|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
1-331 |
0e+00 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 515.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 1 MATIKDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGMLVTQSTNLFFSEVIDG 80
Cdd:PRK10703 1 MATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 81 VESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKHADIPKVIMDWGPISSQ-ADKIID 159
Cdd:PRK10703 81 VEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEYRHIPMVVMDWGEAKADfTDAIID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 160 NSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNFECDTAVMAADKIASWQDRP 239
Cdd:PRK10703 161 NAFEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQKHRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 240 TAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIKDKEHDKRVFE 319
Cdd:PRK10703 241 TAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTIE 320
|
330
....*....|..
gi 499392550 320 MHPELVVRDTVK 331
Cdd:PRK10703 321 VHPRLVERRSVA 332
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-333 |
2.71e-148 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 420.76 E-value: 2.71e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 1 MATIKDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGMLVTQSTNLFFSEVIDG 80
Cdd:COG1609 3 RVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 81 VESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLdKHADIPKVIMDWGPISSQADKIIDN 160
Cdd:COG1609 83 IEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERL-AEAGIPVVLIDRPLPDPGVPSVGVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 161 SEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNFECDTAVMAADKIASWQDRPT 240
Cdd:COG1609 162 NRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 241 AVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIKDKEHDKRVFEM 320
Cdd:COG1609 242 AIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLL 321
|
330
....*....|...
gi 499392550 321 HPELVVRDTVKKI 333
Cdd:COG1609 322 PPELVVRESTAPA 334
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
4-330 |
2.66e-145 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 412.94 E-value: 2.66e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 4 IKDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGMLVTQSTNLFFSEVIDGVES 83
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 84 YCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKHADIPKVIMDWGPISSQADKIIDNSEE 163
Cdd:PRK10423 81 SCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMQRYPSVPTVMMDWAPFDGDSDLIQDNSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 164 GGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNFECDTAVMAADKIASWQDRPTAVF 243
Cdd:PRK10423 161 GGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPLRPQAVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 244 CFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIKDKEHDKRVFEMHPE 323
Cdd:PRK10423 241 TGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTPE 320
|
....*..
gi 499392550 324 LVVRDTV 330
Cdd:PRK10423 321 LMERGSV 327
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
61-329 |
8.47e-140 |
|
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: 396.63 E-value: 8.47e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKHADI 140
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAALRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNF 220
Cdd:cd06275 81 PVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 221 ECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNA 300
Cdd:cd06275 161 EPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGELA 240
|
250 260
....*....|....*....|....*....
gi 499392550 301 FEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd06275 241 VELLLDRIENKREEPQSIVLEPELIERES 269
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
61-325 |
3.36e-110 |
|
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: 321.39 E-value: 3.36e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLdKHADI 140
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEEL-LAAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMDWGPISSQADKI-IDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGN 219
Cdd:cd06267 80 PVVLIDRRLDGLGVDSVvVDN-YAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 220 FECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKN 299
Cdd:cd06267 159 FSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRA 238
|
250 260
....*....|....*....|....*.
gi 499392550 300 AFEILLERIKDKEHDKRVFEMHPELV 325
Cdd:cd06267 239 AAELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
61-329 |
6.57e-96 |
|
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: 285.20 E-value: 6.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKHadI 140
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELSKR--Y 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKV-IMDWGPISSQADKIIDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGN 219
Cdd:cd06284 79 PIVqCCEYIPDSGVPSVSIDN-EAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 220 FECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKN 299
Cdd:cd06284 158 FSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGET 237
|
250 260 270
....*....|....*....|....*....|
gi 499392550 300 AFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd06284 238 AAELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-330 |
8.54e-95 |
|
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: 282.19 E-value: 8.54e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMC-SDLTEELREMLDkhAD 139
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPaRDDAPDLQELAA--RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGN 219
Cdd:cd06285 79 VPVVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 220 FECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKN 299
Cdd:cd06285 159 FTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRR 238
|
250 260 270
....*....|....*....|....*....|.
gi 499392550 300 AFEILLERIKDKEHDKRVFEMHPELVVRDTV 330
Cdd:cd06285 239 AAELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
61-328 |
1.37e-88 |
|
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: 266.42 E-value: 1.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKHADI 140
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNF 220
Cdd:cd19976 81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 221 ECDTAVMAADKIASwQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNA 300
Cdd:cd19976 161 SLEGGYKAAEELLK-SKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQEA 239
|
250 260
....*....|....*....|....*...
gi 499392550 301 FEILLERIKDKEHDKRVFEMHPELVVRD 328
Cdd:cd19976 240 AKLLLKIIKNPAKKKEEIVLPPELIKRD 267
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
61-328 |
2.00e-85 |
|
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: 258.22 E-value: 2.00e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKHaDI 140
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEK-IP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMDWGpISSQADKII--DNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEG 218
Cdd:cd06270 80 PLVVINRY-IPGLADRCVwlDN-EQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 219 NFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGK 298
Cdd:cd06270 158 DFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQ 237
|
250 260 270
....*....|....*....|....*....|.
gi 499392550 299 NAFEILLERIKDKEHD-KRVFEmhPELVVRD 328
Cdd:cd06270 238 AAAELALNLAYGEPLPiSHEFT--PTLIERD 266
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
61-329 |
3.01e-85 |
|
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: 257.87 E-value: 3.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKhADI 140
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKN-MNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVImdwgpISSQADKI------IDNsEEGGYLATKYLIDNGHTKIACLSGHF-EKAACQERIQGFKRAMKEANITLNNE 213
Cdd:cd19975 80 PVVL-----VSTESEDPdipsvkIDD-YQAAYDATNYLIKKGHRKIAMISGPLdDPNAGYPRYEGYKKALKDAGLPIKEN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 214 WILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPK 293
Cdd:cd19975 154 LIVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPF 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 499392550 294 RRVGKNAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd19975 234 YEMGKKAVELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
61-329 |
4.83e-84 |
|
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: 254.75 E-value: 4.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELremlDKHADI 140
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEE----YKKLNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMD--WGP----ISSqadkiiDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEW 214
Cdd:cd06291 77 PIVSIDryLSEgipsVSS------DN-YQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 215 ILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKR 294
Cdd:cd06291 150 IDENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIE 229
|
250 260 270
....*....|....*....|....*....|....*
gi 499392550 295 RVGKNAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd06291 230 EMAKEAVELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
61-329 |
1.82e-79 |
|
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: 243.22 E-value: 1.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQ-STNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEelREMLDKHAD 139
Cdd:cd06288 1 TIGLITDDiATTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHRE--VTLPPELTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIM----DWGPISSqadkIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWI 215
Cdd:cd06288 79 IPLVLLncfdDDPSLPS----VVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 216 LEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRR 295
Cdd:cd06288 155 VHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYE 234
|
250 260 270
....*....|....*....|....*....|....
gi 499392550 296 VGKNAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd06288 235 MGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
61-327 |
2.38e-78 |
|
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: 240.24 E-value: 2.38e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDG-ILVMCSDLTEELREMLdKHaD 139
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGiILAPSAGPSRELKRLL-KH-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGN 219
Cdd:cd06280 79 IPIVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 220 FECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKN 299
Cdd:cd06280 159 STIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRI 238
|
250 260
....*....|....*....|....*...
gi 499392550 300 AFEILLERIKDKEHDKRVFEMHPELVVR 327
Cdd:cd06280 239 AAQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
62-324 |
9.45e-77 |
|
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: 236.37 E-value: 9.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 62 IGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKHADIP 141
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQNVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 142 KVIMDWGP-ISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNF 220
Cdd:cd01537 82 VVFFDKEPsRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTGDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 221 ECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNA 300
Cdd:cd01537 162 DTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKTT 241
|
250 260
....*....|....*....|....
gi 499392550 301 FEILLERIKDKEHDKRVFEMHPEL 324
Cdd:cd01537 242 FDLLLNLADNWKIDNKVVRVPYVL 265
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
1.05e-76 |
|
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: 236.40 E-value: 1.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLT-EELREMLDKhaD 139
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDlSHLARLRAR--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIMDWGPISSQADKI-IDNSEeGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNnEWILEG 218
Cdd:cd06293 79 TAVVLLDRPAPGPAGCSVsVDDVQ-GGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPD-EVVREL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 219 NFECDTAVM---AADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRR 295
Cdd:cd06293 157 SAPDANAELgraAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYE 236
|
250 260 270
....*....|....*....|....*....|....
gi 499392550 296 VGKNAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd06293 237 LGRAAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
61-329 |
1.72e-75 |
|
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: 233.22 E-value: 1.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCS---------DLTEELR 131
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTksalpnpnlDLYEELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 132 EMldkhaDIPKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAAcQERIQGFKRAMKEANITLN 211
Cdd:cd01541 81 KK-----GIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIFKSDDLQG-VERYQGFIKALREAGLPID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 212 NEWIL---EGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTT 288
Cdd:cd01541 155 DDRILwysTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTS 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499392550 289 IHQPKRRVGKNAFEILLERIKDKEHDKRVfEMHPELVVRDT 329
Cdd:cd01541 235 VVHPKEELGRKAAELLLRMIEEGRKPESV-IFPPELIERES 274
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
3.48e-75 |
|
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: 232.12 E-value: 3.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKhaDI 140
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLAE--GI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMDWGPISSQADKI-IDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGN 219
Cdd:cd06290 79 PVVLVDRELEGLNLPVVnVDN-EQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 220 FECDTAVMAADKIASwQDRP-TAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGK 298
Cdd:cd06290 158 FTEESGYEAMKKLLK-RGGPfTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGK 236
|
250 260 270
....*....|....*....|....*....|.
gi 499392550 299 NAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd06290 237 TAAEILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
61-325 |
8.25e-75 |
|
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: 231.26 E-value: 8.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDG-ILVMCSDLTEELREMLDKHad 139
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGiIIAPTGGNEDLIEKLVKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGN 219
Cdd:cd19977 79 IPVVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEELIKHVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 220 FEcDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKN 299
Cdd:cd19977 159 RQ-DDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGRK 237
|
250 260
....*....|....*....|....*..
gi 499392550 300 AFEILLERIKDKEH-DKRVFEMHPELV 325
Cdd:cd19977 238 AAELLLDRIENKPKgPPRQIVLPTELI 264
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
61-328 |
1.47e-72 |
|
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: 225.52 E-value: 1.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDG-ILVMCSDLTEELREMLdKHAD 139
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGlILSPAAGTTAELLRRL-KAWG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIMDWGPISSQADKI-IDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEG 218
Cdd:cd06289 80 IPVVLALRDVPGSDLDYVgIDN-RLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 219 NFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGK 298
Cdd:cd06289 159 PATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGR 238
|
250 260 270
....*....|....*....|....*....|
gi 499392550 299 NAFEILLERIKDKEHDKRVFEMHPELVVRD 328
Cdd:cd06289 239 RAARLLLRRIEGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
61-329 |
2.66e-71 |
|
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: 222.07 E-value: 2.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQ-RDYIRMLAEKRVDGILVMcsDLTEELREMLDK-HA 138
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDEDDPASvREALDRLLSQRVDGIIVI--APDEAVLEALRRlPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 139 DIPKVIMDWGPISSQADKIIDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANitLNNEWILEG 218
Cdd:cd01574 79 GLPVVIVGSGPSPGVPTVSIDQ-EEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAG--LPPPPVVEG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 219 NFECDTAVMAADKIASwQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGK 298
Cdd:cd01574 156 DWSAASGYRAGRRLLD-DGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGR 234
|
250 260 270
....*....|....*....|....*....|.
gi 499392550 299 NAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd01574 235 RAVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
28-330 |
3.44e-71 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 223.34 E-value: 3.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 28 VAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDY 107
Cdd:PRK11041 4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 108 IRMLAEKRVDGILVMCSDL-----TEELRemldkhaDIPKVIM--DWGPISSQADKIIDNSEeGGYLATKYLIDNGHTKI 180
Cdd:PRK11041 84 VNLIITKQIDGMLLLGSRLpfdasKEEQR-------NLPPMVManEFAPELELPTVHIDNLT-AAFEAVNYLHELGHKRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 181 ACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQL 260
Cdd:PRK11041 156 ACIAGPEEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRM 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 261 GLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIKDKEHDKRVFEMHPELVVRDTV 330
Cdd:PRK11041 236 GLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
7.14e-71 |
|
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: 221.23 E-value: 7.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKHaDI 140
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQR-QV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIM----DWGPISSQAdkiIDNsEEGGYLATKYLIDNGHTKIACLSGHFE---KAacQERIQGFKRAMKEANITLNNE 213
Cdd:cd06273 80 PYVLTwsydEDSPHPSIG---FDN-RAAAARAAQHLLDLGHRRIAVISGPTAgndRA--RARLAGIRDALAERGLELPEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 214 WILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPK 293
Cdd:cd06273 154 RVVEAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPA 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 499392550 294 RRVGKNAFEILLERIKDKEHDKRVfEMHPELVVRDT 329
Cdd:cd06273 234 REIGELAARYLLALLEGGPPPKSV-ELETELIVRES 268
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
61-329 |
4.85e-69 |
|
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: 216.65 E-value: 4.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLIL--CNTGGiYEKQRDYIRMLAEKRVDGILV---MCSDltEELREMLD 135
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVepCDSDD-EDLADRLRRFLSRSRPDGVILtppLSDD--PALLDALD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 136 KHaDIPKVIMdwGPISSQADKI---IDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNN 212
Cdd:cd01545 78 EL-GIPYVRI--APGTDDDRSPsvrIDD-RAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 213 EWILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQP 292
Cdd:cd01545 154 DLVVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQP 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 499392550 293 KRRVGKNAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd01545 234 IAEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
61-328 |
2.87e-66 |
|
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: 209.44 E-value: 2.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVM----CSDLTEELREMldk 136
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVptgeNSEGLQALIAQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 137 haDIPKVIMDWG-PISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWI 215
Cdd:cd06299 78 --GLPVVFVDREvEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 216 LEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRR 295
Cdd:cd06299 156 AFGDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVER 235
|
250 260 270
....*....|....*....|....*....|...
gi 499392550 296 VGKNAFEILLERIKDKEHDKRVfEMHPELVVRD 328
Cdd:cd06299 236 IGRRAVELLLALIENGGRATSI-RVPTELIPRE 267
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
61-330 |
3.36e-66 |
|
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: 209.44 E-value: 3.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLdKHADI 140
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLL-RSAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMDwgPISSQADKI----IDNSEeGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWIL 216
Cdd:cd06296 80 PFVLID--PVGEPDPDLpsvgATNWA-GGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 217 EGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRV 296
Cdd:cd06296 157 EGDFTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREM 236
|
250 260 270
....*....|....*....|....*....|....
gi 499392550 297 GKNAFEILLERIKDKEHDKRVFEMHPELVVRDTV 330
Cdd:cd06296 237 GAVAVRLLLRLLEGGPPDARRIELATELVVRGST 270
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
2-330 |
2.00e-65 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 209.85 E-value: 2.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 2 ATIKDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGmLVTQSTNLFF-SEVIDG 80
Cdd:PRK09526 6 VTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIG-LATTSLALHApSQIAAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 81 VESYCYRQGYTLILC--NTGGIYEKQRDYIRMLAEkRVDGILVMCSDLTEELREMLDKHADIPKVIMDWGPiSSQADKII 158
Cdd:PRK09526 85 IKSRADQLGYSVVISmvERSGVEACQAAVNELLAQ-RVSGVIINVPLEDADAEKIVADCADVPCLFLDVSP-QSPVNSVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 159 DNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNewILEGNFECDTAVMAADKIASWQDR 238
Cdd:PRK09526 163 FDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQPIA--VREGDWSAMSGYQQTLQMLREGPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 239 PTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIKDKEHdkRVF 318
Cdd:PRK09526 241 PSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALSQGQAV--KGS 318
|
330
....*....|...
gi 499392550 319 EMHP-ELVVRDTV 330
Cdd:PRK09526 319 QLLPtSLVVRKST 331
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
1.95e-64 |
|
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: 204.71 E-value: 1.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQ---STNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSdLTEELREMLdKH 137
Cdd:cd19974 1 NIAVLIPErffGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGE-ISKEYLEKL-KE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 138 ADIPKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIA-------CLSghFekaacQERIQGFKRAMKEANITL 210
Cdd:cd19974 79 LGIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGfvgdinyTSS--F-----MDRYLGYRKALLEAGLPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 211 NN-EWILEGNfecDTAVMAADKIASWQD--RPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLT 287
Cdd:cd19974 152 EKeEWLLEDR---DDGYGLTEEIELPLKlmLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499392550 288 TIHQPKRRVGKNAFEILLERIKDKEhdkRVFEMH---PELVVRDT 329
Cdd:cd19974 229 TVEVDKEAMGRRAVEQLLWRIENPD---RPFEKIlvsGKLIERDS 270
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
61-317 |
7.02e-61 |
|
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: 195.41 E-value: 7.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLdKHADI 140
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKAL-KKLKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIM--DWGPISSqadkIIDNSEEGGYLATKYLIDNGHTKIACLSGHFE-KAACQERIQGFKRAMKEANITlnNEWILE 217
Cdd:cd01542 80 PVVVLgqEHEGFSC----VYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEdIAVGVARKQGYLDALKEHGID--EVEIVE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 218 GNFECDTAVMAADKIASwQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVG 297
Cdd:cd01542 154 TDFSMESGYEAAKELLK-ENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAG 232
|
250 260
....*....|....*....|
gi 499392550 298 KNAFEILLERIKDKEHDKRV 317
Cdd:cd01542 233 EKAAELLLDMIEGEKVPKKQ 252
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
61-329 |
9.26e-61 |
|
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: 195.41 E-value: 9.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLdKHADI 140
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLL-RAAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKV-IMDWG--PIssqaDKII--DNsEEGGYLATKYLIDNGHTKIACLSGHFEKAAC-QERIQGFKRAMKEANITLNNEW 214
Cdd:cd01575 80 PVVeTWDLPddPI----DMAVgfSN-FAAGRAMARHLIERGYRRIAFVGARLDGDSRaRQRLEGFRDALAEAGLPLPLVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 215 ILE--GNFEcDTAVMAADKIASWQDrPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQP 292
Cdd:cd01575 155 LVElpSSFA-LGREALAELLARHPD-LDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVP 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 499392550 293 KRRVGKNAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd01575 233 RYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
3.00e-60 |
|
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: 193.90 E-value: 3.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEkQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKHaDI 140
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDD-VDDALRQLLQYRVDGVIVTSATLSSELAEECARR-GI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMDWGPISSQADKI-IDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLnnEWILEGN 219
Cdd:cd06278 79 PVVLFNRVVEDPGVDSVsCDN-RAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPP--PAVEAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 220 FECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRL-QQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGK 298
Cdd:cd06278 156 YSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVGFDDIPMAAWPSYDLTTVRQPIEEMAE 235
|
250 260 270
....*....|....*....|....*....|.
gi 499392550 299 NAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd06278 236 AAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
60-328 |
7.34e-59 |
|
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: 190.53 E-value: 7.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 60 RTIGMLVTQSTnLFFSEVIDGVESYCYRQGYTLILCNTGgIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKhAD 139
Cdd:cd06277 8 SDNGDGVVNET-PFFSELIDGIEREARKYGYNLLISSVD-IGDDFDEILKELTDDQSSGIILLGTELEEKQIKLFQD-VS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIMD-WGPiSSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANIT--LNNEWIL 216
Cdd:cd06277 85 IPVVVVDnYFE-DLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSedPEPEFVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 217 EGNFECDTAVMAAdKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRV 296
Cdd:cd06277 164 SVGPEGAYKDMKA-LLDTGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQM 242
|
250 260 270
....*....|....*....|....*....|..
gi 499392550 297 GKNAFEILLERIKDKEHDKRVFEMHPELVVRD 328
Cdd:cd06277 243 GKLAVRRLIEKIKDPDGGTLKILVSTKLVERG 274
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
1-330 |
1.79e-57 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 189.20 E-value: 1.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 1 MATIKDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGMLVTQSTNLFFSEVIDG 80
Cdd:PRK10727 1 MATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 81 VESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILV---MCSDltEELREMLDKhadIPKVIMdwgpissqADKI 157
Cdd:PRK10727 81 VEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVhakMIPD--AELASLMKQ---IPGMVL--------INRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 158 IDNSEE---------GGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNFECDTAVMA 228
Cdd:PRK10727 148 LPGFENrcialddryGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 229 ADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERI 308
Cdd:PRK10727 228 MTELLGRGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALA 307
|
330 340
....*....|....*....|..
gi 499392550 309 KDKEHDKRVFEMHPELVVRDTV 330
Cdd:PRK10727 308 DNRPLPEITNVFSPTLVRRHSV 329
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
61-329 |
1.94e-57 |
|
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: 186.96 E-value: 1.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQS-----TNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRdyirmlaEKRVDGILVMcSDLTEELREMLD 135
Cdd:cd01544 1 TIGIIQWYSeeeelEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLESL-------LEKVDGIIAI-GKFSKEEIEKLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 136 KHADiPKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQE-----RIQGFKRAMKEANItL 210
Cdd:cd01544 73 KLNP-NIVFVDSNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGEeiedpRLRAFREYMKEKGL-Y 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 211 NNEWILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIH 290
Cdd:cd01544 151 NEEYIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVH 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 499392550 291 QPKRRVGKNAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd01544 231 IPTEEMGRTAVRLLLERINGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-328 |
4.08e-57 |
|
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: 185.90 E-value: 4.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDG-ILVMCSDLTEELREMLDkHAD 139
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGlILTPGDEDDPELAAALA-RLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIMDwGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGN 219
Cdd:cd06281 80 IPVVLID-RDLPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 220 FECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKN 299
Cdd:cd06281 159 FSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRA 238
|
250 260 270
....*....|....*....|....*....|
gi 499392550 300 AFEILLERIKDK-EHDKRVFEMHPELVVRD 328
Cdd:cd06281 239 AAELLLDRIEGPpAGPPRRIVVPTELILRD 268
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
61-329 |
2.33e-56 |
|
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: 184.01 E-value: 2.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQS----TNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGiLVMCSDLTEELREMLDK 136
Cdd:cd06292 1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDG-FVLASTRHDDPRVRYLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 137 HADIPKVIMDwGPISSQADKIIDNSEEGG-YLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWI 215
Cdd:cd06292 80 EAGVPFVAFG-RANPDLDFPWVDVDGAAGmRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 216 LEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRR 295
Cdd:cd06292 159 VEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDE 238
|
250 260 270
....*....|....*....|....*....|....
gi 499392550 296 VGKNAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd06292 239 IGRAVVDLLLAAIEGNPSEPREILLQPELVVRES 272
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
61-327 |
2.77e-56 |
|
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: 183.52 E-value: 2.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGiLVMCSdlteelremldkHADI 140
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDG-LIITS------------REND 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMDW---GPI----SSQADKI----IDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAAC--QERIQGFKRAMKEAN 207
Cdd:cd06286 68 WEVIEPYakyGPIvlceETDSPDIpsvyIDR-YEAYLEALEYLKEKGHRKIGYCLGRPESSSAstQARLKAYQDVLGEHG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 208 ITLNNEWILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEyfSPPLT 287
Cdd:cd06286 147 LSLREEWIFTNCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISE--LLNLT 224
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 499392550 288 TIHQPKRRVGKNAFEILLERIKDKEhdKRVFEMHPELVVR 327
Cdd:cd06286 225 TIDQPLEEMGKEAFELLLSQLESKE--PTKKELPSKLIER 262
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-312 |
1.21e-55 |
|
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: 182.10 E-value: 1.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDG-ILVMCSDLTEELREMLDkHAD 139
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGlILTVGDAQGSEALELLE-EEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIMDWGPISSQADKI-IDNsEEGGYLATKYLIDNGHTKIACLSGHFEKA-ACQERIQGFKRAMKEANitLNNEWILE 217
Cdd:cd06282 80 VPYVLLFNQTENSSHPFVsVDN-RLASYDVAEYLIALGHRRIAMVAGDFSASdRARLRYQGYRDALKEAG--LKPIPIVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 218 GNF---ECDTAVMaadKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKR 294
Cdd:cd06282 157 VDFptnGLEEALT---SLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSR 233
|
250
....*....|....*...
gi 499392550 295 RVGKNAFEILLERIKDKE 312
Cdd:cd06282 234 DMGRAAADLLLAEIEGES 251
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
61-312 |
1.77e-55 |
|
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: 181.63 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQST-----NLFFSEVIDGVESYCYRQGYTLILcNTGGIYEKQRDYI-RMLAEKRVDGILVMCSDLTEELREML 134
Cdd:cd06294 1 TIGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLL-ATGNTEEELLEEVkRMVRGRRVDGFILLYSKEDDPLIEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 135 DKHaDIPKVI----MDWGPISSqadkiIDNSE-EGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANIT 209
Cdd:cd06294 80 KEE-GFPFVVigkpLDDNDVLY-----VDNDNvQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 210 LNNEWILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTI 289
Cdd:cd06294 154 LDDDYILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSV 233
|
250 260
....*....|....*....|...
gi 499392550 290 HQPKRRVGKNAFEILLERIKDKE 312
Cdd:cd06294 234 DINPYELGREAAKLLINLLEGPE 256
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
61-327 |
2.33e-52 |
|
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: 173.51 E-value: 2.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVM-CSDLTEELREMLDKHad 139
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQpTGNNNDAYLELAQKG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKA-ACQERIQGFKRAMKEANITLNNEWIlEG 218
Cdd:cd06283 79 LPVVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGIsTRRERLQGFLDALARYNIEGDVYVI-EI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 219 NFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGK 298
Cdd:cd06283 158 EDTEDLQQALAAFLSQHDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGK 237
|
250 260
....*....|....*....|....*....
gi 499392550 299 NAFEILLERIKDKEHDKRVFEMHPELVVR 327
Cdd:cd06283 238 AAAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
61-329 |
1.74e-50 |
|
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: 169.31 E-value: 1.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFS-----EVIDGVESYCYRQGYTLILCNTGGiyekQRDYIRMLAEKRVDGILVMCSDLTEELREMLd 135
Cdd:cd06279 1 AIGVLLPDDLSYAFSdpvaaQFLRGVAEVCEEEGLGLLLLPATD----EGSAAAAVRNAAVDGFIVYGLSDDDPAVAAL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 136 KHADIPKVIMDwGPISSQADKI-IDNsEEGGYLATKYLIDNGHTKIACLS---------GHFEKAAC--------QERIQ 197
Cdd:cd06279 76 RRRGLPLVVVD-GPAPPGIPSVgIDD-RAAARAAARHLLDLGHRRIAILSlrldrgrerGPVSAERLaaatnsvaRERLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 198 GFKRAMKEANITLNNEWILE-GNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNI 276
Cdd:cd06279 154 GYRDALEEAGLDLDDVPVVEaPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDI 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499392550 277 ELAEYFSPPLTTIHQPKRRVGKNAFEILLERIkDKEHDKRVfEMHPELVVRDT 329
Cdd:cd06279 234 PEAAAADPGLTTVRQPAVEKGRAAARLLLGLL-PGAPPRPV-ILPTELVVRAS 284
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
171-330 |
6.91e-50 |
|
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: 163.66 E-value: 6.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 171 YLIDNGHTKIACLSGHFEKAAC--QERIQGFKRAMKEANITLNNEWILEGNFECDTAVmaADKIASWQDRPTAVFCFNDT 248
Cdd:pfam13377 1 HLAELGHRRIALIGPEGDRDDPysDLRERGFREAARELGLDVEPTLYAGDDEAEAAAA--RERLRWLGALPTAVFVANDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 249 MALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIKDKEHDKRVFEMHPELVVRD 328
Cdd:pfam13377 79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERE 158
|
..
gi 499392550 329 TV 330
Cdd:pfam13377 159 ST 160
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
1-330 |
1.92e-49 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 168.42 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 1 MATIKDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGMLVTQSTNLFFSEVIDG 80
Cdd:PRK10401 1 MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 81 VESYCYR-QGYTLIlcntGGIY---EKQRDYIRMLAEKRVDGILVMCSDLT-EELREMLDKhadIPKVIMDWGPISSQAD 155
Cdd:PRK10401 81 VDLVAQQhQKYVLI----GNSYheaEKERHAIEVLIRQRCNALIVHSKALSdDELAQFMDQ---IPGMVLINRVVPGYAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 156 KII--DNSeEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNFECDTAVMAADKIA 233
Cdd:PRK10401 154 RCVclDNV-SGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 234 SWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIKDK-- 311
Cdd:PRK10401 233 GRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNld 312
|
330
....*....|....*....
gi 499392550 312 EHDKRVFemHPELVVRDTV 330
Cdd:PRK10401 313 PRASHCF--MPTLVRRHSV 329
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
61-325 |
4.79e-49 |
|
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: 165.03 E-value: 4.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIG-MLVTQSTNL---FFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVmCSDLTEELR-EMLD 135
Cdd:cd20010 1 AIGlVLPLDPGDLgdpFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFIL-ARTRVNDPRiAYLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 136 KhADIPKVIMdwGPISSQA-----DkiIDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITL 210
Cdd:cd20010 80 E-RGIPFVVH--GRSESGApyawvD--IDN-EGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 211 NNEWILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNI-ELAEYFSPPLTTI 289
Cdd:cd20010 154 DPALVREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALEYFSPPLTTT 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 499392550 290 HQPKRRVGKNAFEILLERIKDKEhDKRVFEM-HPELV 325
Cdd:cd20010 234 RSSLRDAGRRLAEMLLALIDGEP-AAELQELwPPELI 269
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
61-312 |
2.36e-48 |
|
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: 163.23 E-value: 2.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLdKHADI 140
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEF-KRSPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMdwGPISSQaDKI----IDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQE-RIQGFKRAMKEANITLNNEWI 215
Cdd:cd06298 80 PVVLA--GTVDSD-HEIpsvnIDY-EQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDkKLQGYKRALEEAGLEFNEPLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 216 LEGNFECDTAVMAADKIASwQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRR 295
Cdd:cd06298 156 FEGDYDYDSGYELYEELLE-SGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYD 234
|
250
....*....|....*..
gi 499392550 296 VGKNAFEILLERIKDKE 312
Cdd:cd06298 235 IGAVAMRLLTKLMNKEE 251
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
2-328 |
3.35e-46 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 159.87 E-value: 3.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 2 ATIKDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGMLVTQSTNLFFSEVIDGV 81
Cdd:PRK10014 7 ITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 82 ESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVM-CSDLTEELREMLDKHAdIPKVIMDWGPISSQADKIIDN 160
Cdd:PRK10014 87 TEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAgAAGSSDDLREMAEEKG-IPVVFASRASYLDDVDTVRPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 161 SEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILegnfECD-TAVMAADKIASWQDR- 238
Cdd:PRK10014 166 NMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVL----ECTsSQKQAAEAITALLRHn 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 239 P--TAVFCFNDTMALGLMSRLQQLGLRIPED---------ISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLER 307
Cdd:PRK10014 242 PtiSAVVCYNETIAMGAWFGLLRAGRQSGESgvdryfeqqVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRMMQR 321
|
330 340
....*....|....*....|.
gi 499392550 308 IKDKEHDKRVFEMHPELVVRD 328
Cdd:PRK10014 322 ITHEETHSRNLIIPPRLIARK 342
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
57-329 |
6.50e-42 |
|
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: 146.63 E-value: 6.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 57 NTTRTIGMLV-------TQSTNLFFSEVIDGVESYCYRQGYTLILCNtggIYEKQRDYIRMLAEKRVDGILVM-CSDLTE 128
Cdd:cd06295 1 QRSRTIAVVVpmdphgdQSITDPFFLELLGGISEALTDRGYDMLLST---QDEDANQLARLLDSGRADGLIVLgQGLDHD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 129 ELREMLDkhADIPKVImdWGPISSQADKII---DNsEEGGYLATKYLIDNGHTKIACLSG--HFEKAacqERIQGFKRAM 203
Cdd:cd06295 78 ALRELAQ--QGLPMVV--WGAPEDGQSYCSvgsDN-VKGGALATEHLIEIGRRRIAFLGDppHPEVA---DRLQGYRDAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 204 KEANITLNNEWILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFS 283
Cdd:cd06295 150 AEAGLEADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFR 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499392550 284 PPLTTIHQPKRRVGKnafeILLERIKDKEHDKRV-FEMHP-ELVVRDT 329
Cdd:cd06295 230 PPLTTVRQDLALAGR----LLVEKLLALIAGEPVtSSMLPvELVVRES 273
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
61-329 |
6.61e-41 |
|
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: 143.76 E-value: 6.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEeLREMLDKHADI 140
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTE-LFEEVIVPTEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMDWGpiSSQADKIIDNSEEGGYLATKYLIDNGHTKIAC----LSGHFEKAACQERIQGFKRAMKEANITLNNEWIL 216
Cdd:cd06297 80 PVVLIDAN--SMGYDCVYVDNVKGGFMATEYLAGLGEREYVFfgieEDTVFTETVFREREQGFLEALNKAGRPISSSRMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 217 EGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEyfSPPLTTIHQPKRRV 296
Cdd:cd06297 158 RIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTVRQPVEEM 235
|
250 260 270
....*....|....*....|....*....|...
gi 499392550 297 GKNAFEILLERIKDKEHDKRVFEMHPELVVRDT 329
Cdd:cd06297 236 GEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
2-71 |
1.50e-34 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 120.77 E-value: 1.50e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 2 ATIKDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGMLVTQSTN 71
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
4-309 |
3.86e-32 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 122.44 E-value: 3.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 4 IKDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGMLVTQSTNLFFSEVIDGVES 83
Cdd:PRK14987 8 LQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 84 YCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLDKhADIPKV-IMDWGPISSQADKIIDNSE 162
Cdd:PRK14987 88 VTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEV-AGIPVVeLMDSQSPCLDIAVGFDNFE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 163 EGGYLaTKYLIDNGHTKIACLSGHFEKAACQERiQGFKRAMKEANITLNNEwILEGNFECDTAVMAADKIASWQDRPTAV 242
Cdd:PRK14987 167 AARQM-TTAIIARGHRHIAYLGARLDERTIIKQ-KGYEQAMLDAGLVPYSV-MVEQSSSYSSGIELIRQARREYPQLDGV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499392550 243 FCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIK 309
Cdd:PRK14987 244 FCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIR 310
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
112-328 |
1.16e-29 |
|
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: 114.01 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 112 AEKRVDGILVMcsDLTEELREMLDKHAD-IPkvIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIAcLSGHFEKA 190
Cdd:cd06272 53 SENRFDGVIVF--GISDSDIEYLNKNKPkIP--IVLYNRESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIA-YIGNPNSN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 191 ACQ-ERIQGFKRAMKEANITLNNEWILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDIS 269
Cdd:cd06272 128 RNQtLRGKGFIETCEKHGIHLSDSIIDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDIS 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499392550 270 VIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIKDKEHDKRVFEMHPELVVRD 328
Cdd:cd06272 208 IVSYDNIPQEARSDPPLTVVGVPIEKIAEESLRLILKLIEGRENEIQQLILYPELIFRE 266
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
46-330 |
5.39e-28 |
|
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: 110.78 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 46 APSAVARSLKCNTTRTIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSD 125
Cdd:COG1879 20 GSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 126 lTEELREMLDK--HADIPKVIMDWGPISSQADKII--DNsEEGGYLATKYLID--NGHTKIACLSGHFEKAACQERIQGF 199
Cdd:COG1879 100 -PDALAPALKKakAAGIPVVTVDSDVDGSDRVAYVgsDN-YAAGRLAAEYLAKalGGKGKVAILTGSPGAPAANERTDGF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 200 KRAMKEA-NITLNNEwiLEGNFecdTAVMAADKIASW-QDRP--TAVFCFNDTMALGLMSRLQQLGLriPEDISVIGYD- 274
Cdd:COG1879 178 KEALKEYpGIKVVAE--QYADW---DREKALEVMEDLlQAHPdiDGIFAANDGMALGAAQALKAAGR--KGDVKVVGFDg 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499392550 275 NIELAEYF-SPPLT-TIHQPKRRVGKNAFEILLERIKDKEHDKRVFeMHPELVVRDTV 330
Cdd:COG1879 251 SPEALQAIkDGTIDaTVAQDPYLQGYLAVDAALKLLKGKEVPKEIL-TPPVLVTKENV 307
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
61-312 |
3.76e-27 |
|
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: 107.51 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQS---TNLFFSEVIDGVESYCYRQGYTLILcnTGGIYEKQRDYIRMLAEK-RVDGILVMCSDLTEELREMLDK 136
Cdd:cd06271 1 VIALVFPVTeteLNGTVSE*VSGITEEAGTTGYHLLV--WPFEEAES*VPIRDLVETgSADGVILSEIEPNDPRVQFLTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 137 hADIPKVIM-----DWGpissQADKIIDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITln 211
Cdd:cd06271 79 -QNFPFVAHgrsd*PIG----HAWVDIDN-EAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGLT-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 212 nEWILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIE-LAEYFSPPLTTIH 290
Cdd:cd06271 151 -GYPLDADTTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPfLGAMITPPLTTVH 229
|
250 260
....*....|....*....|..
gi 499392550 291 QPKRRVGKNAFEILLERIKDKE 312
Cdd:cd06271 230 APIAEAGRELAKALLARIDGED 251
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
1-310 |
1.32e-26 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 107.15 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 1 MATIKDVARLAGVSTTTVSHVINK--TRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTR-TIGMLVT--QSTNL--- 72
Cdd:PRK10339 1 MATLKDIAIEAGVSLATVSRVLNDdpTLNVKEETKHRILEIAEKLEYKTSSARKLQTGAVNQhHILAIYSyqQELEIndp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 73 FFSEVIDGVESYCYRQGYTLILCntggiYEKQRDyirmLAEKRVDGILVMcSDLTEELREMLDKHADiPKVIMDWGPISS 152
Cdd:PRK10339 81 YYLAIRHGIETQCEKLGIELTNC-----YEHSGL----PDIKNVTGILIV-GKPTPALRAAASALTD-NICFIDFHEPGS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 153 QADKI-ID---NSEEggylATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEwILEGNFECDTAVMA 228
Cdd:PRK10339 150 GYDAVdIDlarISKE----IIDFYINQGVNRIGFIGGEDEPGKADIREVAFAEYGRLKQVVREED-IWRGGFSSSSGYEL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 229 ADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERI 308
Cdd:PRK10339 225 AKQMLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKA 304
|
..
gi 499392550 309 KD 310
Cdd:PRK10339 305 RD 306
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
158-310 |
5.79e-26 |
|
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: 104.16 E-value: 5.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 158 IDNsEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNFECDTAVMAADKIASWQD 237
Cdd:cd20009 100 FDN-EAFAYEAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAARRLLRQPP 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499392550 238 RPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFEILLERIKD 310
Cdd:cd20009 179 RPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEG 251
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
59-317 |
2.89e-25 |
|
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: 102.59 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 59 TRTIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLT-------EELR 131
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSgdditakAEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 132 EM--------LDKHADIPKVIMDWgpisSQAdkiidnseegGYLATKYLIDNGHTK-IACLSGHFEKAACQERIQGFKRA 202
Cdd:pfam00532 81 GIpviaaddaFDNPDGVPCVMPDD----TQA----------GYESTQYLIAEGHKRpIAVMAGPASALTARERVQGFMAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 203 MKEANITLNNEWILEGnfeCDTAVMAADKIASWQDR-PT--AVFCFNDTMALGLMSRLQQLG-LRIPEDI-----SVIGY 273
Cdd:pfam00532 147 LAAAGREVKIYHVATG---DNDIPDAALAANAMLVShPTidAIVAMNDEAAMGAVRALLKQGrVKIPDIVgiginSVVGF 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499392550 274 DNIELAE---YFSPPLTTIHQPKRRVGKNAFEILLERI-KDKEHDKRV 317
Cdd:pfam00532 224 DGLSKAQdtgLYLSPLTVIQLPRQLLGIKASDMVYQWIpKFREHPRVL 271
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
61-317 |
4.39e-25 |
|
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: 101.87 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDlTEELREMLDK--HA 138
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVD-SEALVPAVKKanAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 139 DIPkVIMDWGPISSQADKII----DNsEEGGYLATKYLID--NGHTKIACLSGHFEKAACQERIQGFKRAMKEANitlNN 212
Cdd:cd01536 80 GIP-VVAVDTDIDGGGDVVAfvgtDN-YEAGKLAGEYLAEalGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYP---DI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 213 EWILE--GNFECDTAV-MAADKIASWQDrPTAVFCFNDTMALGLMSRLQQLGLriPEDISVIGYDNIELA-------EYF 282
Cdd:cd01536 155 EIVAEqpANWDRAKALtVTENLLQANPD-IDAVFAANDDMALGAAEALKAAGR--TGDIKIVGVDGTPEAlkaikdgELD 231
|
250 260 270
....*....|....*....|....*....|....*
gi 499392550 283 SppltTIHQPKRRVGKNAFEILLERIKDKEHDKRV 317
Cdd:cd01536 232 A----TVAQDPYLQGYLAVEAAVKLLNGEKVPKEI 262
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
3-311 |
1.59e-24 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 101.49 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 3 TIKDVARLAGVSTTTVSHVIN---KTRFVAEATQEKVMKAVDELNYAPSAVARSLKCNTTRTIGMLVTQSTNLFFSEVID 79
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVINgkaKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 80 GVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILV-----MCSDLTEELREM------LDKHADIPKVImdwg 148
Cdd:PRK11303 82 YLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVstslpPEHPFYQRLQNDglpiiaLDRALDREHFT---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 149 pissqadKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNnewILEGN-F--ECDTA 225
Cdd:PRK11303 158 -------SVVSDDQDDAEMLAESLLKFPAESILLLGALPELSVSFEREQGFRQALKDDPREVH---YLYANsFerEAGAQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 226 VMAAdkiasWQDR---PTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKNAFE 302
Cdd:PRK11303 228 LFEK-----WLEThpmPDALFTTSYTLLQGVLDVLLERPGELPSDLAIATFGDNELLDFLPCPVNAVAQQHRLIAERALE 302
|
....*....
gi 499392550 303 ILLERIKDK 311
Cdd:PRK11303 303 LALAALDEP 311
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
61-317 |
7.66e-24 |
|
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: 98.43 E-value: 7.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREmLDKHADI 140
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYY-LCQAAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 141 PKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILEGNF 220
Cdd:cd06274 80 PVVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWILAEGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 221 ECDTAV-MAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNIELAEYFSPPLTTIHQPKRRVGKN 299
Cdd:cd06274 160 DRESGYqLMAELLARLGGLPQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDHDEIAEH 239
|
250
....*....|....*...
gi 499392550 300 AFEILLERIKDKEHDKRV 317
Cdd:cd06274 240 AFELLDALIEGQPEPGVI 257
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
108-327 |
4.40e-23 |
|
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: 96.12 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 108 IRMLAEKRVDGILVmcsDLTEELREMLDKHADIPKVIMDWGPISSQADKIIDNSEEGGYLATKYLIDNGHTKIACLsGHF 187
Cdd:cd01543 43 LDLLKGWKGDGIIA---RLDDPELAEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFC-GFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 188 EKAACQERIQGFKRAMKEANITLNnEWILEGNFECDTAVMAADKIASWQD---RPTAVFCFNDTMALGLMSRLQQLGLRI 264
Cdd:cd01543 119 NAAWSRERGEGFREALREAGYECH-VYESPPSGSSRSWEEEREELADWLKslpKPVGIFACNDDRARQVLEACREAGIRV 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499392550 265 PEDISVIGYDNIELAEYFS-PPLTTIHQPKRRVGKNAFEILLERIKDKEHDKRVFEMHP-ELVVR 327
Cdd:cd01543 198 PEEVAVLGVDNDELICELSsPPLSSIALDAEQIGYEAAELLDRLMRGERVPPEPILIPPlGVVTR 262
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
5-55 |
1.70e-20 |
|
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: 83.23 E-value: 1.70e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 499392550 5 KDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPSAVARSLK 55
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLR 51
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
3-48 |
9.01e-20 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 81.14 E-value: 9.01e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 499392550 3 TIKDVARLAGVSTTTVSHVINKTRFVAEATQEKVMKAVDELNYAPS 48
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
61-274 |
6.26e-19 |
|
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: 85.02 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDlTEELREMLD--KHA 138
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVD-SGGIVPAIEaaNEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 139 DIPKVIMDwgpISSQADKII-----DNsEEGGYLATKYL---IDNGHTKIACLsGHFEKAACQERIQGFKRAM-KEANIT 209
Cdd:cd06322 80 GIPVFTVD---VKADGAKVVthvgtDN-YAGGKLAGEYAlkaLLGGGGKIAII-DYPEVESVVLRVNGFKEAIkKYPNIE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499392550 210 LNNEwiLEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLriPEDISVIGYD 274
Cdd:cd06322 155 IVAE--QPGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGK--EDKIKVIGFD 215
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
62-312 |
1.79e-18 |
|
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: 83.51 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 62 IGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGI-YEKQRDYIRMLAEKRVDGILVMCSDLTEeLREMLDK--HA 138
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEAdAAEQVAQIEDAIAQGVDAIIVAPVDPTA-LAPVLKKakDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 139 DIPKVIMDWGPISS-QADKIIDNSEEGGYLATKYLID--NGHTKIACLSGHFEKAACQERIQGFKRAMKE--ANITLNNE 213
Cdd:pfam13407 80 GIPVVTFDSDAPSSpRLAYVGFDNEAAGEAAGELLAEalGGKGKVAILSGSPGDPNANERIDGFKKVLKEkyPGIKVVAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 214 WIlEGNFECDTAV-MAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRipEDISVIGYDNI-ELAEYFSPPL--TTI 289
Cdd:pfam13407 160 VE-GTNWDPEKAQqQMEALLTAYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATpEALEAIKDGTidATV 236
|
250 260
....*....|....*....|...
gi 499392550 290 HQPKRRVGKNAFEILLERIKDKE 312
Cdd:pfam13407 237 LQDPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
104-274 |
2.28e-15 |
|
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: 75.33 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 104 QRDYIRMLAE--------KRVDG-ILVMCSDLTEELREMLDKHAdIPKVIMDWGPISSQADK--------------IIDN 160
Cdd:cd06324 39 NRNRFKMLELaeellarpPKPDYlILVNEKGVAPELLELAEQAK-IPVFLINNDLTDEERALlgkprekfkywlgsIVPD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 161 SEEGGYLATKYLI-------DNGHTKIACLSGHFEKAACQERIQGFKRAMKEA-NITLNNewILEGNFECDTAVMAADKI 232
Cdd:cd06324 118 NEQAGYLLAKALIkaarkksDDGKIRVLAISGDKSTPASILREQGLRDALAEHpDVTLLQ--IVYANWSEDEAYQKTEKL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499392550 233 ASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYD 274
Cdd:cd06324 196 LQRYPDIDIVWAANDAMALGAIDALEEAGLKPGKDVLVGGID 237
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
61-332 |
5.31e-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: 74.18 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDlTEELREMLD--KHA 138
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPID-ATGWDPVLKeaKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 139 DIPKVIMDWGPISSQADKII-----DNSEEGgYLATKYLIDN---GHTKIACLSGHFEKAACQERIQGFKRAMKEA---N 207
Cdd:cd06309 80 GIPVILVDRTIDGEDGSLYVtfigsDFVEEG-RRAAEWLVKNykgGKGNVVELQGTAGSSVAIDRSKGFREVIKKHpniK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 208 ITLNNEwileGNFECDTAV-MAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRIPEDISVIGYDNI---------- 276
Cdd:cd06309 159 IVASQS----GNFTREKGQkVMENLLQAGPGDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQkdaleaikag 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499392550 277 ELAeyfsppLTTIHQPkrRVGKNAFEILLERIKDKEHDKRVFeMHPELVVRDTVKK 332
Cdd:cd06309 235 ELN------ATVECNP--LFGPTAFDTIAKLLAGEKVPKLII-VEERLFDKDNAAE 281
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
111-306 |
1.34e-14 |
|
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: 72.69 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 111 LAEKRVDGILVMCSDLTEELREMLDKHADIPKVIMDwgpISSQADK----------IIDNSEEGGYLATKYLIDNGHTKI 180
Cdd:cd01391 54 FIRDNIAGVIGPGSSSVAIVIQNLAQLFDIPQLALD---ATSQDLSdktlykyflsVVFSDTLGARLGLDIVKRKNWTYV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 181 ACLSGHfEKAACQERIQGFKRAMKEANITLNNEWILEGNFECDTAVMAADKIASwQDRPTAVFCFNDTMALGLMSRLQQL 260
Cdd:cd01391 131 AAIHGE-GLNSGELRMAGFKELAKQEGICIVASDKADWNAGEKGFDRALRKLRE-GLKARVIVCANDMTARGVLSAMRRL 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499392550 261 GLRipEDISVIGYDNIELA-----EYFSPPLTTIHQPKRRVGKNAFEILLE 306
Cdd:cd01391 209 GLV--GDVSVIGSDGWADRdevgyEVEANGLTTIKQQKMGFGITAIKAMAD 257
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
61-330 |
2.38e-14 |
|
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: 72.01 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLIlcntggIYEKQRDYIRM------LAEKRVDGILVMCSDlTEELREML 134
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFV------TYDQKNSANEQvtnandLIAQGVDGIIISPTN-SSAAPTVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 135 D--KHADIPKVIMDWGPISSQADKII--DNsEEGGYLATKYLID----NGHT--KIACLSGHFEKAACQERIQGFKRAMK 204
Cdd:cd06319 74 DlaNEAKIPVVIADIGTGGGDYVSYIisDN-YDGGYQAGEYLAEalkeNGWGggSVGIIAIPQSRVNGQARTAGFEDALE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 205 EANITLNNEwILEGNFECDTAVMAA-DKIASWQDRpTAVFCFNDTMALGLMSRLQQLGLRipEDISVIGYDNI-ELAEYF 282
Cdd:cd06319 153 EAGVEEVAL-RQTPNSTVEETYSAAqDLLAANPDI-KGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDGDpEALDLI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499392550 283 SPP--LTTIHQPKRRVGKNAFEILLERIKDKEHDKRVFEMHPELVVRDTV 330
Cdd:cd06319 229 KDGklDGTVAQQPFGMGARAVELAIQALNGDNTVEKEIYLPVLLVTSENV 278
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-279 |
2.49e-14 |
|
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: 71.90 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCY-RQGYTLILcNTGGI---YEKQRDYIRMLAEKRVDGILVMCSD---LTEELREM 133
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKeANGYELLV-KGIKQetdIEQQIAIVENLIAQKVDAIVIAPADskaLVPVLKKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 134 LDkhADIPKVIMDW---GPISSQADKII-----DNsEEGGYLATKYLIDN--GHTKIACLSGHFEKAACQERIQGFKRAM 203
Cdd:cd19970 80 VD--AGIAVINIDNrldADALKEGGINVpfvgpDN-RQGAYLAGDYLAKKlgKGGKVAIIEGIPGADNAQQRKAGFLKAF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499392550 204 KEANITLNNewILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRipEDISVIGYDNIELA 279
Cdd:cd19970 157 EEAGMKIVA--SQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFDNIPAV 228
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
61-277 |
5.47e-14 |
|
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: 70.79 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDlTEELREMLDK--HA 138
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTD-SDAVSPAVEEanEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 139 DIPKVIMDWgpiSSQADKII-----DNsEEGGYLATKYLID--NGHTKIACLSGHFEKAACQERIQGFKRAMKEA-NITL 210
Cdd:cd06323 80 GIPVITVDR---SVTGGKVVshiasDN-VAGGEMAAEYIAKklGGKGKVVELQGIPGTSAARERGKGFHNAIAKYpKINV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499392550 211 NNEwiLEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGlriPEDISVIGYDNIE 277
Cdd:cd06323 156 VAS--QTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGTP 217
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-274 |
9.52e-14 |
|
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: 70.31 E-value: 9.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDlTEELREMLD--KHA 138
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVD-SEGIRPALEaaKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 139 DIPKVIMDWGPI-SSQADKII--DNSeEGGYLATKYLIDN--GHTKIACLsgHFEKA-ACQERIQGFKRAMKEanitlNN 212
Cdd:cd19971 80 GIPVINVDTPVKdTDLVDSTIasDNY-NAGKLCGEDMVKKlpEGAKIAVL--DHPTAeSCVDRIDGFLDAIKK-----NP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499392550 213 EWILEGNFECDTAVMAADKIAS--WQDRP--TAVFCFNDTMALGLMSRLQQLGLriPEDISVIGYD 274
Cdd:cd19971 152 KFEVVAQQDGKGQLEVAMPIMEdiLQAHPdlDAVFALNDPSALGALAALKAAGK--LGDILVYGVD 215
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
61-333 |
1.55e-11 |
|
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: 63.93 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLD-KHAD 139
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRaSEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKV----IMDWGPISSQADkiIDNSEEG---GYLATKYLIDN--GHTKIACLsGHFEKAACQERIQGFKRAMKE-ANIT 209
Cdd:cd06317 81 IPVIaydaVIPSDFQAAQVG--VDNLEGGkeiGKYAADYIKAElgGQAKIGVV-GALSSLIQNQRQKGFEEALKAnPGVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 210 LNNEwiLEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRipEDISVIGYDNIElaEYFSPPL--- 286
Cdd:cd06317 158 IVAT--VDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQ--GKIKVFGWDLTK--QAIFLGIdeg 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499392550 287 ----TTIHQPKrRVGKNAFEILLERIKDKEHDKRVfEMHPELVVRDTVKKI 333
Cdd:cd06317 232 vlqaVVQQDPE-KMGYEAVKAAVKAIKGEDVEKTI-DVPPTIVTKENVDQF 280
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
102-274 |
1.10e-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: 61.02 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 102 EKQRDYIRMLAEKRVDGILVMCSD---LTEELREMLDkhADIPKVIMDWGPISSQADKII--DNSEEGgYLATKYLID-- 174
Cdd:cd06308 43 AKQIADIEDLIAQGVDLLIVSPNEadaLTPVVKKAYD--AGIPVIVLDRKVSGDDYTAFIgaDNVEIG-RQAGEYIAEll 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 175 NGHTKIACLSGHFEKAACQERIQGFKRAM-KEANITLNNEwiLEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGL 253
Cdd:cd06308 120 NGKGNVVEIQGLPGSSPAIDRHKGFLEAIaKYPGIKIVAS--QDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGA 197
|
170 180
....*....|....*....|.
gi 499392550 254 MSRLQQLGLRipEDISVIGYD 274
Cdd:cd06308 198 YQALKKAGRE--KEIKIIGVD 216
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
61-279 |
3.69e-10 |
|
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380481 [Multi-domain] Cd Length: 302 Bit Score: 59.91 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQG-YTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDlTEELREMLD--KH 137
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGkIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVD-RTAAQTIIDkaKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 138 ADIP----------KVIMDW------GPISS-----QADKIIDnseeggYLATKYLID-NGHTKIACL-----SGHFEKA 190
Cdd:cd01539 81 ANIPviffnrepsrEDLKSYdkayyvGTDAEesgimQGEIIAD------YWKANPEIDkNGDGKIQYVmlkgePGHQDAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 191 AcqeRIQGFKRAMKEANITLNnewILEGNFECDTAVMAADKIASWQDRPT----AVFCFNDTMALGLMSRLQQLGL---R 263
Cdd:cd01539 155 A---RTKYSVKTLNDAGIKTE---QLAEDTANWDRAQAKDKMDAWLSKYGdkieLVIANNDDMALGAIEALKAAGYntgD 228
|
250
....*....|....*.
gi 499392550 264 IPEDISVIGYDNIELA 279
Cdd:cd01539 229 GDKYIPVFGVDATPEA 244
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
61-325 |
4.69e-10 |
|
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: 59.22 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYC--YRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDlTEELREMLD--K 136
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAaeINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAAD-SAGIEPAIKraK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 137 HADIPKVIMDWGPISSQADKIIDNSEeGGYLATKYLID--NGHTKIACLSGHFEKAAcQERIQGFKRAMKEA-NITLNNe 213
Cdd:cd06321 80 DAGIIVVAVDVAAEGADATVTTDNVQ-AGYLACEYLVEqlGGKGKVAIIDGPPVSAV-IDRVNGCKEALAEYpGIKLVD- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 214 wILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRipeDISVIGYDN-----IELAEYFSPPLTT 288
Cdd:cd06321 157 -DQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRD---DIVITSVDGspeavAALKREGSPFIAT 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 499392550 289 IHQPKRRVGKNAFEILLERIKDKEHDKRVFEMHPELV 325
Cdd:cd06321 233 AAQDPYDMARKAVELALKILNGQEPAPELVLIPSTLV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-274 |
6.86e-10 |
|
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: 58.99 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREM-LDKHAD 139
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVkAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 140 IPKVIMDWGPISSQADKII--DNSEEGGYLATkYLID--NGHTKIACLSGHFEKAACQERIQGFKRAMKEA-NITLNNEW 214
Cdd:cd19972 81 IPVIAVDRNPEDAPGDTFIatDSVAAAKELGE-WVIKqtGGKGEIAILHGQLGTTPEVDRTKGFQEALAEApGIKVVAEQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 215 ilEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLriPEDISVIGYD 274
Cdd:cd19972 160 --TADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGL--DHKIWVVGFD 215
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
103-325 |
4.68e-09 |
|
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: 56.24 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 103 KQRDYIRMLAEKRVDGILVMCSD---LTEELREMLDkhADIPKVIMDWGPISSQ------ADKIidnseEGGYLATKYLI 173
Cdd:cd19968 43 KQASDLENAIAQGVDGIIVSPIDvkaLVPAIEAAIK--AGIPVVTVDRRAEGAApvphvgADNV-----AGGREVAKFVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 174 DN--GHTKIACLSGHFEKAACQERIQGFKRAM-KEANITLNNEWilEGNFECDTAV-MAADKIASWQDRPTAVFCFNDTM 249
Cdd:cd19968 116 DKlpNGAKVIELTGTPGSSPAIDRTKGFHEELaAGPKIKVVFEQ--TGNFERDEGLtVMENILTSLPGPPDAIICANDDM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 250 ALGLMSRLQQLGLRIpEDISVIGYDNI----------ELAeyfspplTTIHQPKRRVGKNAFEILLERIKDKEHDKRVfE 319
Cdd:cd19968 194 ALGAIEAMRAAGLDL-KKVKVIGFDAVpdalqaikdgELY-------ATVEQPPGGQARTALRILVDYLKDKKAPKKV-N 264
|
....*.
gi 499392550 320 MHPELV 325
Cdd:cd19968 265 LKPKLI 270
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
102-277 |
2.34e-08 |
|
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: 54.13 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 102 EKQRDYIRMLAEKRVDGILVMCSDlTEELREMLDKHAD--IPKVIMDwgpisSQADK------IIDNSEEGGYLATKYLI 173
Cdd:cd06314 43 AEQVQLIEDLIARGVDGIAISPND-PEAVTPVINKAADkgIPVITFD-----SDAPDskrlayIGTDNYEAGREAGELMK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 174 D--NGHTKIACLSGHFEKAACQERIQGFKRAMKEANitlNNEW--ILEGNFECDTAVMAADKIASWQDRPTAVFCFNDTM 249
Cdd:cd06314 117 KalPGGGKVAIITGGLGADNLNERIQGFKDALKGSP---GIEIvdPLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYN 193
|
170 180
....*....|....*....|....*...
gi 499392550 250 ALGLMSRLQQLGLRipEDISVIGYDNIE 277
Cdd:cd06314 194 GPAIAAALKDAGKV--GKVKIVGFDTLP 219
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
61-332 |
4.17e-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: 53.43 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVM------CSDLTEELREml 134
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVpvdadaLAPAVEKAKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 135 dkhADIPKVIMDWGPISSQADKIIDNSE-EGGYLATKYLID--NGHTKIACLSGHFEKAACQERIQGFKRAMKEA-NITL 210
Cdd:cd06313 79 ---AGIPLVGVNALIENEDLTAYVGSDDvVAGELEGQAVADrlGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYpDIKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 211 NNEwiLEGNFECDTAV-MAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLripEDISVIGYDNIELA-------EYf 282
Cdd:cd06313 156 LAE--QTANWSRDEAMsLMENWLQAYGDEIDGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDGIEDAlqavksgEL- 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499392550 283 sppLTTIHQPKRRVGKNAFEILLERIKDKEHDKRVfEMHPELVVRDTVKK 332
Cdd:cd06313 230 ---IATVLQDAEAQGKGAVEVAVDAVKGEGVEKKY-YIPFVLVTKDNVDD 275
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
241-327 |
1.87e-07 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 51.65 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 241 AVFCFNDTMALGLMSRLQQLGLRIPEDISVIG-YDNIElAEYFSPPLTTIHQPKRRVGKNAFEILLERIKDKEHDKRVFE 319
Cdd:cd06287 181 AVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTrYDGIR-ARTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSVEVGP 259
|
....*...
gi 499392550 320 MhPELVVR 327
Cdd:cd06287 260 A-PELVVR 266
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-274 |
1.90e-07 |
|
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: 51.57 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLIL--CNTGGIYEKQRDYIRMLAEKRVDGILVMCSDlTEELREMLDKHA 138
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFvgPESEEDVAGQNSLLEELINKKPDAIVVAPLD-SEDLVDPLKDAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 139 D--IPKVIMDWGPISSQADKII--DNSEeGGYLATKYLID--NGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNn 212
Cdd:cd06310 80 DkgIPVIVIDSGIKGDAYLSYIatDNYA-AGRLAAQKLAEalGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIK- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499392550 213 ewILEGNFECDTAVMAADKIASWQDR-PTA--VFCFNDTMALGLMSRLQQLGLRipEDISVIGYD 274
Cdd:cd06310 158 --VLASQYAGSDYAKAANETEDLLGKyPDIdgIFATNEITALGAAVAIKSRKLS--GQIKIVGFD 218
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-274 |
2.43e-07 |
|
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: 51.08 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLIL--CNTGGIYEKQRDYIRMLAEKRVDGILVMCSD---LTEELREMLD 135
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWrgPSREDDVEAQIQIIEYFIDQGVDGIVLAPLDrkaLVAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 136 khADIPKVIMDWGPissQADKII-----DNsEEGGYLATKYLID--NGHTKIACL---SGHfekAACQERIQGFKRAMKE 205
Cdd:cd20004 81 --QGIPVVIIDSDL---GGDAVIsfvatDN-YAAGRLAAKRMAKllNGKGKVALLrlaKGS---ASTTDRERGFLEALKK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499392550 206 ANitlNNEWILEGNF---ECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLriPEDISVIGYD 274
Cdd:cd20004 152 LA---PGLKVVDDQYaggTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGL--AGKVKFIGFD 218
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
62-318 |
6.64e-07 |
|
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: 49.95 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 62 IGMLVTQSTNLFFSEVIDGVESYCYRQG--YTLILCNTGGIYEKQRDYIRMLAEKRVDGILVM---CSDLTEELREMLDK 136
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGvkVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSpisDTNLIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 137 HadIPKVIMDWGPISSQADKI---------IDNSEEGGyLATKYLIDN--GHTKIACLSGHFEKAACQERIQGFKRAMKe 205
Cdd:cd06320 82 G--IPVINLDDAVDADALKKAggkvtsfigTDNVAAGA-LAAEYIAEKlpGGGKVAIIEGLPGNAAAEARTKGFKETFK- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 206 ANITLNNEWILEGNFECDTAVMAADKIAswQDRP--TAVFCFNDTMALGLMSRLQQLGLRipEDISVIGYDNIELA--EY 281
Cdd:cd06320 158 KAPGLKLVASQPADWDRTKALDAATAIL--QAHPdlKGIYAANDTMALGAVEAVKAAGKT--GKVLVVGTDGIPEAkkSI 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 499392550 282 FSPPLT-TIHQPKRRVGKNAFEILLERIKDKEHDKRVF 318
Cdd:cd06320 234 KAGELTaTVAQYPYLEGAMAVEAALRLLQGQKVPAVVA 271
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-275 |
9.48e-07 |
|
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: 49.54 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGMLVTQSTNLFFSEVIDGVESYCYRQGYTLILcnTGGIYE----KQRDYIRMLAEKRVDGILVMCSDltEELREMLDK 136
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTF--LGPATEadiaGQVNLVENAISRKPDAIVLAPND--TAALVPAVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 137 HAD--IPKVIMDWGPISSQADKII--DNsEEGGYLATKYLID------NGHTKIACLSGHFEKAACQERIQGFKRAMKEa 206
Cdd:cd20008 77 AADagIPVVLVDSGANTDDYDAFLatDN-VAAGALAADELAEllkasgGGKGKVAIISFQAGSQTLVDREEGFRDYIKE- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499392550 207 nitlNNEWI-LEGNFECDTAVMAADKIAswQDRPTA------VFCFNDTMALGLMSRLQQLGLRipEDISVIGYDN 275
Cdd:cd20008 155 ----KYPDIeIVDVQYSDGDIAKALNQT--TDLLTAnpdlvgIFGANNPSAVGVAQALAEAGKA--GKIVLVGFDS 222
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
73-275 |
1.78e-06 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380621 [Multi-domain] Cd Length: 278 Bit Score: 48.86 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 73 FFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEELREMLD--KHADIPKVIMDwGPI 150
Cdd:cd19966 14 FWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTPLIEaaKKAGIIVTSFN-TDL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 151 SSQADK------IIDNSEEGGYLATKYLIDNGHTKiaclSGHF--------EKAACQERIQGFKRAMKEANITLNnewIL 216
Cdd:cd19966 93 PKLEYGdcglgyVGADLYAAGYTLAKELVKRGGLK----TGDRvfvpgllpGQPYRVLRTKGVIDALKEAGIKVD---YL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499392550 217 EGNFECDTAVMAADKIASW---QDRPTAVFCFNDTMALGLMSRLQQLGLRiPEDISVIGYDN 275
Cdd:cd19966 166 EISLEPNKPAEGIPVMTGYlaaNPDVKAIVGDGGGLTANVAKYLKAAGKK-PGEIPVAGFDL 226
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
73-328 |
2.85e-06 |
|
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: 48.18 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 73 FFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDlTEELREMLDKHAD--IPKVIMD---- 146
Cdd:cd06318 13 YYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVD-PEGLTPAVKAAKAagIPVITVDsald 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 147 -WGPISSQADKiiDNSeEGGYLATKYLID---NGHTKIACLSGHFEKAACQERIQGFKRAMKEANITLNNEWILE----- 217
Cdd:cd06318 92 pSANVATQVGR--DNK-QNGVLVGKEAAKalgGDPGKIIELSGDKGNEVSRDRRDGFLAGVNEYQLRKYGKSNIKvvaqp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 218 -GNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGLMSRLQQLGLRipEDISVIGYDN-------IELAEYFSpplTTI 289
Cdd:cd06318 169 yGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGML--DKVKVAGADGqkealklIKDGKYVA---TGL 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 499392550 290 HQPkRRVGKNAFEILLERIKDKEHDKRVFEMHPELVVRD 328
Cdd:cd06318 244 NDP-DLLGKTAVDTAAKVVKGEESFPEFTYTPTALITKD 281
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
101-280 |
3.81e-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: 380661 [Multi-domain] Cd Length: 274 Bit Score: 47.59 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 101 YEKQRDYIRMLAEKRVDGILVMCSD---LTEELREMLDKHadIPKVIMDWGPISSQADKII--DNSEEGGYLATK--YLI 173
Cdd:cd20006 45 IDGQIELIEEAIAQKPDAIVLAASDydrLVEAVERAKKAG--IPVITIDSPVNSKKADSFVatDNYEAGKKAGEKlaSLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 174 DNGhTKIACLSghFEK--AACQERIQGFKRAMKEA-NITLNNEWILEGNFE--CDTAVMAADKiaswQDRPTAVFCFNDT 248
Cdd:cd20006 123 GEK-GKVAIVS--FVKgsSTAIEREEGFKQALAEYpNIKIVETEYCDSDEEkaYEITKELLSK----YPDINGIVALNEQ 195
|
170 180 190
....*....|....*....|....*....|....*.
gi 499392550 249 MALGLMSRLQQLGLRipEDISVIGYDN----IELAE 280
Cdd:cd20006 196 STLGAARALKELGLG--GKVKVVGFDSsveeIQLLE 229
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
62-327 |
1.04e-05 |
|
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: 46.40 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 62 IGMLVTQSTNLFFSEVIDGVEsycyRQGYTL--------ILCNTGGIYEKQRDYIRMLAEkRVDGILVMCSDlTEELREM 133
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIE----AAAAALrdrrvrlrIHFVDSLDPEALAAALRRLAA-GCDGVALVAPD-HPLVRAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 134 LDK--HADIPKVIMdwgpIS--SQADKI----IDNSEEG---GYLATKYLIDNGHtKIACLSGHFEKAACQERIQGFKRA 202
Cdd:cd06307 76 IDElaARGIPVVTL----VSdlPGSRRLayvgIDNRAAGrtaAWLMGRFLGRRPG-KVLVILGSHRFRGHEEREAGFRSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 203 MKEANITLNNEWILEGNfECDTAV--MAADKIASWQDrPTAVFCFNDTMAlGLMSRLQQLGLriPEDISVIGYDnielae 280
Cdd:cd06307 151 LRERFPDLTVLEVLEGL-DDDELAyeLLRELLARHPD-LVGIYNAGGGNE-GIARALREAGR--ARRVVFIGHE------ 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499392550 281 yfsppLT--------------TIHQPKRRVGKNAFEILLERIKDKEHDKRVFEMHPELVVR 327
Cdd:cd06307 220 -----LTpetrrllrdgtidaVIDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEIITR 275
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
71-315 |
3.61e-05 |
|
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: 44.62 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 71 NLFFSEVIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSDLTEEL---REMldKHADIPKVIMDW 147
Cdd:cd19967 11 NPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIaavKKA--KDAGIPVFLIDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 148 G---PISSQAdKIIDNSEEGGYLATKYLID--NGHTKIACLSGHFEKAACQERIQGF----------KRAMKEanitlNN 212
Cdd:cd19967 89 EinaEGVAVA-QIVSDNYQGAVLLAQYFVKlmGEKGLYVELLGKESDTNAQLRSQGFhsvidqypelKMVAQQ-----SA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 213 EWILEGNFECDTAVMAADKiaswqdRPTAVFCFNDTMALGLMSRLQQLGlrIPEDISVIGYD------NIELAEYFSppl 286
Cdd:cd19967 163 DWDRTEAFEKMESILQANP------DIKGVICGNDEMALGAIAALKAAG--RAGDVIIVGFDgsndvrDAIKEGKIS--- 231
|
250 260
....*....|....*....|....*....
gi 499392550 287 TTIHQPKRRVGKNAFEILLERIKDKEHDK 315
Cdd:cd19967 232 ATVLQPAKLIARLAVEQADQYLKGGSTGK 260
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
110-274 |
6.74e-05 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380662 [Multi-domain] Cd Length: 271 Bit Score: 43.77 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 110 MLAeKRVDGILVMCSD---LTEELREMLDkhADIPKVIMDwgpiSSQADK------IIDNSEEGGYLATKYLID--NGHT 178
Cdd:cd20007 52 VIA-KKPDALLIAPTDpqaLIAPLKRAAD--AGIKVVTVD----TTLGDPsfvlsqIASDNVAGGALAAEALAEliGGKG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 179 KIACLSGHFEKAACQERIQGFKRAMKEA-NITLnnewiLEGNFECDTAVMAADKI-ASWQDRP--TAVFCFNDTMALGLM 254
Cdd:cd20007 125 KVLVINSTPGVSTTDARVKGFAEEMKKYpGIKV-----LGVQYSENDPAKAASIVaAALQANPdlAGIFGTNTFSAEGAA 199
|
170 180
....*....|....*....|
gi 499392550 255 SRLQQLGLRipEDISVIGYD 274
Cdd:cd20007 200 AALRNAGKT--GKVKVVGFD 217
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
61-274 |
1.07e-04 |
|
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: 43.05 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 61 TIGmLVTQSTNLFFSE-VIDGVESYCYRQGYTLILCNTGGIYEKQRDYIRMLAEKRVDGILVMCSD---LTEELREMLDk 136
Cdd:cd06305 1 TIA-VVRNGTSGDWDQqALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDadaLDPKLKKALD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 137 hADIPKVIMDWGPISSQADKIIDNSEEGGYLATKYLID--NGHTKIACLSGhFEKAACQERIQGFKRAMKEaniTLNNEW 214
Cdd:cd06305 79 -AGIPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKdlNGEGNIAVFNV-FGVPPLDKRYDIYKAVLKA---NPGIKK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499392550 215 ILE------GNFECDTAVMAADKIASWQD-RPTAVFCFNDTMALGLMSRLQQLGLripEDISVIGYD 274
Cdd:cd06305 154 IVAelgdvtPNTAADAQTQVEALLKKYPEgGIDAIWAAWDEPAKGAVQALEEAGR---TDIKVYGVD 217
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
95-274 |
1.42e-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: 380660 [Multi-domain] Cd Length: 274 Bit Score: 43.00 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 95 CNTGGIYEKQRDYIRMLAEKRVDGILVMCSDlTEELREMLD--KHADIPKVIMDWG-----PISSQAdkiIDNSEEGGYL 167
Cdd:cd20005 37 PDTESDVDKQIEMLDNAIAKKPDAIALAALD-TNALLPQLEkaKEKGIPVVTFDSGvpsdlPLATVA---TDNYAAGALA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 168 ATKY--LIDnGHTKIACLSGHFEKAACQERIQGFKRAMKEaNITlNNEwILEGNFECDTAVMAADKIASW-QDRP--TAV 242
Cdd:cd20005 113 ADHLaeLIG-GKGKVAIVAHDATSETGIDRRDGFKDEIKE-KYP-DIK-VVNVQYGVGDHAKAADIAKAIlQANPdlKGI 188
|
170 180 190
....*....|....*....|....*....|..
gi 499392550 243 FCFNDTMALGLMSRLQQLGLRipEDISVIGYD 274
Cdd:cd20005 189 YATNEGAAIGVANALKEMGKL--GKIKVVGFD 218
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
114-275 |
2.14e-04 |
|
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: 42.32 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 114 KRVDGILVMCSDlTEELREMLDK--HADIPKVIMDWGPISSQADKII--DNSEEGGYLAtKYLID--NGHTKIACLSG-- 185
Cdd:cd19969 55 KNPDGIAVSAID-PEALTPTINKavDAGIPVVTFDSDAPESKRISYVgtDNYEAGYAAA-EKLAEllGGKGKVAVLTGpg 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 186 ---HfekaacQERIQGFKRAMKE-ANItlnnEWILEGNFECDtaVMAADKIAS--WQDRP--TAVFCFNDTMALGLMSRL 257
Cdd:cd19969 133 qpnH------EERVEGFKEAFAEyPGI----EVVAVGDDNDD--PEKAAQNTSalLQAHPdlVGIFGVDASGGVGAAQAV 200
|
170
....*....|....*...
gi 499392550 258 QQLGLRIpeDISVIGYDN 275
Cdd:cd19969 201 REAGKTG--KVKIVAFDD 216
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
102-276 |
3.22e-04 |
|
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: 41.83 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 102 EKQRDYIRMLAEKRVDGILVMCSDlTEELREMLD--KHADIPKVIMDWGPISSQADK--IIDNSEEGGYLATKYLID--N 175
Cdd:cd06301 44 AKQLSQVENFIAQGVDAIIVNPVD-TDASAPAVDaaADAGIPLVYVNREPDSKPKGVafVGSDDIESGELQMEYLAKllG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 176 GHTKIACLSGHFEKAACQERIQGFKRAMKE-ANITLnnewilegnfecdtavmAADKIASWQ---------------DRP 239
Cdd:cd06301 123 GKGNIAILDGVLGHEAQILRTEGNKDVLAKyPGMKI-----------------VAEQTANWSrekamdivenwlqsgDKI 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 499392550 240 TAVFCFNDTMALGLMSRLQQLGLRipEDISVIGYDNI 276
Cdd:cd06301 186 DAIVANNDEMAIGAILALEAAGKK--DDILVAGIDAT 220
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
102-261 |
7.25e-04 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 40.81 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 102 EKQRDYIRMLAEKRVDGILVMCSD---LTEELREMLDkhADIPKVIMDWGPISSQADKIIDNSEEG-GYLATKYLID--N 175
Cdd:cd06311 42 NEQVSQLEDLIAQKVDAIVILPQDseeLTVAAQKAKD--AGIPVVNFDRGLNVLIYDLYVAGDNPGmGVVSAEYIGKklG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 176 GHTKIACLSGHFEKAACQERIQGFKRAMKEA--NITLNNEwilEGNFECDTAVMAADKIASWQDRPTAVFCFNDTMALGL 253
Cdd:cd06311 120 GKGNVVVLEVPSSGSVNEERVAGFKEVIKGNpgIKILAMQ---AGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGV 196
|
....*...
gi 499392550 254 MSRLQQLG 261
Cdd:cd06311 197 LQAIKEAG 204
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
97-211 |
1.07e-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: 380535 [Multi-domain] Cd Length: 272 Bit Score: 40.29 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499392550 97 TGGIYEKQRDYIRMLAEKRVDGILVMCSD---LTEELREMLDKHadIPKVIMDWGPISSQADK-----IIDNSEEGGYLA 168
Cdd:cd06312 39 QNNDIADQARLIEQAIAAKPDGIIVTIPDpdaLEPALKRAVAAG--IPVIAINSGDDRSKERLgaltyVGQDEYLAGQAA 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 499392550 169 TKYLIDNGHTKIACLSgHFEKAACQE-RIQGFKRAMKEANITLN 211
Cdd:cd06312 117 GERALEAGPKNALCVN-HEPGNPGLEaRCKGFADAFKGAGILVE 159
|
|
| |
