*
gi 518276643 310 EIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd19976 234 EMGQEAAKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
70-339 |
1.39e-57 |
|
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: 187.47 E-value: 1.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKtLETLIDSEL 149
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRE-LKRLLKHGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECER 229
Cdd:cd06280 80 PIVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 230 TQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyIGQQVALLGFDDVAEAELTSPALTFVSSPAR 309
Cdd:cd06280 160 TIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLE------IPQDISVVGFDDSDWFEIVDPPLTVVAQPAY 233
|
250 260 270
....*....|....*....|....*....|
gi 518276643 310 EIGRQAARRLLTRMLQPELAPNRHIITPNL 339
Cdd:cd06280 234 EIGRIAAQLLLERIEGQGEEPRRIVLPTEL 263
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
70-345 |
4.46e-57 |
|
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: 186.32 E-value: 4.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLIL----RDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTlETLI 145
Cdd:cd06292 1 LIGYVVpelpGGFSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDDPRV-RYLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 146 DSELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVL 225
Cdd:cd06292 80 EAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 226 ECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVS 305
Cdd:cd06292 160 EGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRD------VSVVGFDDSPLAAFTHPPLTTVR 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 518276643 306 SPAREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRESA 345
Cdd:cd06292 234 QPIDEIGRAVVDLLLAAIEGNPSEPREILLQPELVVRESS 273
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
70-343 |
2.56e-56 |
|
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: 184.26 E-value: 2.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPvRGAAAKTLETLIDSEL 149
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHS-RALSDEELILIAEKIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECER 229
Cdd:cd06270 80 PLVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 230 TQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAR 309
Cdd:cd06270 160 TIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPED------VSVIGFDDVPLARYLSPKLTTVHYPIE 233
|
250 260 270
....*....|....*....|....*....|....
gi 518276643 310 EIGRQAARRLLTRMLQPELAPNrHIITPNLQKRE 343
Cdd:cd06270 234 EMAQAAAELALNLAYGEPLPIS-HEFTPTLIERD 266
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
70-344 |
8.67e-56 |
|
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: 182.75 E-value: 8.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDI-TDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFnpVRGAAAKTLETLIDSE 148
Cdd:cd06288 1 TIGLITDDIaTTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIY--ASMHHREVTLPPELTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVCAarsYYRDD---VDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVL 225
Cdd:cd06288 79 IPLVLL---NCFDDdpsLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 226 ECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVS 305
Cdd:cd06288 156 HGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPED------LSVVGFDNQELAAYLRPPLTTVA 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 518276643 306 SPAREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06288 230 LPYYEMGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
70-344 |
1.77e-54 |
|
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: 179.67 E-value: 1.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIF--NPVRgaaAKTLETLIDS 147
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFasGTLT---EENKQLLKNM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 148 ELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLT-RAERIGGYCASLLQYGLPFKPEWVLE 226
Cdd:cd19975 78 NIPVVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNaGYPRYEGYKKALKDAGLPIKENLIVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 227 CERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSS 306
Cdd:cd19975 158 GDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPED------ISVIGFDNTEIAEMSIPPLTTVSQ 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 518276643 307 PAREIGRQAARRLLtRMLQPELAPNRHIITP-NLQKRES 344
Cdd:cd19975 232 PFYEMGKKAVELLL-DLIKNEKKEEKSIVLPhQIIERES 269
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
71-344 |
2.95e-52 |
|
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: 173.60 E-value: 2.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFnpVRGAAAKTLETLIDS--E 148
Cdd:cd06275 2 IGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLL--MCSEMTDDDAELLAAlrS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECE 228
Cdd:cd06275 80 IPVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 229 RTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPA 308
Cdd:cd06275 160 FEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQD------ISIIGYDDIELARYFSPALTTIHQPK 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 518276643 309 REIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06275 234 DELGELAVELLLDRIENKREEPQSIVLEPELIERES 269
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
70-344 |
4.00e-52 |
|
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: 173.45 E-value: 4.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHS-LSRQgVAGIIFNPVRGAAAkTLETLIDSE 148
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRAlLSRR-PAGLILTGTEHTPA-TRKLLRAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVcAARSYYRDDVDF-IGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRA-ERIGGYCASLLQYGLPFKPEWVLE 226
Cdd:cd01575 79 IPVV-ETWDLPDDPIDMaVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSRArQRLEGFRDALAEAGLPLPLVLLVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 227 CERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYgvEASGRtvGKDnyIGQQVALLGFDDVAEAELTSPALTFVSS 306
Cdd:cd01575 158 LPSSFALGREALAELLARHPDLDAIFCSNDDLALGALF--ECQRR--GIR--VPGDIAIAGFGDLDIAAALPPALTTVRV 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 518276643 307 PAREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd01575 232 PRYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
71-344 |
1.75e-51 |
|
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: 171.64 E-value: 1.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFnpVRGAAAKTLETLIDSELP 150
Cdd:cd06290 2 IGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIV--VGGFGDEELLKLLAEGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 151 VVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERT 230
Cdd:cd06290 80 VVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 231 QRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVgkdnyiGQQVALLGFDDVAEAELTSPALTFVSSPARE 310
Cdd:cd06290 160 EESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRV------PDDVSVIGFDDLPFSKYTTPPLTTVRQPLYE 233
|
250 260 270
....*....|....*....|....*....|....
gi 518276643 311 IGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06290 234 MGKTAAEILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-344 |
9.16e-50 |
|
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: 167.45 E-value: 9.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVrGAAAKTLETLIDSEL 149
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPS-DDDLSHLARLRARGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPfKPEWVLECER 229
Cdd:cd06293 80 AVVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLD-PDEVVRELSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 230 TQRSAA---DTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSS 306
Cdd:cd06293 159 PDANAElgrAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDD------VSVVGYDDLPFAAAANPPLTTVRQ 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 518276643 307 PAREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06293 233 PSYELGRAAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
70-344 |
2.59e-49 |
|
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: 165.77 E-value: 2.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLtqC--GHSPERLQQSIHSLSRQGVAGIIFnpvrGAAAKTLETLIDS 147
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMIL--CnsNEDEEKEKEYLEMLKRNKVDGIIL----GSHSLDIEEYKKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 148 ELPVVCAARsYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLEC 227
Cdd:cd06291 75 NIPIVSIDR-YLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDEN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 228 ERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSP 307
Cdd:cd06291 154 DFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPED------VQIIGFDGIEISELLYPELTTIRQP 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 518276643 308 AREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06291 228 IEEMAKEAVELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
15-345 |
1.72e-48 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 165.64 E-value: 1.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 15 DVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITDPFYTEVTAGVSEVL 94
Cdd:PRK10423 3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 95 EQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFnpvrgaaaKTLETLIDSE--------LPVVCAARSYYRDDVDFI 166
Cdd:PRK10423 83 FERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLL--------LCTETHQPSReimqrypsVPTVMMDWAPFDGDSDLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 167 GPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERTQRSAADTIAQLLHQHP 246
Cdd:PRK10423 155 QDNSLLGGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 247 KVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAREIGRQAARRLLTRMLQP 326
Cdd:PRK10423 235 RPQAVFTGNDAMAVGVYQALYQAGLSVPQD------IAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQP 308
|
330
....*....|....*....
gi 518276643 327 ELAPNRHIITPNLQKRESA 345
Cdd:PRK10423 309 TLQQQRLQLTPELMERGSV 327
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
71-344 |
3.05e-48 |
|
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: 163.45 E-value: 3.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIfnpVRGA--AAKTLETLIDSE 148
Cdd:cd06273 2 IGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLI---LVGSdhDPELFELLEQRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVCAarSYYRDDVDF--IGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRA-ERIGGYCASLLQYGLPFKPEWVL 225
Cdd:cd06273 79 VPYVLT--WSYDEDSPHpsIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRArARLAGIRDALAERGLELPEERVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 226 ECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGkdnyigQQVALLGFDDVAEAELTSPALTFVS 305
Cdd:cd06273 157 EAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVP------EDLSITGFDDLELAAHLSPPLTTVR 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 518276643 306 SPAREIGRQAARRLLtRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06273 231 VPAREIGELAARYLL-ALLEGGPPPKSVELETELIVRES 268
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
71-339 |
4.67e-47 |
|
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: 160.41 E-value: 4.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILR----DITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFN-PVRGAAakTLETLI 145
Cdd:cd20010 2 IGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILArTRVNDP--RIAYLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 146 DSELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVL 225
Cdd:cd20010 80 ERGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPALVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 226 ECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAE-AELTSPALTFV 304
Cdd:cd20010 160 EGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKD------VSVIGHDDLLPaLEYFSPPLTTT 233
|
250 260 270
....*....|....*....|....*....|....*
gi 518276643 305 SSPAREIGRQAARRLLTRMLQPELAPNRHIITPNL 339
Cdd:cd20010 234 RSSLRDAGRRLAEMLLALIDGEPAAELQELWPPEL 268
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
10-344 |
1.67e-46 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 161.05 E-value: 1.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 10 ATkITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITDPFYTEVTAG 89
Cdd:PRK10703 2 AT-IKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 90 VSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFnpvrgAAAKTLETLID-----SELPVVC----AARSYYR 160
Cdd:PRK10703 81 VEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLV-----MCSEYPEPLLAmleeyRHIPMVVmdwgEAKADFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 161 DDVDfigpDNT-HAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERTQRSAADTIA 239
Cdd:PRK10703 156 DAII----DNAfEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 240 QLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAREIGRQAARRL 319
Cdd:PRK10703 232 QILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQD------ISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNML 305
|
330 340
....*....|....*....|....*
gi 518276643 320 LTRMLQPELAPNRHIITPNLQKRES 344
Cdd:PRK10703 306 LDRIVNKREEPQTIEVHPRLVERRS 330
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
70-342 |
4.29e-46 |
|
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: 157.71 E-value: 4.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVrGAAAKTLETLIDSEL 149
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPT-GNNNDAYLELAQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSL-TRAERIGGYCASLLQYGLPFKPEWVlECE 228
Cdd:cd06283 80 PVVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGIsTRRERLQGFLDALARYNIEGDVYVI-EIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 229 RTQRSAADtIAQLLHQHPKV-TAVLCHYPEVALGAIYGVEASGRTvgkdnyIGQQVALLGFDDVAEAELTSPALTFVSSP 307
Cdd:cd06283 159 DTEDLQQA-LAAFLSQHDGGkTAIFAANGVVLLRVLRALKALGIR------IPDDVGLCGFDDWDWADLIGPGITTIRQP 231
|
250 260 270
....*....|....*....|....*....|....*
gi 518276643 308 AREIGRQAARRLLTRMLQPELAPNRHIITPNLQKR 342
Cdd:cd06283 232 TYEIGKAAAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-344 |
3.93e-45 |
|
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: 155.00 E-value: 3.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGY--LLFLTQCGHSPERlqqSIHSLSRQGVAGIIfnpVRGAA--AKTLETLI 145
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLrpLLFNVDDEDDVDD---ALRQLLQYRVDGVI---VTSATlsSELAEECA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 146 DSELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPfkPEWVL 225
Cdd:cd06278 75 RRGIPVVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLP--PPAVE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 226 ECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVgkdnyIGQQVALLGFDDVAEAELTSPALTFVS 305
Cdd:cd06278 153 AGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGLV-----VPEDISVVGFDDIPMAAWPSYDLTTVR 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 518276643 306 SPAREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06278 228 QPIEEMAEAAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
71-343 |
4.97e-45 |
|
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: 155.36 E-value: 4.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLETLIDSELP 150
Cdd:pfam00532 4 LGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKAEGYGIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 151 VVCAARSYYRDD-VDFIGPDNTHAAKQATTYLIEQGH-RHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECE 228
Cdd:pfam00532 84 VIAADDAFDNPDgVPCVMPDDTQAGYESTQYLIAEGHkRPIAVMAGPASALTARERVQGFMAALAAAGREVKIYHVATGD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 229 RTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGK---DNYIGQQVALLGFDDVAEAELTSPALTFVS 305
Cdd:pfam00532 164 NDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRVKIPdivGIGINSVVGFDGLSKAQDTGLYLSPLTVIQ 243
|
250 260 270
....*....|....*....|....*....|....*...
gi 518276643 306 SPAREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRE 343
Cdd:pfam00532 244 LPRQLLGIKASDMVYQWIPKFREHPRVLLIPRDFFKET 281
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
71-344 |
1.28e-44 |
|
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: 153.93 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLETLIDSELP 150
Cdd:cd06281 2 VGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDPELAAALARLDIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 151 VVCAARSyYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERT 230
Cdd:cd06281 82 VVLIDRD-LPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGSFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 231 QRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPARE 310
Cdd:cd06281 161 ADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGD------LSVVSIGDSDLAELHDPPITAIRWDLDA 234
|
250 260 270
....*....|....*....|....*....|....*
gi 518276643 311 IGRQAARRLLTRM-LQPELAPNRHIITPNLQKRES 344
Cdd:cd06281 235 VGRAAAELLLDRIeGPPAGPPRRIVVPTELILRDS 269
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
70-344 |
1.36e-44 |
|
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: 153.87 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQC-GHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLETLIDSE 148
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVEPCdSDDEDLADRLRRFLSRSRPDGVILTPPLSDDPALLDALDELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECE 228
Cdd:cd01545 81 IPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPDLVVQGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 229 RTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYgvEASGRTVGkdnyIGQQVALLGFDDVAEAELTSPALTFVSSPA 308
Cdd:cd01545 161 FTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLA--AAHRLGLR----VPDDLSVAGFDDSPIARLVWPPLTTVRQPI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 518276643 309 REIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd01545 235 AEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
6-331 |
1.34e-42 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 150.53 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 6 LSAKATKITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITDPFYTE 85
Cdd:PRK09526 1 MKSKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 86 VTAGVSEVLEQQGYLLFLTQCG-HSPERLQQSIHSLSRQGVAGIIFN-PVRGAAAKTLETLIDSeLPVVCAARSYYrDDV 163
Cdd:PRK09526 81 IAAAIKSRADQLGYSVVISMVErSGVEACQAAVNELLAQRVSGVIINvPLEDADAEKIVADCAD-VPCLFLDVSPQ-SPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 164 DFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLpfKPEWVLECERTQRSAADTIAQLLH 243
Cdd:PRK09526 159 NSVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQL--QPIAVREGDWSAMSGYQQTLQMLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 244 QHPKVTAVLCHYPEVALGAIYGVEASGRTVgkdnyiGQQVALLGFDDVAEAELTSPALTFVSSPAREIGRQAARRLLTRM 323
Cdd:PRK09526 237 EGPVPSAILVANDQMALGVLRALHESGLRV------PGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALS 310
|
....*...
gi 518276643 324 LQPELAPN 331
Cdd:PRK09526 311 QGQAVKGS 318
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
70-344 |
3.37e-42 |
|
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: 147.70 E-value: 3.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKT----LETLI 145
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSALPNPnldlYEELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 146 DSELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVgGRADSLTRAERIGGYCASLLQYGLPFKPEWVL 225
Cdd:cd01541 81 KKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGI-FKSDDLQGVERYQGFIKALREAGLPIDDDRIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 226 EC---ERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALT 302
Cdd:cd01541 160 WYsteDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPED------LSVVGFDDSYLASLSEPPLT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518276643 303 FVSSPAREIGRQAARRLLtRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd01541 234 SVVHPKEELGRKAAELLL-RMIEEGRKPESVIFPPELIERES 274
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
70-344 |
3.45e-42 |
|
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: 147.34 E-value: 3.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGH-SPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLEtLIDSE 148
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDEdDPASVREALDRLLSQRVDGIIVIAPDEAVLEALR-RLPPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVcAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPfkPEWVLECE 228
Cdd:cd01574 80 LPVV-IVGSGPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLP--PPPVVEGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 229 RTQRSAADTIAQLLHQHPkVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPA 308
Cdd:cd01574 157 WSAASGYRAGRRLLDDGP-VTAVFAANDQMALGALRALHERGLRVPED------VSVVGFDDIPEAAYFVPPLTTVRQDF 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 518276643 309 REIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd01574 230 AELGRRAVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
71-344 |
5.67e-41 |
|
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: 144.23 E-value: 5.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDI---TDPFYTEVTAGVSEVLEQQGYLLFLtqCGHSPERLQQSI--HSLSRQGVAGIIfnpVRGAAAKT-LETL 144
Cdd:cd19974 2 IAVLIPERffgDNSFYGKIYQGIEKELSELGYNLVL--EIISDEDEEELNlpSIISEEKVDGII---ILGEISKEyLEKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 145 IDSELPVVCAArSYYRD-DVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLP-FKPE 222
Cdd:cd19974 77 KELGIPVVLVD-HYDEElNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVGDINYTSSFMDRYLGYRKALLEAGLPpEKEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 223 WVLECERTQRSAADTIAQLLHQHpKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALT 302
Cdd:cd19974 156 WLLEDRDDGYGLTEEIELPLKLM-LPTAFVCANDSIAIQLIKALKEKGYRVPED------ISVVGFDNIELAELSTPPLT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518276643 303 FVSSPAREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd19974 229 TVEVDKEAMGRRAVEQLLWRIENPDRPFEKILVSGKLIERDS 270
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
36-345 |
4.63e-40 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 143.21 E-value: 4.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 36 RISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQ 115
Cdd:PRK11041 3 KVSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 116 SIHSLSRQGVAGII-------FNpVRGAAAKTLETLI-------DSELPVVcaarsyyrddvdFIgpDNTHAAKQATTYL 181
Cdd:PRK11041 83 FVNLIITKQIDGMLllgsrlpFD-ASKEEQRNLPPMVmanefapELELPTV------------HI--DNLTAAFEAVNYL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 182 IEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALG 261
Cdd:PRK11041 148 HELGHKRIACIAGPEEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 262 AIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAREIGRQAARRLLTRMLQPELAPNRHIITPNLQK 341
Cdd:PRK11041 228 ALSQAKRMGLRVPQD------LSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELII 301
|
....
gi 518276643 342 RESA 345
Cdd:PRK11041 302 RGST 305
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
71-335 |
1.16e-39 |
|
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: 140.80 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITD-----PFYTEVTAGVSEVLEQQGYLLFLTqCGHSPERLQQSIHSLSRQG-VAGIIF------NPVrgaaa 138
Cdd:cd06294 2 IGLVLPSSAEelfqnPFFSEVLRGISQVANENGYSLLLA-TGNTEEELLEEVKRMVRGRrVDGFILlyskedDPL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 139 ktLETLIDSELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLP 218
Cdd:cd06294 76 --IEYLKEEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 219 FKPEWVLECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTS 298
Cdd:cd06294 154 LDDDYILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPED------VSIISFNNSPLAELAS 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 518276643 299 PALTFVSSPAREIGRQAARRLLTRMLQPELAPNRHII 335
Cdd:cd06294 228 PPLTSVDINPYELGREAAKLLINLLEGPESLPKNVIV 264
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
71-344 |
1.43e-37 |
|
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: 135.34 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLIL-----RDITDPFYTEVTAGVSEVLEQQGY-LLFLtqcghspERLQQSIHSLSRQgVAGII----FNPvrgaaaKT 140
Cdd:cd01544 2 IGIIQwyseeEELEDPYYLSIRLGIEKEAKKLGYeIKTI-------FRDDEDLESLLEK-VDGIIaigkFSK------EE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 141 LETLIDSELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAE-----RIGGYCASLLQY 215
Cdd:cd01544 68 IEKLKKLNPNIVFVDSNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGEeiedpRLRAFREYMKEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 216 GLpFKPEWVLECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAE 295
Cdd:cd01544 148 GL-YNEEYIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPED------ISIISFNDIEVAK 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 518276643 296 LTSPALTFVSSPAREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd01544 221 YVTPPLTTVHIPTEEMGRTAVRLLLERINGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
70-344 |
1.45e-37 |
|
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: 135.48 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRgAAAKTLETLIDSEL 149
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSD-PTSRQLRLLRSAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVC--AARSYYRDDVDfIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLEC 227
Cdd:cd06296 80 PFVLidPVGEPDPDLPS-VGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 228 ERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyIGQQVALLGFDDVAEAELTSPALTFVSSP 307
Cdd:cd06296 159 DFTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLR------VPDDLSVIGFDDTPPARWTSPPLTTVHQP 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 518276643 308 AREIGRQAArRLLTRMLQPELAPNRHIITP-NLQKRES 344
Cdd:cd06296 233 LREMGAVAV-RLLLRLLEGGPPDARRIELAtELVVRGS 269
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
71-344 |
5.54e-37 |
|
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: 134.26 E-value: 5.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRD-----ITDPFYTEVTAGVSEVLEQQGY-LLFLTqcGHSPERLQQSIHSLSrqgVAGIIFNPVRgAAAKTLETL 144
Cdd:cd06279 2 IGVLLPDdlsyaFSDPVAAQFLRGVAEVCEEEGLgLLLLP--ATDEGSAAAAVRNAA---VDGFIVYGLS-DDDPAVAAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 145 IDSELPVV---CAARsyyrDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGR-----------------ADSLTRAER 204
Cdd:cd06279 76 RRRGLPLVvvdGPAP----PGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRldrgrergpvsaerlaaATNSVARER 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 205 IGGYCASLLQYGLPFKPEWVLEC-ERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGkdnyigQQV 283
Cdd:cd06279 152 LAGYRDALEEAGLDLDDVPVVEApGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVP------EDL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518276643 284 ALLGFDDVAEAELTSPALTFVSSPAREIGRQAARRLLTRMlqpELAPNRHIITP-NLQKRES 344
Cdd:cd06279 226 SVTGFDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLL---PGAPPRPVILPtELVVRAS 284
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
11-344 |
6.43e-37 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 135.67 E-value: 6.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 11 TKITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITDPFYTEVTAGV 90
Cdd:PRK10401 2 ITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 91 SEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNpVRGAAAKTLETLIDSELPVVCAARSYYRDDVDFIGPDN 170
Cdd:PRK10401 82 DLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVH-SKALSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 171 THAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERTQRSAADTIAQLLHQHPKVTA 250
Cdd:PRK10401 161 VSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLQLTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 251 VLCHYPEVALGAIygveasgrTVGKDNYIG--QQVALLGFDDVAEAELTSPALTFVSSP-------AREIGRQAARRLLT 321
Cdd:PRK10401 241 VFAYNDNMAAGAL--------TALKDNGIAipLHLSIIGFDDIPIARYTDPQLTTVRYPiasmaklATELALQGAAGNLD 312
|
330 340
....*....|....*....|...
gi 518276643 322 RMlqpelapNRHIITPNLQKRES 344
Cdd:PRK10401 313 PR-------ASHCFMPTLVRRHS 328
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
70-335 |
3.15e-36 |
|
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: 131.46 E-value: 3.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVrGAAAKTLETLIDSEL 149
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFAT-EITDEHRKALKKLKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYyrDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVG-GRADSLTRAERIGGYCASLLQYGLPfkPEWVLECE 228
Cdd:cd01542 80 PVVVLGQEH--EGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGvDEEDIAVGVARKQGYLDALKEHGID--EVEIVETD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 229 RTQRSAADTIAQLLhQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPA 308
Cdd:cd01542 156 FSMESGYEAAKELL-KENKPDAIICATDNIALGAIKALRELGIKIPED------ISVAGFGGYDLSEFVSPSLTTVKFDY 228
|
250 260
....*....|....*....|....*..
gi 518276643 309 REIGRQAArRLLTRMLQPELAPNRHII 335
Cdd:cd01542 229 EEAGEKAA-ELLLDMIEGEKVPKKQKL 254
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
13-330 |
5.01e-36 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 133.23 E-value: 5.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 13 ITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITDPFYTEVTAGVSE 92
Cdd:PRK14987 8 LQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 93 VLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPvRGAAAKTLETLIDSELPVVCAARSYYRDDVDFIGPDNTH 172
Cdd:PRK14987 88 VTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTE-RTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAVGFDNFE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 173 AAKQATTYLIEQGHRHIAYVGGRADSLTRAERiGGYCASLLQYGL-PFKPewVLECERTQRSAADTIAQLLHQHPKVTAV 251
Cdd:PRK14987 167 AARQMTTAIIARGHRHIAYLGARLDERTIIKQ-KGYEQAMLDAGLvPYSV--MVEQSSSYSSGIELIRQARREYPQLDGV 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518276643 252 LCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAREIGRQAARRLLTRMLQPELAP 330
Cdd:PRK14987 244 FCTNDDLAVGAAFECQRLGLKVPDD------MAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTP 316
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
13-344 |
1.01e-35 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 132.57 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 13 ITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITDPFYTEVTAGVSE 92
Cdd:PRK10727 4 IKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVEQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 93 VLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNpvrgaaAKTLEtliDSELP--------VVCAARSYYRDDVD 164
Cdd:PRK10727 84 VAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVH------AKMIP---DAELAslmkqipgMVLINRILPGFENR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 165 FIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERTQRSAADTIAQLLHQ 244
Cdd:PRK10727 155 CIALDDRYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 245 HPKVTAVLCHYPEVALGAIygveasgrTVGKDNYIG--QQVALLGFDDVAEAELTSPALTFVSSPAREIGRQAARRLLTR 322
Cdd:PRK10727 235 GRNFTAVACYNDSMAAGAM--------GVLNDNGIDvpGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALAL 306
|
330 340
....*....|....*....|..
gi 518276643 323 MLQPELAPNRHIITPNLQKRES 344
Cdd:PRK10727 307 ADNRPLPEITNVFSPTLVRRHS 328
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
66-344 |
9.64e-32 |
|
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: 120.05 E-value: 9.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 66 QQSNLVGLIL-------RDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPerlQQSIHSLSRQGVAGIIfnpVRGAAA 138
Cdd:cd06295 1 QRSRTIAVVVpmdphgdQSITDPFFLELLGGISEALTDRGYDMLLSTQDEDA---NQLARLLDSGRADGLI---VLGQGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 139 KT--LETLIDSELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTrAERIGGYCASLLQYG 216
Cdd:cd06295 75 DHdaLRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEV-ADRLQGYRDALAEAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 217 LPFKPEWVLECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAEL 296
Cdd:cd06295 154 LEADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGD------VAVVGYDDIPLAAY 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 518276643 297 TSPALTFVSSPAREIGRQAARRLLT----RMLQPELAPNRHIItpnlqkRES 344
Cdd:cd06295 228 FRPPLTTVRQDLALAGRLLVEKLLAliagEPVTSSMLPVELVV------RES 273
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-332 |
4.43e-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: 380505 [Multi-domain] Cd Length: 267 Bit Score: 118.15 E-value: 4.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLETLIDSEL 149
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSEALELLEEEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGR-ADSLTRAERIGGYCASLLQYGLpfKPEWVLECE 228
Cdd:cd06282 81 PYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDfSASDRARLRYQGYRDALKEAGL--KPIPIVEVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 229 RTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPA 308
Cdd:cd06282 159 FPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDD------VSVIGFDGIAIGELLTPTLATVVQPS 232
|
250 260
....*....|....*....|....
gi 518276643 309 REIGRQAARRLLTRMLQPELAPNR 332
Cdd:cd06282 233 RDMGRAAADLLLAEIEGESPPTSI 256
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
71-344 |
9.41e-31 |
|
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: 117.39 E-value: 9.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIF--NPVrgaAAKTLETLIDSE 148
Cdd:cd06298 2 VGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFmgDEL---TEEIREEFKRSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGG-RADSLTRAERIGGYCASLLQYGLPFKPEWVLEC 227
Cdd:cd06298 79 VPVVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGpLKEYINNDKKLQGYKRALEEAGLEFNEPLIFEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 228 ERTQRSAADtIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSP 307
Cdd:cd06298 159 DYDYDSGYE-LYEELLESGEPDAAIVVRDEIAVGLLNAAQDRGLKVPED------LEIIGFDNTRYATMSRPQLTSINQP 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 518276643 308 AREIGrQAARRLLTRMLQPELAPNRHIITP-NLQKRES 344
Cdd:cd06298 232 LYDIG-AVAMRLLTKLMNKEEVEETIVKLPhSIIWRQS 268
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
80-344 |
2.61e-30 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 116.18 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 80 DPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIhSLSRQGVAGIIfnpVRGA--AAKTLETLIDSELPVVcAARS 157
Cdd:cd06277 18 TPFFSELIDGIEREARKYGYNLLISSVDIGDDFDEILK-ELTDDQSSGII---LLGTelEEKQIKLFQDVSIPVV-VVDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 158 YYRD-DVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERTQRSAAD 236
Cdd:cd06277 93 YFEDlNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEPEFVVSVGPEGAYK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 237 TIAQLLHQHPKV-TAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAREIGRQA 315
Cdd:cd06277 173 DMKALLDTGPKLpTAFFAENDIIALGCIKALQEAGIRVPED------VSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLA 246
|
250 260
....*....|....*....|....*....
gi 518276643 316 ARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06277 247 VRRLIEKIKDPDGGTLKILVSTKLVERGS 275
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
11-80 |
1.25e-29 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 108.44 E-value: 1.25e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 11 TKITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITD 80
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
71-342 |
5.48e-29 |
|
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: 112.25 E-value: 5.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFnpvrGAAAKTLETLID--SE 148
Cdd:cd06286 2 IGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLII----TSRENDWEVIEPyaKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVCAARsYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRA--DSLTRAERIGGYCASLLQYGLPFKPEWVLE 226
Cdd:cd06286 78 GPIVLCEE-TDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGRPesSSASTQARLKAYQDVLGEHGLSLREEWIFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 227 CERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELtsPALTFVSS 306
Cdd:cd06286 157 NCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPED------LAVIGFDNQPISEL--LNLTTIDQ 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 518276643 307 PAREIGRQAARRLLTRMLQPElaPNRHIITPNLQKR 342
Cdd:cd06286 229 PLEEMGKEAFELLLSQLESKE--PTKKELPSKLIER 262
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
70-344 |
6.42e-29 |
|
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: 112.56 E-value: 6.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGY--LLFLTQCGHSPERLQQSiHSLSRQgVAGIIFNPVRGAAAKTlETLIDS 147
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYdlAIFPLLSEYRLEKYLRN-STLAYQ-CDGLVMASLDLTELFE-EVIVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 148 ELPVVCAARsyYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTR----AERIGGYCASLLQYGLPFKPEW 223
Cdd:cd06297 78 EKPVVLIDA--NSMGYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTetvfREREQGFLEALNKAGRPISSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 224 VLECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAEltSPALTF 303
Cdd:cd06297 156 MFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGED------VAVIGFDGQPWAA--SPGLTT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 518276643 304 VSSPAREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06297 228 VRQPVEEMGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
180-344 |
8.70e-28 |
|
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: 106.27 E-value: 8.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 180 YLIEQGHRHIAYVG--GRADSLTRAERIGGYCASLLQYGLPFKPEWVLECERTQRSAADtiAQLLHQHPKVTAVLCHYPE 257
Cdd:pfam13377 1 HLAELGHRRIALIGpeGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAAR--ERLRWLGALPTAVFVANDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 258 VALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPAREIGRQAARRLLTRMLQPELAPNRHIITP 337
Cdd:pfam13377 79 VALGVLQALREAGLRVPED------LSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPP 152
|
....*..
gi 518276643 338 NLQKRES 344
Cdd:pfam13377 153 ELVERES 159
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
12-252 |
7.87e-27 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 108.04 E-value: 7.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 12 KITDVAQRAGVSVTTVSMVLNGKG---RISPATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLILRDITDPFYtevtA 88
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVINGKAkqyRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSY----A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 89 GVSEVLEQQ----GYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLETLIDSELPVVCAARSYYRDDVD 164
Cdd:PRK11303 78 RIAKYLERQarqrGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTSLPPEHPFYQRLQNDGLPIIALDRALDREHFT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 165 FIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKpewVLECERTQR-SAADTIAQLLH 243
Cdd:PRK11303 158 SVVSDDQDDAEMLAESLLKFPAESILLLGALPELSVSFEREQGFRQALKDDPREVH---YLYANSFEReAGAQLFEKWLE 234
|
....*....
gi 518276643 244 QHPKVTAVL 252
Cdd:PRK11303 235 THPMPDALF 243
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
70-322 |
3.24e-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: 102.32 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLETLIDSEL 149
Cdd:cd01537 1 RIGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQNV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDD-VDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVLECE 228
Cdd:cd01537 81 PVVFFDKEPSRYDkAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 229 RTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFVSSPA 308
Cdd:cd01537 161 WDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSD------ISVFGYDALPEALKSGPLLTTILQDA 234
|
250
....*....|....
gi 518276643 309 REIGRQAARRLLTR 322
Cdd:cd01537 235 NNLGKTTFDLLLNL 248
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
58-337 |
6.74e-23 |
|
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: 96.92 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 58 SAAANLRSQQSNLVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAA 137
Cdd:COG1879 23 AAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 138 AKT-LETLIDSELPVVCAARSYYRDDVD-FIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLL 213
Cdd:COG1879 103 LAPaLKKAKAAGIPVVTVDSDVDGSDRVaYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPAANERTDGFKEALK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 214 QYglpfkPEW----VLECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigQQVALLGFD 289
Cdd:COG1879 183 EY-----PGIkvvaEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRK--------GDVKVVGFD 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 518276643 290 DVAEA--ELTSPALTF-VSSPAREIGRQAArRLLTRMLQPELAPnRHIITP 337
Cdd:COG1879 250 GSPEAlqAIKDGTIDAtVAQDPYLQGYLAV-DAALKLLKGKEVP-KEILTP 298
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
15-65 |
2.12e-22 |
|
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.
Pssm-ID: 143331 [Multi-domain] Cd Length: 52 Bit Score: 88.62 E-value: 2.12e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 518276643 15 DVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPNSAAANLRS 65
Cdd:cd01392 2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
108-344 |
2.40e-21 |
|
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: 91.88 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 108 HSPERLQQSIHSLSRQGVAGIIfnpVRGAAAKTLETLIDSELPVVCAarSYYRDDVDF--IGPDNTHAAKQATTYLIEQG 185
Cdd:cd01543 34 LEPPGYEELLDLLKGWKGDGII---ARLDDPELAEALRRLGIPVVNV--SGSRPEPGFprVTTDNEAIGRMAAEHLLERG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 186 HRHIAYVG--------GRADSLTRAERIGGYCASLLQYGLPFKPEWVlecERTQRSAADTIAQLlhqhPKVTAVLCHYPE 257
Cdd:cd01543 109 FRHFAFCGfrnaawsrERGEGFREALREAGYECHVYESPPSGSSRSW---EEEREELADWLKSL----PKPVGIFACNDD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 258 VALGAIYGVEASGRTVgkdnyiGQQVALLGFD-DVAEAELTSPALTFVSSPAREIGRQAArRLLTRMLQPELAPNRHIIT 336
Cdd:cd01543 182 RARQVLEACREAGIRV------PEEVAVLGVDnDELICELSSPPLSSIALDAEQIGYEAA-ELLDRLMRGERVPPEPILI 254
|
250
....*....|
gi 518276643 337 P--NLQKRES 344
Cdd:cd01543 255 PplGVVTRQS 264
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
71-339 |
1.78e-20 |
|
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380664 [Multi-domain] Cd Length: 266 Bit Score: 89.52 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLIL--RDITDPFYTEVTAGVSEVLEQQGYLLFLTqcghsPERLQQ----SIHSLSRQGVA-GIIFN---P----VRga 136
Cdd:cd20009 2 IALVLptEDEIDGFTSQLISGISEALRGTPYHLVVT-----PEFPGDdplePVRYIVENRLAdGIIIShtePqdprVR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 137 aaktleTLIDSELPVVCAARSYYRDD---VDFigpDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLL 213
Cdd:cd20009 75 ------YLLERGFPFVTHGRTELSTPhayFDF---DNEAFAYEAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 214 QYGLPFKPEWVLECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAE 293
Cdd:cd20009 146 EAGLEVEPLLIVTLDSSAEAIRAAARRLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRD------VDVVAKETSPI 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 518276643 294 AELTSPALTFVSSPAREIGRQAARRLLTRMLQPELAPNRHIITPNL 339
Cdd:cd20009 220 LDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAEPLQTLERPEL 265
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
71-294 |
5.34e-20 |
|
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: 88.01 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKT-LETLIDSEL 149
Cdd:cd01536 2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPaVKKANAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCA-ARSYYRDDVD-FIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLLQYGlpfKPEWVL 225
Cdd:cd01536 82 PVVAVdTDIDGGGDVVaFVGTDNYEAGKLAGEYLAEAlgGKGKVAILEGPPGSSTAIDRTKGFKEALKKYP---DIEIVA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518276643 226 E----CERTQrsAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigQQVALLGFDDVAEA 294
Cdd:cd01536 159 EqpanWDRAK--ALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRT--------GDIKIVGVDGTPEA 221
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
82-339 |
1.15e-19 |
|
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380495 [Multi-domain] Cd Length: 264 Bit Score: 87.10 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 82 FYTEVTAGVSEVLEQQGYLLFLTQcgHSPERLQQSIHSLSRQGVA-GIIFNPVRGAAAKtLETLIDSELPVVCAARSYYR 160
Cdd:cd06271 16 TVSE*VSGITEEAGTTGYHLLVWP--FEEAES*VPIRDLVETGSAdGVILSEIEPNDPR-VQFLTKQNFPFVAHGRSD*P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 161 DDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLpfkPEWVLECERTQRSAADTIAQ 240
Cdd:cd06271 93 IGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGL---TGYPLDADTTLEAGRAAAQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 241 LLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAE-AELTSPALTFVSSPAREIGRQAARRL 319
Cdd:cd06271 170 LLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGED------VSIIGKDSAPFlGAMITPPLTTVHAPIAEAGRELAKAL 243
|
250 260
....*....|....*....|
gi 518276643 320 LTRMLQPELAPNRHIITPNL 339
Cdd:cd06271 244 LARIDGEDPETLQVLVQPSL 263
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
12-57 |
2.96e-17 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 74.21 E-value: 2.96e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 518276643 12 KITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIKELDYVPN 57
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
70-340 |
7.28e-17 |
|
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: 79.17 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYtevtAGVSEVLEQQ----GYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRgAAAKTLETLI 145
Cdd:cd06274 1 TIGLIVPDLANRFF----ARLAEALERLarerGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPST-PPDDIYYLCQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 146 DSELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWVL 225
Cdd:cd06274 76 AAGLPVVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 226 ECERTQRSAADTIAQLLHQH---PKvtAVLCHypevALGAIYGV-EASGRTVGKdnyIGQQVALLGFDDVAEAELTSPAL 301
Cdd:cd06274 156 AEGYDRESGYQLMAELLARLgglPQ--ALFTS----SLTLLEGVlRFLRERLGA---IPSDLVLGTFDDHPLLDFLPNPV 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 518276643 302 TFVSSPAREIGRQAARRLLTRMlQPELAPNRHIITPNLQ 340
Cdd:cd06274 227 DSVRQDHDEIAEHAFELLDALI-EGQPEPGVIIIPPELI 264
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
71-294 |
8.12e-15 |
|
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: 73.79 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPV-RGAAAKTLETLIDSEL 149
Cdd:cd06309 2 VGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIdATGWDPVLKEAKDAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYyrDDVD------FIGPDNTHAAKQATTYLIEQ---GHRHIAYVGGRADSLTRAERIGGYCASLLQYglpfk 220
Cdd:cd06309 82 PVILVDRTI--DGEDgslyvtFIGSDFVEEGRRAAEWLVKNykgGKGNVVELQGTAGSSVAIDRSKGFREVIKKH----- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518276643 221 PEWVLECERT---QRSAADTIAQ-LLHQHP-KVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEA 294
Cdd:cd06309 155 PNIKIVASQSgnfTREKGQKVMEnLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLKPGKD------VLVVGIDGQKDA 227
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
77-316 |
3.59e-12 |
|
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: 65.68 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 77 DITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKT-LETLIDSELPVVCAA 155
Cdd:cd19971 8 TMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPaLEAAKEAGIPVINVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 156 RSYYRDD-VD-FIGPDNTHAAKQATTYLIEQ---GHRhIAYVggrADSLTRA--ERIGGYCASlLQYGLPFKPEWVLECE 228
Cdd:cd19971 88 TPVKDTDlVDsTIASDNYNAGKLCGEDMVKKlpeGAK-IAVL---DHPTAEScvDRIDGFLDA-IKKNPKFEVVAQQDGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 229 rTQRSAADTIAQ-LLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigQQVALLGFD--DVAEAELTSPALTFVS 305
Cdd:cd19971 163 -GQLEVAMPIMEdILQAHPDLDAVFALNDPSALGALAALKAAGKL--------GDILVYGVDgsPDAKAAIKDGKMTATA 233
|
250
....*....|...
gi 518276643 306 --SPArEIGRQAA 316
Cdd:cd19971 234 aqSPI-EIGKKAV 245
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
82-344 |
5.28e-12 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 65.13 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 82 FYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQqsihSLSRQGVagIIFNPVRGAAAktLETLIDSELPVVCAAR-SYYR 160
Cdd:cd06287 21 FMMEVAAAAAEEALEHDLALVLVPPLHHVSMLD----ALDVDGA--IVVEPTVEDPI--LARLRQRGVPVVSIGRaPGTD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 161 DDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGG--RADSLTRAERIggYCASLLQYGLPfkpEWVLECERTQ--RSAAD 236
Cdd:cd06287 93 EPVPYVDLQSAATARLLLEHLHGAGARQVALLTGssRRNSSLESEAA--YLRFAQEYGTT---PVVYKVPESEgeRAGYE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 237 TIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKD-----NYIGQQvallgfddvaeAELTSPALTFVSSPAREI 311
Cdd:cd06287 168 AAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDlmvvtRYDGIR-----------ARTADPPLTAVDLHLDRV 236
|
250 260 270
....*....|....*....|....*....|...
gi 518276643 312 GRQAArRLLTRMLQPELAPNRHIITPNLQKRES 344
Cdd:cd06287 237 ARTAI-DLLFASLSGEERSVEVGPAPELVVRAS 268
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
71-294 |
6.70e-12 |
|
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: 65.01 E-value: 6.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKT-LETLIDSEL 149
Cdd:cd06323 2 IGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPaVEEANEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDV-DFIGPDNTHAAKQATTYLIE--QGHRHIAYVGGRADSLTRAERIGGYCASLLQY-GLPFKPEWVL 225
Cdd:cd06323 82 PVITVDRSVTGGKVvSHIASDNVAGGEMAAEYIAKklGGKGKVVELQGIPGTSAARERGKGFHNAIAKYpKINVVASQTA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518276643 226 ECERTQrsAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigqQVALLGFDDVAEA 294
Cdd:cd06323 162 DFDRTK--GLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRK---------DVIVVGFDGTPDA 219
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
71-325 |
2.30e-11 |
|
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: 63.10 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGY-LLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRG-AAAKTLETLIDSE 148
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGeVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPtALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVC---AARSYYRDdvDFIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYcASLLQYGLPfKPEW 223
Cdd:pfam13407 81 IPVVTfdsDAPSSPRL--AYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGF-KKVLKEKYP-GIKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 224 VLECERTQRSAADT---IAQLLHQHP-KVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigQQVALLGFDDVAEA--ELT 297
Cdd:pfam13407 157 VAEVEGTNWDPEKAqqqMEALLTAYPnPLDGIISPNDGMAGGAAQALEAAGLA--------GKVVVTGFDATPEAleAIK 228
|
250 260
....*....|....*....|....*....
gi 518276643 298 SPALTF-VSSPAREIGRQAArRLLTRMLQ 325
Cdd:pfam13407 229 DGTIDAtVLQDPYGQGYAAV-ELAAALLK 256
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
75-320 |
1.36e-10 |
|
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: 61.13 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 75 LRDITDPFYTEVTAGVSEVLEQQGY-LLFLTQCGHSPERLQQSiHSLSRQGVAGIIFNP-------VRGAAAKTLETLID 146
Cdd:cd01391 9 LHQIREQFGIQRVEAIFHTADKLGAsVEIRDSCWHGSVALEQS-IEFIRDNIAGVIGPGsssvaivIQNLAQLFDIPQLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 147 SELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAeRIGGYCASLLQYGLPFKPEWVLE 226
Cdd:cd01391 88 LDATSQDLSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNSGEL-RMAGFKELAKQEGICIVASDKAD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 227 CERTQrSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigQQVALLGFDDVAEA-----ELTSPAL 301
Cdd:cd01391 167 WNAGE-KGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLV--------GDVSVIGSDGWADRdevgyEVEANGL 237
|
250
....*....|....*....
gi 518276643 302 TFVSSPAREIGRQAARRLL 320
Cdd:cd01391 238 TTIKQQKMGFGITAIKAMA 256
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
109-321 |
1.89e-10 |
|
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: 60.64 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 109 SPERLQQSIHSLSRQGVAGIIFNPVRGAA-AKTLETLIDSELPVVCAARSYYRDDVD-FIGPDNTHAAKQATTYLIEQ-- 184
Cdd:cd06308 41 DAAKQIADIEDLIAQGVDLLIVSPNEADAlTPVVKKAYDAGIPVIVLDRKVSGDDYTaFIGADNVEIGRQAGEYIAELln 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 185 GHRHIAYVGGRADSLTRAERIGGYCASLLQYglpfkPEWVL----ECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVAL 260
Cdd:cd06308 121 GKGNVVEIQGLPGSSPAIDRHKGFLEAIAKY-----PGIKIvasqDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMAL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518276643 261 GAIYGVEASGRT-----VGKDnyiGQQVAllGFDDVAEAELTSpalTFVSSPAREIGRQAARRLLT 321
Cdd:cd06308 196 GAYQALKKAGREkeikiIGVD---GLPEA--GEKAVKDGILAA---TFLYPTGGKEAIEAALKILN 253
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
71-294 |
1.65e-09 |
|
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: 57.76 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAKTLETLIDSE-L 149
Cdd:cd06319 2 IGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAkI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCA---ARSyyRDDVDFIGPDNTHAAKQATTYLIEQ------GHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFK 220
Cdd:cd06319 82 PVVIAdigTGG--GDYVSYIISDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518276643 221 PEwVLECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigQQVALLGFDDVAEA 294
Cdd:cd06319 160 AL-RQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--------GDILVVGFDGDPEA 224
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
71-292 |
1.99e-09 |
|
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: 57.45 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRG-AAAKTLETLIDSEL 149
Cdd:cd19972 2 IGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGAtAAAVPVKAARAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVD-FIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLLQYglpfkPEWVLE 226
Cdd:cd19972 82 PVIAVDRNPEDAPGDtFIATDSVAAAKELGEWVIKQtgGKGEIAILHGQLGTTPEVDRTKGFQEALAEA-----PGIKVV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518276643 227 CERTQRSAAD---TIAQ-LLHQHPKVTAVLCHYPEVALGAIYGVEASGrtvgkdnyIGQQVALLGFD-DVA 292
Cdd:cd19972 157 AEQTADWDQDegfKVAQdMLQANPNITVFFGQSDAMALGAAQAVKVAG--------LDHKIWVVGFDgDVA 219
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
15-342 |
2.58e-09 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 57.85 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 15 DVAQRAGVSVTTVSMVLNGKGRIS--PATAERVQQAIKELDYVPNSAAANLRSQQSNLVGLIL------RDITDPFYTEV 86
Cdd:PRK10339 6 DIAIEAGVSLATVSRVLNDDPTLNvkEETKHRILEIAEKLEYKTSSARKLQTGAVNQHHILAIysyqqeLEINDPYYLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 87 TAGVSEVLEQQGylLFLTQCGHSPErlqqsihSLSRQGVAGIIF----NPVRGAAAKTLETlidselPVVCAARSYYRDD 162
Cdd:PRK10339 86 RHGIETQCEKLG--IELTNCYEHSG-------LPDIKNVTGILIvgkpTPALRAAASALTD------NICFIDFHEPGSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 163 VDFIGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYcaslLQYGL---PFKPEWVLECERTQRSAADTIA 239
Cdd:PRK10339 151 YDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIREVAF----AEYGRlkqVVREEDIWRGGFSSSSGYELAK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 240 QLLHQ--HPKvtAVLCHYPEVALGAIYGVEASGRTvgkdnyIGQQVALLGFDDVAEAELTSPALTFVSSPAREIGRQAAR 317
Cdd:PRK10339 227 QMLARedYPK--ALFVASDSIAIGVLRAIHERGLN------IPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVN 298
|
330 340
....*....|....*....|....*
gi 518276643 318 RLLTRMLQPELAPNRHIITPNLQKR 342
Cdd:PRK10339 299 LLYEKARDGRALPLLVFVPSKLKLR 323
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
70-343 |
3.08e-09 |
|
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380496 [Multi-domain] Cd Length: 266 Bit Score: 57.00 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFY-TEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIfnpVRGAAAKTLETLIDSE 148
Cdd:cd06272 1 TIGLYWPSVGERVAlTRLLSGINEAISKQGYNINLSICPYKVGHLCTAKGLFSENRFDGVI---VFGISDSDIEYLNKNK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 L--PVVcaarSYYRDDVDF--IGPDNTHAAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWV 224
Cdd:cd06272 78 PkiPIV----LYNRESPKYstVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTLRGKGFIETCEKHGIHLSDSII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 225 LECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVGKDnyigqqVALLGFDDVAEAELTSPALTFV 304
Cdd:cd06272 154 DSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPED------ISIVSYDNIPQEARSDPPLTVV 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 518276643 305 SSPAREIGRQAARRLLTRMLQPELAPNRHIITPNLQKRE 343
Cdd:cd06272 228 GVPIEKIAEESLRLILKLIEGRENEIQQLILYPELIFRE 266
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
71-294 |
6.39e-09 |
|
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: 56.10 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIH---SLSRQGVAGIIFNP----------VRGAA 137
Cdd:cd19970 2 VALVMKSLANEFFIEMEKGARKHAKEANGYELLVKGIKQETDIEQQIAiveNLIAQKVDAIVIAPadskalvpvlKKAVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 138 AKTLETLIDSEL-PVVCAARSYyrdDVDFIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLLQ 214
Cdd:cd19970 82 AGIAVINIDNRLdADALKEGGI---NVPFVGPDNRQGAYLAGDYLAKKlgKGGKVAIIEGIPGADNAQQRKAGFLKAFEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 215 YGLPF----KPEWvlECERtqrsAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigQQVALLGFDD 290
Cdd:cd19970 159 AGMKIvasqSANW--EIDE----ANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKA--------GKVLVVGFDN 224
|
....
gi 518276643 291 VAEA 294
Cdd:cd19970 225 IPAV 228
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
71-294 |
2.57e-08 |
|
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: 54.20 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAA-AKTLETLIDSEL 149
Cdd:cd06313 2 IGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADAlAPAVEKAKEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVD-FIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLLQYglpfkPEWVLE 226
Cdd:cd06313 82 PLVGVNALIENEDLTaYVGSDDVVAGELEGQAVADRlgGKGNVVILEGPIGQSAQIDRGKGIENVLKKY-----PDIKVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518276643 227 CERT---QRSAADTIAQ-LLHQHP-KVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigqQVALLGFDDVAEA 294
Cdd:cd06313 157 AEQTanwSRDEAMSLMEnWLQAYGdEIDGIIAQNDDMALGALQAVKAAGRD---------DIPVVGIDGIEDA 220
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
71-315 |
2.60e-08 |
|
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: 54.22 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLE--QQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAA-AKTLETLIDS 147
Cdd:cd06321 2 IGVTVQDLGNPFFVAMVRGAEEAAAeiNPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGiEPAIKRAKDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 148 ELPVVC---AARSyyrddVD-FIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRaERIGGYCASLLQYglpfkP 221
Cdd:cd06321 82 GIIVVAvdvAAEG-----ADaTVTTDNVQAGYLACEYLVEQlgGKGKVAIIDGPPVSAVI-DRVNGCKEALAEY-----P 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 222 EWVL----ECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigqQVALLGFDDVAEA--E 295
Cdd:cd06321 151 GIKLvddqNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRD---------DIVITSVDGSPEAvaA 221
|
250 260
....*....|....*....|...
gi 518276643 296 LTSPALTFVSSPA---REIGRQA 315
Cdd:cd06321 222 LKREGSPFIATAAqdpYDMARKA 244
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
71-331 |
3.27e-08 |
|
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: 53.82 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPV-RGAAAKTLETLIDSEL 149
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVdSGGIVPAIEAANEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVV-CAARSYYRDDVDFIGPDNTHAAKQATTYLIEQ---GHRHIAYVGGRADSLTRaERIGGYCASLLQYGlPFKPEWVL 225
Cdd:cd06322 82 PVFtVDVKADGAKVVTHVGTDNYAGGKLAGEYALKAllgGGGKIAIIDYPEVESVV-LRVNGFKEAIKKYP-NIEIVAEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 226 ECeRTQRSAADTIAQ-LLHQHPKVTAVLCHYPEVALGAIYGVEASGRtvgkdnyiGQQVALLGFDDVAEA-ELTSPALTF 303
Cdd:cd06322 160 PG-DGRREEALAATEdMLQANPDLDGIFAIGDPAALGALTAIESAGK--------EDKIKVIGFDGNPEAiKAIAKGGKI 230
|
250 260 270
....*....|....*....|....*....|.
gi 518276643 304 VSSPARE---IGRQAARRLLTRMLQPELAPN 331
Cdd:cd06322 231 KADIAQQpdkIGQETVEAIVKYLAGETVEKE 261
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
71-337 |
3.34e-08 |
|
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: 54.19 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFlTQCGHSPERLQ---QSIHSLSRQGVAGIIFNPVRG--------AAAK 139
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVD-VQAAPSETDTQgqlNLLETMLNKGYDAILVSPISDtnlippieKANK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 140 TLETLIDSELPVVCAARSYYRDDVD-FIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLLQYG 216
Cdd:cd06320 81 KGIPVINLDDAVDADALKKAGGKVTsFIGTDNVAAGALAAEYIAEKlpGGGKVAIIEGLPGNAAAEARTKGFKETFKKAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 217 lPFKPEWVLECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigQQVALLGFDDVAEA-- 294
Cdd:cd06320 161 -GLKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKT--------GKVLVVGTDGIPEAkk 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 518276643 295 -----ELTSpalTFVSSPArEIGRQAARRLLtRMLQPELAPnRHIITP 337
Cdd:cd06320 232 sikagELTA---TVAQYPY-LEGAMAVEAAL-RLLQGQKVP-AVVATP 273
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
70-316 |
3.82e-08 |
|
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: 53.87 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRG-AAAKTLETLIDSE 148
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADAdASIAAVKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVCAARSYYRDDVDF--IGPDNTHAAKQATTYLIEQGHRHIAYV-----GGRADSLTRAErigGYCASLLQYglpfkP 221
Cdd:cd19967 81 IPVFLIDREINAEGVAVaqIVSDNYQGAVLLAQYFVKLMGEKGLYVellgkESDTNAQLRSQ---GFHSVIDQY-----P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 222 EWVLECER----TQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigQQVALLGFD---DVAEA 294
Cdd:cd19967 153 ELKMVAQQsadwDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRA--------GDVIIVGFDgsnDVRDA 224
|
250 260
....*....|....*....|..
gi 518276643 295 ELTSPALTFVSSPAREIGRQAA 316
Cdd:cd19967 225 IKEGKISATVLQPAKLIARLAV 246
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
70-274 |
5.06e-07 |
|
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: 50.31 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVS-EVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPV-RGAAAKTLETLIDS 147
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEaYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVdTDASAPAVDAAADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 148 ELPVVCAARSY--YRDDVDFIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLLQYglpfkPEW 223
Cdd:cd06301 82 GIPLVYVNREPdsKPKGVAFVGSDDIESGELQMEYLAKLlgGKGNIAILDGVLGHEAQILRTEGNKDVLAKY-----PGM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518276643 224 VLECERT---QRSAADTIAQ-LLHQHPKVTAVLCHYPEVALGAIYGVEASGRTVG 274
Cdd:cd06301 157 KIVAEQTanwSREKAMDIVEnWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDD 211
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
121-294 |
1.29e-06 |
|
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: 49.52 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 121 SRQGVAGIIFNPVRGAAAKTLE--------------TLIDSELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQGH 186
Cdd:cd06324 55 RPPKPDYLILVNEKGVAPELLElaeqakipvflinnDLTDEERALLGKPREKFKYWLGSIVPDNEQAGYLLAKALIKAAR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 187 RH--------IAYVGGRADSLTRaERIGG--------YCASLLQ--YGlpfkpEWvlecertQRSAADTIAQLLHQ-HPK 247
Cdd:cd06324 135 KKsddgkirvLAISGDKSTPASI-LREQGlrdalaehPDVTLLQivYA-----NW-------SEDEAYQKTEKLLQrYPD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518276643 248 VTAVLCHYPEVALGAIYGVEASGRTVGKDNYIGqqvallGFDDVAEA 294
Cdd:cd06324 202 IDIVWAANDAMALGAIDALEEAGLKPGKDVLVG------GIDWSPEA 242
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
71-320 |
2.99e-06 |
|
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: 48.11 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGY-LLFLTQCGHSPERLQQS-IHSLSRQGVAGIIFNPVRGAAAK-TLETLIDS 147
Cdd:cd06310 2 IGVVLKGTTSAFWRTVREGAEAAAKDLGVkIIFVGPESEEDVAGQNSlLEELINKKPDAIVVAPLDSEDLVdPLKDAKDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 148 ELPVVCAARSYYRDDVD-FIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWV 224
Cdd:cd06310 82 GIPVIVIDSGIKGDAYLsYIATDNYAAGRLAAQKLAEAlgGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIKVLAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 225 LECERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVeasgrtvgKDNYIGQQVALLGFDDVAEAE--LTSPALT 302
Cdd:cd06310 162 QYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAI--------KSRKLSGQIKIVGFDSQEELLdaLKNGKID 233
|
250 260
....*....|....*....|
gi 518276643 303 F--VSSPArEIGRQAARRLL 320
Cdd:cd06310 234 AlvVQNPY-EIGYEGIKLAL 252
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
80-293 |
3.84e-06 |
|
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: 47.58 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 80 DPFYTEVTAGVSEVLEQQGY-LLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAA-AKTLETLIDSELPVVC---- 153
Cdd:cd06314 11 NPFWDLAEAGAEKAAKELGVnVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAvTPVINKAADKGIPVITfdsd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 154 ---AARSYYrddvdfIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLLQYglpFKPEWV--LE 226
Cdd:cd06314 91 apdSKRLAY------IGTDNYEAGREAGELMKKAlpGGGKVAIITGGLGADNLNERIQGFKDALKGS---PGIEIVdpLS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518276643 227 CERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRtVGKdnyigqqVALLGFDDVAE 293
Cdd:cd06314 162 DNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGK-VGK-------VKIVGFDTLPE 220
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
123-339 |
1.06e-05 |
|
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: 46.23 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 123 QGVAGIIFNPVR-GAAAKTLETLIDSELPVVCAARSYYRDD-VDFIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADS 198
Cdd:cd19968 54 QGVDGIIVSPIDvKALVPAIEAAIKAGIPVVTVDRRAEGAApVPHVGADNVAGGREVAKFVVDKlpNGAKVIELTGTPGS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 199 LTRAERIGGycaslLQYGLPFKPEWVLECERT---QRSAADTIAQ-LLHQHP-KVTAVLCHYPEVALGAIYGVEASGRTV 273
Cdd:cd19968 134 SPAIDRTKG-----FHEELAAGPKIKVVFEQTgnfERDEGLTVMEnILTSLPgPPDAIICANDDMALGAIEAMRAAGLDL 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518276643 274 GKdnyigqqVALLGFDDVAEA-------ELtspALTFVSSPAREIGrqAARRLLTRMLQPELAPNRHIITPNL 339
Cdd:cd19968 209 KK-------VKVIGFDAVPDAlqaikdgEL---YATVEQPPGGQAR--TALRILVDYLKDKKAPKKVNLKPKL 269
|
|
| VapI |
COG3093 |
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense ... |
12-48 |
2.71e-05 |
|
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms];
Pssm-ID: 442327 [Multi-domain] Cd Length: 87 Bit Score: 42.10 E-value: 2.71e-05
10 20 30
....*....|....*....|....*....|....*..
gi 518276643 12 KITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQA 48
Cdd:COG3093 24 SQTELAKALGVSRQRISEILNGKRAITADTALRLARA 60
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
71-294 |
2.89e-05 |
|
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: 45.09 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAA-AKTLETLIDSEL 149
Cdd:cd06318 2 IGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGlTPAVKAAKAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDD--VDFIGPDNTH---AAKQATTYLIEQGHRHIAYVGGRADSLTRAERIGGYCASLLQYGLPFKPEWV 224
Cdd:cd06318 82 PVITVDSALDPSAnvATQVGRDNKQngvLVGKEAAKALGGDPGKIIELSGDKGNEVSRDRRDGFLAGVNEYQLRKYGKSN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518276643 225 LE------CERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigQQVALLGFDDVAEA 294
Cdd:cd06318 162 IKvvaqpyGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGML--------DKVKVAGADGQKEA 229
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
58-289 |
6.41e-05 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 43.92 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 58 SAAANLRSQQSNLVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRG-A 136
Cdd:PRK10653 16 SATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSdA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 137 AAKTLETLIDSELPVVCAARSYYRDDV-DFIGPDNTHAAKQATTYLIEQ---GHRHIAYVGGRADSLTRaERIGGYCASL 212
Cdd:PRK10653 96 VGNAVKMANQANIPVITLDRGATKGEVvSHIASDNVAGGKMAGDFIAKKlgeGAKVIQLEGIAGTSAAR-ERGEGFKQAV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518276643 213 LQYGLPFKPEWVLECERTQrsAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvgkdnyigqQVALLGFD 289
Cdd:PRK10653 175 AAHKFNVLASQPADFDRTK--GLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKS---------DVMVVGFD 240
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
144-289 |
3.50e-04 |
|
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: 41.81 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 144 LIDSELPVvcaarsyyrDDVD-FIGPDNTHAAKQATTYLIEQGHR--HIAYVGGRADSLTRAERIGGycasLLQYGLPFK 220
Cdd:cd20006 89 TIDSPVNS---------KKADsFVATDNYEAGKKAGEKLASLLGEkgKVAIVSFVKGSSTAIEREEG----FKQALAEYP 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518276643 221 PEWVLE---CERTQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRtvgkdnyiGQQVALLGFD 289
Cdd:cd20006 156 NIKIVEteyCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGL--------GGKVKVVGFD 219
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
123-289 |
8.54e-04 |
|
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: 40.68 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 123 QGVAGIIFNPVRGAAAKTLETLIDSELPVVCAARSYYRDDVD-FIGPDNTHAAKQATTYLIEQ------GHRHIAYVGGR 195
Cdd:cd20008 56 RKPDAIVLAPNDTAALVPAVEAADAGIPVVLVDSGANTDDYDaFLATDNVAAGALAADELAELlkasggGKGKVAIISFQ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 196 ADSLTRAERIGGYCASLLQYglpfKPEwvLECERTQRSAADT-----IAQ-LLHQHPKVTAVLCHYPEVALGAIYGVEAS 269
Cdd:cd20008 136 AGSQTLVDREEGFRDYIKEK----YPD--IEIVDVQYSDGDIakalnQTTdLLTANPDLVGIFGANNPSAVGVAQALAEA 209
|
170 180
....*....|....*....|
gi 518276643 270 GRtvgkdnyiGQQVALLGFD 289
Cdd:cd20008 210 GK--------AGKIVLVGFD 221
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
71-339 |
8.80e-04 |
|
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: 40.62 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGY----LLFLTQCGHSPERLQQSIHSLSRqGVAGIIFNP-----VRGAaaktL 141
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRDrrvrLRIHFVDSLDPEALAAALRRLAA-GCDGVALVApdhplVRAA----I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 142 ETLIDSELPVVC-------AARSYYrddvdfIGPDNtHAAKQATTYLIEQGHRH----IAYVGGRADSLTRAERIGGYCA 210
Cdd:cd06307 77 DELAARGIPVVTlvsdlpgSRRLAY------VGIDN-RAAGRTAAWLMGRFLGRrpgkVLVILGSHRFRGHEEREAGFRS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 211 SLLQYGLPFKPEWVLECERTQRSAADTIAQLLHQHPKVTAVlchYpeVALGAIYGV----EASGRTvgkdnyigQQVALL 286
Cdd:cd06307 150 VLRERFPDLTVLEVLEGLDDDELAYELLRELLARHPDLVGI---Y--NAGGGNEGIaralREAGRA--------RRVVFI 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 518276643 287 GFD--DVAEAELTSPALTFV-SSPAREIGRQAARRLLTRMLQPELAPNRHIITPNL 339
Cdd:cd06307 217 GHEltPETRRLLRDGTIDAViDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEI 272
|
|
| HTH_XRE |
smart00530 |
Helix-turn-helix XRE-family like proteins; |
12-45 |
1.03e-03 |
|
Helix-turn-helix XRE-family like proteins;
Pssm-ID: 197775 [Multi-domain] Cd Length: 56 Bit Score: 36.73 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|....
gi 518276643 12 KITDVAQRAGVSVTTVSMVLNGKGRISPATAERV 45
Cdd:smart00530 12 TQEELAEKLGVSRSTLSRIENGKRKPSLETLKKL 45
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
109-271 |
1.65e-03 |
|
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: 39.60 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 109 SPERLQQsIHSLSRQGVAGIIFNPVRGAAAK-TLETLIDSELPVVCAARSYYRDDVDFIGPDNTHAAKQATTYLIEQ--G 185
Cdd:cd19999 46 ATGQISQ-IRNMINEGVDAILIDPVSATALNpVIEKAQAAGILVVSFDQPVSSPDAINVVIDQYKWAAIQAQWLAEQlgG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 186 HRHIAYVGGRADSLTRAERIGGYCASLLQYglpfkPEW-VL---ECERTQRSAADTIAQLLHQHPKVTAVLCHyPEVALG 261
Cdd:cd19999 125 KGNIVAINGVAGNPANEARVKAADDVFAKY-----PGIkVLasvPGGWDQATAQQVMATLLATYPDIDGVLTQ-DGMAEG 198
|
170
....*....|
gi 518276643 262 AIYGVEASGR 271
Cdd:cd19999 199 VLRAFQAAGK 208
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
71-289 |
2.03e-03 |
|
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: 39.52 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTqcghSPERL------QQSIHSLSRQGVAGIIFNPV-RGAAAKTLET 143
Cdd:cd20004 2 IAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWR----GPSREddveaqIQIIEYFIDQGVDGIVLAPLdRKALVAPVER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 144 LIDSELPVVCAARSYYRDDVD-FIGPDNTHAAKQATTYLIE--QGHRHIAYVGGRADSLTRAERIGGYcASLLQYGLPFk 220
Cdd:cd20004 78 ARAQGIPVVIIDSDLGGDAVIsFVATDNYAAGRLAAKRMAKllNGKGKVALLRLAKGSASTTDRERGF-LEALKKLAPG- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518276643 221 pEWVLECER---TQRSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRtvgkdnyiGQQVALLGFD 289
Cdd:cd20004 156 -LKVVDDQYaggTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGL--------AGKVKFIGFD 218
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
71-339 |
2.28e-03 |
|
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: 39.20 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAA-AKTLETLIDSEL 149
Cdd:cd06305 2 IAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADAlDPKLKKALDAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAarsyyrdDVDFIGP-------DNTHAAKQATTYLIEQ--GHRHIAYVGGradsltraeriGGY--CAS---LLQY 215
Cdd:cd06305 82 PVVTF-------DTDSQVPgvnnitqDDYALGTLSLGQLVKDlnGEGNIAVFNV-----------FGVppLDKrydIYKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 216 GLPFKP--EWVLECER--TQRSAADT---IAQLLHQHPK--VTAVLCHYPEVALGAIYGVEASGRTvgkdnyigqQVALL 286
Cdd:cd06305 144 VLKANPgiKKIVAELGdvTPNTAADAqtqVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRT---------DIKVY 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518276643 287 GFD----DVAE-AELTSPaltFVSSPA---REIGRQAArRLLTRMLQPELAPNRHIITPNL 339
Cdd:cd06305 215 GVDisnqDLELmADEGSP---WVATAAqdpALIGTVAV-RNVARKLAGEDLPDKYSLVPVL 271
|
|
| HTH_XRE |
cd00093 |
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ... |
12-49 |
3.24e-03 |
|
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.
Pssm-ID: 238045 [Multi-domain] Cd Length: 58 Bit Score: 35.22 E-value: 3.24e-03
10 20 30
....*....|....*....|....*....|....*...
gi 518276643 12 KITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAI 49
Cdd:cd00093 14 TQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKAL 51
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
70-316 |
3.53e-03 |
|
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: 38.56 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 70 LVGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAA-AKTLETLIDSE 148
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQAlSPVVAEAKAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 149 LPVVCAARSYYRDDVDF-IGPDNTHAAK-QATTYLIEQGHRHIAYVGGR-ADSLTRAERIGGYcaSLLQYGLPFKPEWVL 225
Cdd:cd01538 81 IKVIAYDRLILNADVDYyISFDNEKVGElQAQALLDAKPEGNYVLIGGSpTDNNAKLFRDGQM--KVLQPAIDSGKIKVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 226 ECERTQRSAADTIAQLLHQ-----HPKVTAVLCHYPEVALGAIYGVEASGrtvgkdnyIGQQVALLGFD-DVAEAE--LT 297
Cdd:cd01538 159 GDQWVDDWLPANAQQIMENaltanGNNVDAVVASNDGTAGGAIAALKAQG--------LSGGVPVSGQDaDLAAIKriLA 230
|
250
....*....|....*....
gi 518276643 298 SPALTFVSSPAREIGRQAA 316
Cdd:cd01538 231 GTQTMTVYKDIRLLADAAA 249
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
101-271 |
3.69e-03 |
|
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: 38.76 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 101 LFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPV-RGAAAKTLETLIDSELPVV-CAARSYYRDDVDFIGPDNTHAAKQAT 178
Cdd:cd19996 35 LIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNsPTALLPAIEKAAAAGIPVVlFDSGVGSDKYTAFVGVDDAAFGRVGA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 179 TYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLLQY-GLPFKPEWVLECERTQrsAADTIAQLLHQHPKVTAVLCHY 255
Cdd:cd19996 115 EWLVKQlgGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYpGIKIVGEVYADWDYAK--AKQAVESLLAAYPDIDGVWSDG 192
|
170
....*....|....*.
gi 518276643 256 PEVALGAIYGVEASGR 271
Cdd:cd19996 193 GAMTLGAIEAFEEAGR 208
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
123-290 |
3.82e-03 |
|
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: 38.47 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 123 QGVAGIIFNPVRGAA-AKTLETLIDSELPVVC-AARSYYRDDVDFIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGrADS 198
Cdd:cd19969 55 KNPDGIAVSAIDPEAlTPTINKAVDAGIPVVTfDSDAPESKRISYVGTDNYEAGYAAAEKLAELlgGKGKVAVLTG-PGQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 199 LTRAERIGGYCASllqyglpFKPEWVLECERTQRS------AADTIAQLLHQHPKvtavlchypevaLGAIYGVEASG-- 270
Cdd:cd19969 134 PNHEERVEGFKEA-------FAEYPGIEVVAVGDDnddpekAAQNTSALLQAHPD------------LVGIFGVDASGgv 194
|
170 180
....*....|....*....|....*.
gi 518276643 271 ------RTVGKDNyigqQVALLGFDD 290
Cdd:cd19969 195 gaaqavREAGKTG----KVKIVAFDD 216
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
71-294 |
4.07e-03 |
|
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: 38.51 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 71 VGLILRDITDPFYTEVTAGVSEVLEQQGYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIFNPVRGAAAK-TLETLIDSEL 149
Cdd:cd06317 2 IALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIpAIKRASEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 150 PVVCAARSYYRDDVD-FIGPDNTHAAKQ----ATTYLIEQ--GHRHIAYVGGRAdSLTRAERIGGYCASLLQygLPfKPE 222
Cdd:cd06317 82 PVIAYDAVIPSDFQAaQVGVDNLEGGKEigkyAADYIKAElgGQAKIGVVGALS-SLIQNQRQKGFEEALKA--NP-GVE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518276643 223 WVLECE-RTQRSAADTIAQ-LLHQHPKVTAVLCHYPEVALGAIYGVEASGRTvGKdnyigqqVALLGFDDVAEA 294
Cdd:cd06317 158 IVATVDgQNVQEKALSAAEnLLTANPDLDAIYATGEPALLGAVAAVRSQGRQ-GK-------IKVFGWDLTKQA 223
|
|
| AF2118 |
COG3620 |
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ... |
9-76 |
6.18e-03 |
|
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];
Pssm-ID: 442838 [Multi-domain] Cd Length: 95 Bit Score: 35.77 E-value: 6.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518276643 9 KATKIT--DVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAI-KELDYVPnsaaanlRSQQSNLVGLILR 76
Cdd:COG3620 27 KELGLSqlPVAELVGVSQSDILRIESGKRDPTVSTLEKIAEALgKELSAVL-------VVDDGKLVGIITR 90
|
|
| HipB |
COG1396 |
Transcriptional regulator, contains XRE-family HTH domain [Transcription]; |
14-48 |
6.30e-03 |
|
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
Pssm-ID: 441006 [Multi-domain] Cd Length: 83 Bit Score: 35.36 E-value: 6.30e-03
10 20 30
....*....|....*....|....*....|....*
gi 518276643 14 TDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQA 48
Cdd:COG1396 24 EELAERLGVSRSTISRIERGRRNPSLETLLKLAKA 58
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
87-272 |
6.61e-03 |
|
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: 37.73 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 87 TAGVSEVLEQQ----GYLLFLTQCGHSPERLQQSIHSLSRQGVAGIIF-----NPVRGAAAKTLetliDSELPVVCAARS 157
Cdd:cd06311 14 TAGVAYYAEKQakelADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVIlpqdsEELTVAAQKAK----DAGIPVVNFDRG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518276643 158 YYRDDVD-FIGPDNTHAAKQATTYLIEQ--GHRHIAYVGGRADSLTRAERIGGYCASLlQYGLPFKpewVLECER---TQ 231
Cdd:cd06311 90 LNVLIYDlYVAGDNPGMGVVSAEYIGKKlgGKGNVVVLEVPSSGSVNEERVAGFKEVI-KGNPGIK---ILAMQAgdwTR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518276643 232 RSAADTIAQLLHQHPKVTAVLCHYPEVALGAIYGVEASGRT 272
Cdd:cd06311 166 EDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRT 206
|
|
| HTH_3 |
pfam01381 |
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ... |
13-50 |
7.03e-03 |
|
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.
Pssm-ID: 460181 [Multi-domain] Cd Length: 55 Bit Score: 34.44 E-value: 7.03e-03
10 20 30
....*....|....*....|....*....|....*...
gi 518276643 13 ITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAIK 50
Cdd:pfam01381 12 QEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALG 49
|
|
| antidote_HigA |
TIGR02607 |
addiction module antidote protein, HigA family; Members of this family form a distinct clade ... |
12-49 |
9.89e-03 |
|
addiction module antidote protein, HigA family; Members of this family form a distinct clade within the larger family HTH_3 of helix-turn-helix proteins, described by pfam01381. Members of this clade are strictly bacterial and nearly always shorter than 110 amino acids. This family includes the characterized member HigA, without which the killer protein HigB cannot be cloned. The hig (host inhibition of growth) system is noted to be unusual in that killer protein is uncoded by the upstream member of the gene pair. [Regulatory functions, DNA interactions, Regulatory functions, Protein interactions, Mobile and extrachromosomal element functions, Other]
Pssm-ID: 274228 [Multi-domain] Cd Length: 78 Bit Score: 34.52 E-value: 9.89e-03
10 20 30
....*....|....*....|....*....|....*...
gi 518276643 12 KITDVAQRAGVSVTTVSMVLNGKGRISPATAERVQQAI 49
Cdd:TIGR02607 20 SVRALAKALGVSRSTLSRIVNGRAAITADMALRLAKAL 57
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