|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
1-329 |
1.07e-154 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 437.27 E-value: 1.07e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 1 MATIKDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVKA 80
Cdd:PRK10727 1 MATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 81 VDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKGLVLINRYIAEIANHCIFLDN 160
Cdd:PRK10727 81 VEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASLMKQIPGMVLINRILPGFENRCIALDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 161 KKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTNLLTKSLPITG 240
Cdd:PRK10727 161 RYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRGRNFTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 241 IVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGENTSTEPMMFS 320
Cdd:PRK10727 241 VACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADNRPLPEITNVFS 320
|
....*....
gi 515634216 321 PTLVRRNSV 329
Cdd:PRK10727 321 PTLVRRHSV 329
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
1-329 |
5.39e-143 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 407.63 E-value: 5.39e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 1 MATIKDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVKA 80
Cdd:PRK10401 1 MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 81 VDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKGLVLINRYIAEIANHCIFLDN 160
Cdd:PRK10401 81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 161 KKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTNLLTKSLPITG 240
Cdd:PRK10401 161 VSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLQLTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 241 IVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGENTSTEPMMFS 320
Cdd:PRK10401 241 VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNLDPRASHCFM 320
|
....*....
gi 515634216 321 PTLVRRNSV 329
Cdd:PRK10401 321 PTLVRRHSV 329
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
61-327 |
6.70e-131 |
|
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: 373.78 E-value: 6.70e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPT 220
Cdd:cd06270 81 LVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGDFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 221 SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKAT 300
Cdd:cd06270 161 IEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQAAA 240
|
250 260
....*....|....*....|....*..
gi 515634216 301 RLALHLAKGEnTSTEPMMFSPTLVRRN 327
Cdd:cd06270 241 ELALNLAYGE-PLPISHEFTPTLIERD 266
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-329 |
3.86e-130 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 374.54 E-value: 3.86e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 1 MATIKDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVKA 80
Cdd:COG1609 3 RVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 81 VDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKGLVLINRYIAEIANHCIFLDN 160
Cdd:COG1609 83 IEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGVDN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 161 KKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTNLLTKSLPITG 240
Cdd:COG1609 163 RAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPTA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 241 IVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGENTSTEPMMFS 320
Cdd:COG1609 243 IFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLLP 322
|
....*....
gi 515634216 321 PTLVRRNSV 329
Cdd:COG1609 323 PELVVREST 331
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
61-324 |
6.79e-90 |
|
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: 269.77 E-value: 6.79e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPT 220
Cdd:cd06267 81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 221 SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKAT 300
Cdd:cd06267 161 EESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAAA 240
|
250 260
....*....|....*....|....
gi 515634216 301 RLALHLAKGENTSTEPMMFSPTLV 324
Cdd:cd06267 241 ELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
61-328 |
3.55e-76 |
|
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: 234.84 E-value: 3.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAY-AKEVK 139
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLlKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 140 GLVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAP 219
Cdd:cd19976 81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 220 TSDGGeYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKA 299
Cdd:cd19976 161 SLEGG-YKAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQEA 239
|
250 260
....*....|....*....|....*....
gi 515634216 300 TRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd19976 240 AKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
61-328 |
1.46e-74 |
|
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: 230.48 E-value: 1.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVkg 140
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYKKLNIPI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 lVLINRYIAEiANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPT 220
Cdd:cd06291 79 -VSIDRYLSE-GIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 221 SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKAT 300
Cdd:cd06291 157 EEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEAV 236
|
250 260
....*....|....*....|....*...
gi 515634216 301 RLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd06291 237 ELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-328 |
4.16e-67 |
|
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: 211.32 E-value: 4.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSkGLTDEELIAYAKEVKG 140
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVG-GFGDEELLKLLAEGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPT 220
Cdd:cd06290 80 VVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 221 SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKAT 300
Cdd:cd06290 160 EESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTAA 239
|
250 260
....*....|....*....|....*...
gi 515634216 301 RLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd06290 240 EILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
61-328 |
8.23e-67 |
|
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: 210.87 E-value: 8.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDI-SDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVK 139
Cdd:cd06288 1 TIGLITDDIaTTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLPPELTDIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 140 gLVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAP 219
Cdd:cd06288 81 -LVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHGDW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 220 TSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKA 299
Cdd:cd06288 160 GRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGRRA 239
|
250 260
....*....|....*....|....*....
gi 515634216 300 TRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd06288 240 AELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
1.99e-66 |
|
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: 209.77 E-value: 1.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPT 220
Cdd:cd06285 81 VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGGFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 221 SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKAT 300
Cdd:cd06285 161 IEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRAA 240
|
250 260
....*....|....*....|....*....
gi 515634216 301 RLALHLAKGENTSTEPMMFSPTLVRRNSV 329
Cdd:cd06285 241 ELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
61-328 |
9.34e-66 |
|
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: 208.16 E-value: 9.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKg 140
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELSKRYP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPT 220
Cdd:cd06284 80 IVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGDFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 221 SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKAT 300
Cdd:cd06284 160 FEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAA 239
|
250 260
....*....|....*....|....*...
gi 515634216 301 RLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd06284 240 ELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
61-324 |
3.07e-65 |
|
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: 206.61 E-value: 3.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSkglTDEELIAYAKEVKG 140
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAP---TGGNEDLIEKLVKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 ---LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEyS 217
Cdd:cd19977 78 gipVVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEELIK-H 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 218 APTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAE 297
Cdd:cd19977 157 VDRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGR 236
|
250 260
....*....|....*....|....*...
gi 515634216 298 KATRLALH-LAKGENTSTEPMMFSPTLV 324
Cdd:cd19977 237 KAAELLLDrIENKPKGPPRQIVLPTELI 264
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
61-328 |
1.15e-63 |
|
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: 202.79 E-value: 1.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKNMNIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACI-ASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAP 219
Cdd:cd19975 81 VVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMIsGPLDDPNAGYPRYEGYKKALKDAGLPIKENLIVEGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 220 TSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKA 299
Cdd:cd19975 161 SFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMGKKA 240
|
250 260
....*....|....*....|....*....
gi 515634216 300 TRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd19975 241 VELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
61-328 |
1.68e-63 |
|
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: 202.49 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLT--DEELIAYAKEV 138
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTddDAELLAALRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 139 KgLVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSA 218
Cdd:cd06275 81 P-VVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 219 PTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEK 298
Cdd:cd06275 160 FEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGEL 239
|
250 260 270
....*....|....*....|....*....|..
gi 515634216 299 ATRLAlhLAKGENTSTEP--MMFSPTLVRRNS 328
Cdd:cd06275 240 AVELL--LDRIENKREEPqsIVLEPELIERES 269
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
1-329 |
4.21e-62 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 201.11 E-value: 4.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 1 MATIKDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVKA 80
Cdd:PRK10703 1 MATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 81 VDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELiayakevkGLVLINRYIAEI--------A 152
Cdd:PRK10703 81 VEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLL--------AMLEEYRHIPMVvmdwgeakA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 153 NHC-IFLDNK-KGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTN 230
Cdd:PRK10703 153 DFTdAIIDNAfEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 231 LLT-KSLPiTGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKG 309
Cdd:PRK10703 233 ILSqKHRP-TAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVN 311
|
330 340
....*....|....*....|
gi 515634216 310 ENTSTEPMMFSPTLVRRNSV 329
Cdd:PRK10703 312 KREEPQTIEVHPRLVERRSV 331
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
61-328 |
4.15e-57 |
|
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380515 [Multi-domain] Cd Length: 273 Bit Score: 185.93 E-value: 4.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLV----GDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIhSKGLTDEELIAYAK 136
Cdd:cd06292 1 LIGYVVpelpGGFSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVL-ASTRHDDPRVRYLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 137 EvKGL--VLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYI 214
Cdd:cd06292 80 E-AGVpfVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 215 EYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQM 294
Cdd:cd06292 159 VEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDE 238
|
250 260 270
....*....|....*....|....*....|....
gi 515634216 295 MAEKATRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd06292 239 IGRAVVDLLLAAIEGNPSEPREILLQPELVVRES 272
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
61-326 |
7.97e-57 |
|
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380503 [Multi-domain] Cd Length: 266 Bit Score: 185.15 E-value: 7.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVI-HSKGLTDEELIAYAKEVK 139
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILaPSAGPSRELKRLLKHGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 140 gLVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAP 219
Cdd:cd06280 81 -IVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 220 TSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKA 299
Cdd:cd06280 160 TIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIA 239
|
250 260
....*....|....*....|....*..
gi 515634216 300 TRLALHLAKGENTSTEPMMFSPTLVRR 326
Cdd:cd06280 240 AQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
61-328 |
1.96e-56 |
|
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: 184.30 E-value: 1.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREE-ERQAIELLINSRCDALVI---HSkglTDEELIAYAK 136
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVEPCDSDDEDlADRLRRFLSRSRPDGVILtppLS---DDPALLDALD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 137 EVKG-LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIE 215
Cdd:cd01545 78 ELGIpYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPDLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 216 YSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMM 295
Cdd:cd01545 158 QGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAEM 237
|
250 260 270
....*....|....*....|....*....|...
gi 515634216 296 AEKATRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd01545 238 ARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
4-329 |
3.59e-56 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 185.29 E-value: 3.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 4 IKDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVKAVDN 83
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 84 VARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSkglTDEELIAyaKEVkglvlINRYIA-----------EIA 152
Cdd:PRK10423 81 SCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLC---TETHQPS--REI-----MQRYPSvptvmmdwapfDGD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 153 NHCIfLDNK-KGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTNL 231
Cdd:PRK10423 151 SDLI-QDNSlLGGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 232 LTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGEN 311
Cdd:PRK10423 230 LALPLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPT 309
|
330
....*....|....*...
gi 515634216 312 TSTEPMMFSPTLVRRNSV 329
Cdd:PRK10423 310 LQQQRLQLTPELMERGSV 327
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
61-326 |
1.15e-55 |
|
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: 181.99 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIH-SKGLTDEELIAYAKEVK 139
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSpAAGTTAELLRRLKAWGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 140 GLVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAP 219
Cdd:cd06289 81 PVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVPGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 220 TSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKA 299
Cdd:cd06289 161 TREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRRA 240
|
250 260
....*....|....*....|....*..
gi 515634216 300 TRLALHLAKGENTSTEPMMFSPTLVRR 326
Cdd:cd06289 241 ARLLLRRIEGPDTPPERIIIEPRLVVR 267
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
61-328 |
2.60e-55 |
|
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: 181.22 E-value: 2.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIH-SK-GLTDEELIAYAK-E 137
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEpTKsALPNPNLDLYEElQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 138 VKG--LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEdADERIQGYLAALSDYKIALSDSYIE 215
Cdd:cd01541 81 KKGipVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIFKSDDLQ-GVERYQGFIKALREAGLPIDDDRIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 216 -YSAPT--SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPI 292
Cdd:cd01541 160 wYSTEDleDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSVVHPK 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 515634216 293 QMMAEKATRLALHLAKGENTStEPMMFSPTLVRRNS 328
Cdd:cd01541 240 EELGRKAAELLLRMIEEGRKP-ESVIFPPELIERES 274
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-328 |
3.10e-54 |
|
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: 178.62 E-value: 3.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPT 220
Cdd:cd06293 81 VVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEVVRELSAPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 221 S--DGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEK 298
Cdd:cd06293 161 AnaELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELGRA 240
|
250 260 270
....*....|....*....|....*....|
gi 515634216 299 ATRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd06293 241 AADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
61-326 |
4.84e-52 |
|
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: 172.73 E-value: 4.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKevKG 140
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDWEVIEPYAK--YG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 -LVLINRYIAEIAnHCIFLDNKKGAYLATEYLIRHGHKNIACI------ASSHSIEdadeRIQGYLAALSDYKIALSDSY 213
Cdd:cd06286 79 pIVLCEETDSPDI-PSVYIDRYEAYLEALEYLKEKGHRKIGYClgrpesSSASTQA----RLKAYQDVLGEHGLSLREEW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 214 IEYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHpkLTTIRYPIQ 293
Cdd:cd06286 154 IFTNCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISELLN--LTTIDQPLE 231
|
250 260 270
....*....|....*....|....*....|...
gi 515634216 294 MMAEKATRLALHLAKGENTSTEPMmfSPTLVRR 326
Cdd:cd06286 232 EMGKEAFELLLSQLESKEPTKKEL--PSKLIER 262
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
27-329 |
2.33e-51 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 172.10 E-value: 2.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 27 KASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQ 106
Cdd:PRK11041 3 KVSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 107 AIELLINSRCDALVIHSKGLTDEELIAYAKEVKGLVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSH 186
Cdd:PRK11041 83 FVNLIITKQIDGMLLLGSRLPFDASKEEQRNLPPMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIAGPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 187 SIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDK 266
Cdd:PRK11041 163 EMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGLRVPQD 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515634216 267 MSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGENTSTEPMMFSPTLVRRNSV 329
Cdd:PRK11041 243 LSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-328 |
4.55e-49 |
|
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: 165.01 E-value: 4.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERqAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDD-ALRQLLQYRVDGVIVTSATLSSELAEECARRGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDsyIEYSAPT 220
Cdd:cd06278 80 VVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPPPA--VEAGDYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 221 SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVL-DENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKA 299
Cdd:cd06278 158 YEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVGFDDIPMAAWPSYDLTTVRQPIEEMAEAA 237
|
250 260
....*....|....*....|....*....
gi 515634216 300 TRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd06278 238 VDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
2-329 |
4.15e-48 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 164.78 E-value: 4.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 2 ATIKDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVKAV 81
Cdd:PRK09526 6 VTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQIAAAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 82 DNVARENGKHILVGN-GSHDREEERQAIELLINSRCDALVIhSKGLTDEELIAYAkevkglvlinryiAEIAN-HCIFLD 159
Cdd:PRK09526 86 KSRADQLGYSVVISMvERSGVEACQAAVNELLAQRVSGVII-NVPLEDADAEKIV-------------ADCADvPCLFLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 160 -------------NKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIA-LSDSYIEYSAptSDGGE 225
Cdd:PRK09526 152 vspqspvnsvsfdPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQpIAVREGDWSA--MSGYQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 226 YAMTnLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALH 305
Cdd:PRK09526 230 QTLQ-MLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLA 308
|
330 340
....*....|....*....|....
gi 515634216 306 LAKGENTSTePMMFSPTLVRRNSV 329
Cdd:PRK09526 309 LSQGQAVKG-SQLLPTSLVVRKST 331
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
2-327 |
1.57e-47 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 163.34 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 2 ATIKDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVKAV 81
Cdd:PRK10014 7 ITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 82 DNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEvKGLVLINRYIAEIANHCIFL--D 159
Cdd:PRK10014 87 TEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMAEE-KGIPVVFASRASYLDDVDTVrpD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 160 NKKGAYLATEYLIRHGHKNIACI-ASSHSIEDAdERIQGYLAALSDYKIAL-SDSYIEYSAPTSDGGEyAMTNLLTKSLP 237
Cdd:PRK10014 166 NMQAAQLLTEHLIRNGHQRIAWLgGQSSSLTRA-ERVGGYCATLLKFGLPFhSEWVLECTSSQKQAAE-AITALLRHNPT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 238 ITGIVAYNDYMAAGALSVLDENGIQAPD---------KMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAK 308
Cdd:PRK10014 244 ISAVVCYNETIAMGAWFGLLRAGRQSGEsgvdryfeqQVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRMMQRIT 323
|
330
....*....|....*....
gi 515634216 309 GENTSTEPMMFSPTLVRRN 327
Cdd:PRK10014 324 HEETHSRNLIIPPRLIARK 342
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
61-328 |
5.21e-46 |
|
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: 157.05 E-value: 5.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIAQGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHCIFL-DNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAP 219
Cdd:cd06299 81 VVFVDREVEGLGGVPVVTsDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 220 TSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKA 299
Cdd:cd06299 161 RQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRRA 240
|
250 260
....*....|....*....|....*....
gi 515634216 300 TRLALHLAKGeNTSTEPMMFSPTLVRRNS 328
Cdd:cd06299 241 VELLLALIEN-GGRATSIRVPTELIPRES 268
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
61-328 |
1.62e-45 |
|
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: 155.82 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGN-GSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVK 139
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATvDEDDPASVREALDRLLSQRVDGIIVIAPDEAVLEALRRLPPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 140 GLVLINRYIAEIANHcIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYkiALSDSYIEYSAP 219
Cdd:cd01574 81 PVVIVGSGPSPGVPT-VSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEA--GLPPPPVVEGDW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 220 TSDGGeYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKA 299
Cdd:cd01574 158 SAASG-YRAGRRLLDDGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRRA 236
|
250 260
....*....|....*....|....*....
gi 515634216 300 TRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd01574 237 VELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
69-328 |
8.43e-44 |
|
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: 151.52 E-value: 8.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 69 ISDPFFGTLVKAVDNVARENGKHILvgngshdREEERQAIELLINSRCDALVIHSKgLTDEELIAYAKEVKGLVLINRYI 148
Cdd:cd01544 14 LEDPYYLSIRLGIEKEAKKLGYEIK-------TIFRDDEDLESLLEKVDGIIAIGK-FSKEEIEKLKKLNPNIVFVDSNP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 149 AEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIA-----SSHSIEDADERIQGYLAALSDYKIaLSDSYIEYSAPTSDG 223
Cdd:cd01544 86 DPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGgkeytSDDGEEIEDPRLRAFREYMKEKGL-YNEEYIYIGEFSVES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 224 GEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLA 303
Cdd:cd01544 165 GYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLL 244
|
250 260
....*....|....*....|....*
gi 515634216 304 LHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd01544 245 LERINGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-328 |
9.59e-44 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 151.62 E-value: 9.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 70 SDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLiNSRCDALVIHSKGLTDEELIAYAKEVKGLVLINRYIA 149
Cdd:cd06277 17 ETPFFSELIDGIEREARKYGYNLLISSVDIGDDFDEILKELT-DDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNYFE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 150 EIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMT 229
Cdd:cd06277 96 DLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEPEFVVSVGPEGAYKDMK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 230 NLLTKS--LPiTGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLA 307
Cdd:cd06277 176 ALLDTGpkLP-TAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKI 254
|
250 260
....*....|....*....|.
gi 515634216 308 KGENTSTEPMMFSPTLVRRNS 328
Cdd:cd06277 255 KDPDGGTLKILVSTKLVERGS 275
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
61-318 |
1.66e-43 |
|
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: 150.34 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEeLIAYAKEVKG 140
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDE-HRKALKKLKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 -LVLINRYIAEIanHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHsiEDAD---ERIQGYLAALSDYKIALSDSYI-E 215
Cdd:cd01542 80 pVVVLGQEHEGF--SCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDE--EDIAvgvARKQGYLDALKEHGIDEVEIVEtD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 216 YSAPTSdggeYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMM 295
Cdd:cd01542 156 FSMESG----YEAAKELLKENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEA 231
|
250 260
....*....|....*....|...
gi 515634216 296 AEKATRLALHLAKGENTSTEPMM 318
Cdd:cd01542 232 GEKAAELLLDMIEGEKVPKKQKL 254
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
61-328 |
2.21e-43 |
|
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: 150.34 E-value: 2.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDE--ELIAYAkev 138
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPAtrKLLRAA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 139 kglvliNRYIAEIAN-------HCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIED-ADERIQGYLAALSDYKIALS 210
Cdd:cd01575 78 ------GIPVVETWDlpddpidMAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 211 DSYIEYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRY 290
Cdd:cd01575 152 LVLLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRV 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 515634216 291 PIQMMAEKATRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd01575 232 PRYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
61-304 |
1.19e-42 |
|
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: 148.50 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVL-----VGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDrEEERQAIELLINSR-CDALVI-HSKglTDEELIA 133
Cdd:cd06294 1 TIGLVlpssaEELFQNPFFSEVLRGISQVANENGYSLLLATGNTE-EELLEEVKRMVRGRrVDGFILlYSK--EDDPLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 134 YAKEVK-GLVLINRYIAeiANHCIFL--DNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALS 210
Cdd:cd06294 78 YLKEEGfPFVVIGKPLD--DNDVLYVdnDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 211 DSYIEYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRY 290
Cdd:cd06294 156 DDYILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDI 235
|
250
....*....|....
gi 515634216 291 PIQMMAEKATRLAL 304
Cdd:cd06294 236 NPYELGREAAKLLI 249
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-315 |
2.82e-42 |
|
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: 147.43 E-value: 2.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVK- 139
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSEALELLEEEGv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 140 GLVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIED-ADERIQGYLAALSDYKIALSDsYIEYSA 218
Cdd:cd06282 81 PYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSASDrARLRYQGYRDALKEAGLKPIP-IVEVDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 219 PTSDGGEyAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEK 298
Cdd:cd06282 160 PTNGLEE-ALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGRA 238
|
250
....*....|....*..
gi 515634216 299 ATRLALHLAKGENTSTE 315
Cdd:cd06282 239 AADLLLAEIEGESPPTS 255
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
2.36e-41 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 145.07 E-value: 2.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVK- 139
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDPELAAALARLDi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 140 GLVLINRyiaEIANH--CIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYS 217
Cdd:cd06281 81 PVVLIDR---DLPGDidSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 218 APTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAE 297
Cdd:cd06281 158 SFSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGR 237
|
250 260 270
....*....|....*....|....*....|...
gi 515634216 298 KATRLAL-HLAKGENTSTEPMMFSPTLVRRNSV 329
Cdd:cd06281 238 AAAELLLdRIEGPPAGPPRRIVVPTELILRDSC 270
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-328 |
6.37e-41 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 143.80 E-value: 6.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVI----HskgltDEELIAYAK 136
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILvgsdH-----DPELFELLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 137 EvKGLVLINRYIAEIAN--HCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIED-ADERIQGYLAALSDYKIALSDSY 213
Cdd:cd06273 76 Q-RQVPYVLTWSYDEDSphPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDrARARLAGIRDALAERGLELPEER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 214 IEYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQ 293
Cdd:cd06273 155 VVEAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAR 234
|
250 260 270
....*....|....*....|....*....|....*
gi 515634216 294 MMAEKATRLALHLAKGEnTSTEPMMFSPTLVRRNS 328
Cdd:cd06273 235 EIGELAARYLLALLEGG-PPPKSVELETELIVRES 268
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
61-329 |
7.19e-39 |
|
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: 138.56 E-value: 7.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIAN-HCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAP 219
Cdd:cd06296 81 FVLIDPVGEPDPDlPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 220 TSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKA 299
Cdd:cd06296 161 TYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGAVA 240
|
250 260 270
....*....|....*....|....*....|
gi 515634216 300 TRLALHLAKGENTSTEPMMFSPTLVRRNSV 329
Cdd:cd06296 241 VRLLLRLLEGGPPDARRIELATELVVRGST 270
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
61-328 |
7.68e-38 |
|
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: 135.88 E-value: 7.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIA--EIANHCIflDNKKGAYLATEYLIRHGHKNIACIASSHSIE-DADERIQGYLAALSDYKIALSDSYIEYS 217
Cdd:cd06298 81 VVLAGTVDSdhEIPSVNI--DYEQAAYDATKSLIDKGHKKIAFVSGPLKEYiNNDKKLQGYKRALEEAGLEFNEPLIFEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 218 APTSDGGEYAMTNLLTKSLPiTGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAE 297
Cdd:cd06298 159 DYDYDSGYELYEELLESGEP-DAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGA 237
|
250 260 270
....*....|....*....|....*....|.
gi 515634216 298 KATRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd06298 238 VAMRLLTKLMNKEEVEETIVKLPHSIIWRQS 268
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-328 |
2.40e-37 |
|
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: 134.60 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDI---SDPFFGTLVKAVDNVARENGkHILVGNGSHDREEERQAIELLINS-RCDALVIhsKGLTDEEliaYAK 136
Cdd:cd19974 1 NIAVLIPERffgDNSFYGKIYQGIEKELSELG-YNLVLEIISDEDEEELNLPSIISEeKVDGIII--LGEISKE---YLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 137 EVKGL----VLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIA---SSHSIEDadeRIQGYLAALSDYKIAL 209
Cdd:cd19974 75 KLKELgipvVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVGdinYTSSFMD---RYLGYRKALLEAGLPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 210 SDSYIEYSAPTSDGGEYAMTNL-LTKSLPiTGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTI 288
Cdd:cd19974 152 EKEEWLLEDRDDGYGLTEEIELpLKLMLP-TAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 515634216 289 RYPIQMMAEKATRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd19974 231 EVDKEAMGRRAVEQLLWRIENPDRPFEKILVSGKLIERDS 270
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
61-326 |
4.54e-37 |
|
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: 133.83 E-value: 4.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQKGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIasSHSIEDAD---ERIQGYLAALSDYKIALSDSYIEYS 217
Cdd:cd06283 81 VVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFV--TEPIKGIStrrERLQGFLDALARYNIEGDVYVIEIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 218 APTSDggEYAMTNLLTKS-LPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMA 296
Cdd:cd06283 159 DTEDL--QQALAAFLSQHdGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIG 236
|
250 260 270
....*....|....*....|....*....|
gi 515634216 297 EKATRLALHLAKGENTSTEPMMFSPTLVRR 326
Cdd:cd06283 237 KAAAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
67-324 |
6.91e-37 |
|
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: 133.45 E-value: 6.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 67 GDISDPFFGTLVKAVDNVARENGKHILVGNGShDREEERQAIELLINS-RCDALVIHSKgLTDEELIAYAKEvKGL--VL 143
Cdd:cd20010 11 GDLGDPFFLEFLAGLSEALAERGLDLLLAPAP-SGEDELATYRRLVERgRVDGFILART-RVNDPRIAYLLE-RGIpfVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 144 INRyIAEIANH-CIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSD 222
Cdd:cd20010 88 HGR-SESGAPYaWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPALVREGPLTEE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 223 GGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGL-IARYVHPKLTTIRYPIQMMAEKATR 301
Cdd:cd20010 167 GGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLpALEYFSPPLTTTRSSLRDAGRRLAE 246
|
250 260
....*....|....*....|...
gi 515634216 302 LALHLAKGENTSTEPMMFSPTLV 324
Cdd:cd20010 247 MLLALIDGEPAAELQELWPPELI 269
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
57-306 |
1.78e-36 |
|
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: 132.37 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 57 QSTNTVGVLV-------GDISDPFFGTLVKAVDNVARENGKHILVgngSHDREEERQAIELLINSRCDALVIHSKGLTDE 129
Cdd:cd06295 1 QRSRTIAVVVpmdphgdQSITDPFFLELLGGISEALTDRGYDMLL---STQDEDANQLARLLDSGRADGLIVLGQGLDHD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 130 ELIAYAKevKGLVLI--------NRYIAeianhcIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADeRIQGYLAA 201
Cdd:cd06295 78 ALRELAQ--QGLPMVvwgapedgQSYCS------VGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEVAD-RLQGYRDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 202 LSDYKIALSDSYIEYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYV 281
Cdd:cd06295 149 LAEAGLEADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYF 228
|
250 260
....*....|....*....|....*
gi 515634216 282 HPKLTTIRypiQMMAEKATRLALHL 306
Cdd:cd06295 229 RPPLTTVR---QDLALAGRLLVEKL 250
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
61-328 |
3.20e-32 |
|
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: 121.03 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELFEEVIVPTEKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIanHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDAD----ERIQGYLAALSDYKIALSDSYIEY 216
Cdd:cd06297 81 VVLIDANSMGY--DCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTEtvfrEREQGFLEALNKAGRPISSSRMFR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 217 SAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARyvHPKLTTIRYPIQMMA 296
Cdd:cd06297 159 IDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTVRQPVEEMG 236
|
250 260 270
....*....|....*....|....*....|..
gi 515634216 297 EKATRLALHLAKGENTSTEPMMFSPTLVRRNS 328
Cdd:cd06297 237 EAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
61-328 |
4.01e-32 |
|
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: 121.16 E-value: 4.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGD-----ISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLInsrcDALVIHSKGLTDEELIAYA 135
Cdd:cd06279 1 AIGVLLPDdlsyaFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAAV----DGFIVYGLSDDDPAVAALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 136 KEVKGLVLINRYIAEIAnHCIFLDNKKGAYLATEYLIRHGHKNIACI-------------------ASSHSIedADERIQ 196
Cdd:cd06279 77 RRGLPLVVVDGPAPPGI-PSVGIDDRAAARAAARHLLDLGHRRIAILslrldrgrergpvsaerlaAATNSV--ARERLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 197 GYLAALSDYKIALSDSYI-EYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDG 275
Cdd:cd06279 154 GYRDALEEAGLDLDDVPVvEAPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDI 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 515634216 276 LIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGEntSTEPMMFSPTLVRRNS 328
Cdd:cd06279 234 PEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGA--PPRPVILPTELVVRAS 284
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
170-329 |
4.18e-32 |
|
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: 117.44 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 170 YLIRHGHKNIACIASSHSIED--ADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTNLLtKSLPiTGIVAYNDY 247
Cdd:pfam13377 1 HLAELGHRRIALIGPEGDRDDpySDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWL-GALP-TAVFVANDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 248 MAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGENTSTEPMMFSPTLVRRN 327
Cdd:pfam13377 79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERE 158
|
..
gi 515634216 328 SV 329
Cdd:pfam13377 159 ST 160
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
62-307 |
8.67e-30 |
|
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: 114.27 E-value: 8.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 62 VGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKgLTDEELIAYAKEVKGL 141
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLV-DPAAAGVAEKARGQNV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 142 --VLINR--YIAEIANHCIFlDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYS 217
Cdd:cd01537 81 pvVFFDKepSRYDKAYYVIT-DSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 218 APTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAE 297
Cdd:cd01537 160 DWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGK 239
|
250
....*....|
gi 515634216 298 KATRLALHLA 307
Cdd:cd01537 240 TTFDLLLNLA 249
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
2-71 |
1.01e-28 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 105.75 E-value: 1.01e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 2 ATIKDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISD 71
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
106-327 |
3.12e-28 |
|
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: 110.16 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 106 QAIELLINSRCDALVIHSKGLTDEELIAYAKEVKGLVLINRYIAEIAnhCIFLDNKKGAYLATEYLIRHGHKNIACIASS 185
Cdd:cd06272 47 TAKGLFSENRFDGVIVFGISDSDIEYLNKNKPKIPIVLYNRESPKYS--TVNVDNEKAGRLAVLLLIQKGHKSIAYIGNP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 186 HSIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPD 265
Cdd:cd06272 125 NSNRNQTLRGKGFIETCEKHGIHLSDSIIDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPE 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515634216 266 KMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGENTSTEPMMFSPTLVRRN 327
Cdd:cd06272 205 DISIVSYDNIPQEARSDPPLTVVGVPIEKIAEESLRLILKLIEGRENEIQQLILYPELIFRE 266
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
39-310 |
5.40e-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: 110.40 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 39 AMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDA 118
Cdd:COG1879 13 ALALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 119 LVI---HSKGLTDeeLIAYAKEvKG--LVLINRYIAE-IANHCIFLDNKKGAYLATEYLIRH--GHKNIACIASSHSIED 190
Cdd:COG1879 93 IIVspvDPDALAP--ALKKAKA-AGipVVTVDSDVDGsDRVAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 191 ADERIQGYLAALSDY-KIALSDSYieYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSI 269
Cdd:COG1879 170 ANERTDGFKEALKEYpGIKVVAEQ--YADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRK--GDVKV 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 515634216 270 IGFD----------DGLIAryvhpklTTIRYPIQMMAEKATRLALHLAKGE 310
Cdd:COG1879 246 VGFDgspealqaikDGTID-------ATVAQDPYLQGYLAVDAALKLLKGK 289
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
59-262 |
5.45e-27 |
|
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: 107.21 E-value: 5.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 59 TNTVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEV 138
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKAEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 139 KGLV--LINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKN-IACIASSHSIEDADERIQGYLAALSDYKIALSDSYIE 215
Cdd:pfam00532 81 GIPViaADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAGPASALTARERVQGFMAALAAAGREVKIYHVA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515634216 216 YSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQ 262
Cdd:pfam00532 161 TGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRV 207
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
61-310 |
8.76e-26 |
|
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: 103.80 E-value: 8.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSkgLTDEELIAYAKEVKG 140
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAP--VDSEALVPAVKKANA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 ----LVLINRYIAEIANHCIFL--DNKKGAYLATEYLIRH--GHKNIACIASSHSIEDADERIQGYLAALSDYkialSDS 212
Cdd:cd01536 79 agipVVAVDTDIDGGGDVVAFVgtDNYEAGKLAGEYLAEAlgGKGKVAILEGPPGSSTAIDRTKGFKEALKKY----PDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 213 YIEYSAPT---SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFD----------DGLIAr 279
Cdd:cd01536 155 EIVAEQPAnwdRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRT--GDIKIVGVDgtpealkaikDGELD- 231
|
250 260 270
....*....|....*....|....*....|.
gi 515634216 280 yvhpkLTTIRYPIqMMAEKATRLALHLAKGE 310
Cdd:cd01536 232 -----ATVAQDPY-LQGYLAVEAAVKLLNGE 256
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
61-311 |
1.11e-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: 100.74 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIhsKGLTDEELIAYAKEVKG 140
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIV--APSTPPDDIYYLCQAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 L--VLINRYIAEIANHCIFLDNKKGAYLATEYLIRHGHKNIACI---ASSHSIEdadERIQGYLAALSDYKIALSDSYIE 215
Cdd:cd06274 79 LpvVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLggrPELPSTA---ERIRGFRAALAEAGITEGDDWIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 216 YSAPTSDGGEYAMT-----------NLLTKSLPitgivayndyMAAGALSVLDENGIQAPDKMSIIGFDDgliaryvHPK 284
Cdd:cd06274 156 AEGYDRESGYQLMAellarlgglpqALFTSSLT----------LLEGVLRFLRERLGAIPSDLVLGTFDD-------HPL 218
|
250 260 270
....*....|....*....|....*....|....
gi 515634216 285 LTTIRYPIQM-------MAEKATRLALHLAKGEN 311
Cdd:cd06274 219 LDFLPNPVDSvrqdhdeIAEHAFELLDALIEGQP 252
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
73-324 |
3.15e-24 |
|
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: 99.42 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 73 FFGTLVKAVDNVARENGKHILVGNGSHDreEERQAIELLINS-RCDALVIHSKGLTDEELIAYAKEVKGLVLINRYIAEI 151
Cdd:cd06271 16 TVSE*VSGITEEAGTTGYHLLVWPFEEA--ES*VPIRDLVETgSADGVILSEIEPNDPRVQFLTKQNFPFVAHGRSD*PI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 152 ANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIAlsdSYIEYSAPTSDGGEYAMTNL 231
Cdd:cd06271 94 GHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGLT---GYPLDADTTLEAGRAAAQRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 232 LTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDG-LIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGE 310
Cdd:cd06271 171 LALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSApFLGAMITPPLTTVHAPIAEAGRELAKALLARIDGE 250
|
250
....*....|....
gi 515634216 311 NTSTEPMMFSPTLV 324
Cdd:cd06271 251 DPETLQVLVQPSLS 264
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
4-323 |
9.43e-22 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 93.94 E-value: 9.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 4 IKDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVKAVDN 83
Cdd:PRK14987 8 LQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 84 VARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYakEVKGLVLINryIAEIANHC----IFLD 159
Cdd:PRK14987 88 VTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMI--EVAGIPVVE--LMDSQSPCldiaVGFD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 160 NKKGAYLATEYLIRHGHKNIACIASShsiedADERI----QGYLAALSDYKIALSDSYIEYSAPTSDGGEyaMTNLLTKS 235
Cdd:PRK14987 164 NFEAARQMTTAIIARGHRHIAYLGAR-----LDERTiikqKGYEQAMLDAGLVPYSVMVEQSSSYSSGIE--LIRQARRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 236 LP-ITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGENTST 314
Cdd:PRK14987 237 YPqLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTP 316
|
....*....
gi 515634216 315 EPMMFSPTL 323
Cdd:PRK14987 317 KMLDLGFTL 325
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
62-310 |
1.54e-21 |
|
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: 91.99 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 62 VGVLVGDISDPFFGTLVKAVDNVARENG-KHILVGNGSHDREEERQAIELLINSRCDALVIH---SKGLTDeeLIAYAKE 137
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGgEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVApvdPTALAP--VLKKAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 138 vKG--LVLINRYIAEIANHCIF-LDNKKGAYLATEYLIRH--GHKNIACIASSHSIEDADERIQGYLAAL----SDYKIA 208
Cdd:pfam13407 79 -AGipVVTFDSDAPSSPRLAYVgFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGFKKVLkekyPGIKVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 209 LSDSYIEYSAPTSDGgeyAMTNLLTKSL-PITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFD----------DGLI 277
Cdd:pfam13407 158 AEVEGTNWDPEKAQQ---QMEALLTAYPnPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDatpealeaikDGTI 232
|
250 260 270
....*....|....*....|....*....|...
gi 515634216 278 ARYVHpklttirYPIQMMAEKATRLALHLAKGE 310
Cdd:pfam13407 233 DATVL-------QDPYGQGYAAVELAAALLKGK 258
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
3-327 |
3.76e-20 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 89.17 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 3 TIKDVAKEAGVSVATVSRVIN---KSPKASASSVESVTKAMSKLGYRPNANARALVSQSTNTVGVLVGDISDPFFGTLVK 79
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVINgkaKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 80 AVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELiaYAKEV-KGL--VLINRYIAeiANH-- 154
Cdd:PRK11303 82 YLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTSLPPEHPF--YQRLQnDGLpiIALDRALD--REHft 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 155 CIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALsdSYIEYSAPTSDGGEYAMTNLLTK 234
Cdd:PRK11303 158 SVVSDDQDDAEMLAESLLKFPAESILLLGALPELSVSFEREQGFRQALKDDPREV--HYLYANSFEREAGAQLFEKWLET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 235 -SLPiTGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDgliaryvHPKLTTIRYPIQMM-------AEKATRLALHl 306
Cdd:PRK11303 236 hPMP-DALFTTSYTLLQGVLDVLLERPGELPSDLAIATFGD-------NELLDFLPCPVNAVaqqhrliAERALELALA- 306
|
330 340
....*....|....*....|.
gi 515634216 307 AKGENTSTEPmmfSPTLVRRN 327
Cdd:PRK11303 307 ALDEPRKPKP---GLTRIRRN 324
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
5-56 |
2.00e-17 |
|
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: 74.75 E-value: 2.00e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 515634216 5 KDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPNANARALVS 56
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-273 |
2.11e-17 |
|
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: 80.76 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVK-AVDNVARENGKHILVGNGSHDREEERQ--AIELLINSRCDALVI---HSKGLtdeeLIAY 134
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKgARKHAKEANGYELLVKGIKQETDIEQQiaIVENLIAQKVDAIVIapaDSKAL----VPVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 135 AKEVK-GLVLIN-------RYIAEIANHCIFL--DNKKGAYLATEYLIRH--GHKNIACIASSHSIEDADERIQGYLAAL 202
Cdd:cd19970 77 KKAVDaGIAVINidnrldaDALKEGGINVPFVgpDNRQGAYLAGDYLAKKlgKGGKVAIIEGIPGADNAQQRKAGFLKAF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515634216 203 SDYKIALSDSYieySAPT-SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFD 273
Cdd:cd19970 157 EEAGMKIVASQ---SANWeIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFD 223
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
158-324 |
1.27e-16 |
|
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: 78.35 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 158 LDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTNLLTKSLP 237
Cdd:cd20009 100 FDNEAFAYEAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAARRLLRQPPR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 238 ITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGENTSTEPM 317
Cdd:cd20009 180 PDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAEPLQT 259
|
....*..
gi 515634216 318 MFSPTLV 324
Cdd:cd20009 260 LERPELI 266
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
61-324 |
2.84e-16 |
|
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: 77.45 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIH---SKGLTDEELIAYAKE 137
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNpvdPEGLTPAVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 138 VKgLVLINRYIAEIANHCIFL--DNKKGAYLATEYLIRHGHKN---IACIASSHSIEDADERIQGYLAALSDYKIA-LSD 211
Cdd:cd06318 81 IP-VITVDSALDPSANVATQVgrDNKQNGVLVGKEAAKALGGDpgkIIELSGDKGNEVSRDRRDGFLAGVNEYQLRkYGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 212 SYIE-----YSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFD----------DGL 276
Cdd:cd06318 160 SNIKvvaqpYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGML--DKVKVAGADgqkealklikDGK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 515634216 277 IaryvhpKLTTIRYPIqMMAEKATRLALHLAKGENTSTEPMMFSPTLV 324
Cdd:cd06318 238 Y------VATGLNDPD-LLGKTAVDTAAKVVKGEESFPEFTYTPTALI 278
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
3-48 |
5.56e-16 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 70.74 E-value: 5.56e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515634216 3 TIKDVAKEAGVSVATVSRVINKSPKASASSVESVTKAMSKLGYRPN 48
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
85-328 |
6.06e-16 |
|
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: 76.47 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 85 ARENGK-HILVGNGSHDREeerqaIELLINSRCDALVIHSkgLTDEELIAYAKevKGLVLINRYIAEIANHC--IFLDNK 161
Cdd:cd01543 24 AREHGPwSLYLEPPGYEEL-----LDLLKGWKGDGIIARL--DDPELAEALRR--LGIPVVNVSGSRPEPGFprVTTDNE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 162 KGAYLATEYLIRHGHKNIACIASSHSiEDADERIQGYLAALSDYKIALSdsyiEYSAPTSDGGEYAMTNL--LT---KSL 236
Cdd:cd01543 95 AIGRMAAEHLLERGFRHFAFCGFRNA-AWSRERGEGFREALREAGYECH----VYESPPSGSSRSWEEEReeLAdwlKSL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 237 PI-TGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFD-DGLIARYVHPKLTTIRYPIQMMAEKATRLaLH-LAKGENTS 313
Cdd:cd01543 170 PKpVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDnDELICELSSPPLSSIALDAEQIGYEAAEL-LDrLMRGERVP 248
|
250
....*....|....*.
gi 515634216 314 TEPMMFSPT-LVRRNS 328
Cdd:cd01543 249 PEPILIPPLgVVTRQS 264
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
1-312 |
1.54e-15 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 75.95 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 1 MATIKDVAKEAGVSVATVSRVINKSPKAsasSVESVTK-----AMSKLGYRpNANARALVSQSTNTVGVLV-------GD 68
Cdd:PRK10339 1 MATLKDIAIEAGVSLATVSRVLNDDPTL---NVKEETKhrileIAEKLEYK-TSSARKLQTGAVNQHHILAiysyqqeLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 69 ISDPFFGTLVKAVDNVARENGkhILVGNgSHDREEERQaielliNSRCDALVIHSKgLTDEELIAYAKEVKGLVLINRYI 148
Cdd:PRK10339 77 INDPYYLAIRHGIETQCEKLG--IELTN-CYEHSGLPD------IKNVTGILIVGK-PTPALRAAASALTDNICFIDFHE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 149 AEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQgylaALSDYK-----IALSDSYI-EYSapTSD 222
Cdd:PRK10339 147 PGSGYDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIREV----AFAEYGrlkqvVREEDIWRgGFS--SSS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 223 GGEYAMTNLLTKSLPITGIVAyNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRL 302
Cdd:PRK10339 221 GYELAKQMLAREDYPKALFVA-SDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNL 299
|
330
....*....|
gi 515634216 303 ALHLAKGENT 312
Cdd:PRK10339 300 LYEKARDGRA 309
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
61-324 |
2.92e-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 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: 74.63 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARE--NGKHILVGNGSHDREEERQAIELLINSRCDALVIH---SKGLtdEELIAYA 135
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEinPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNaadSAGI--EPAIKRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 136 KEVKGLVLINRYIAEIANHCIFLDNKKGAYLATEYLIRH--GHKNIAcIASSHSIEDADERIQGYLAALSDYK-IALSDs 212
Cdd:cd06321 79 KDAGIIVVAVDVAAEGADATVTTDNVQAGYLACEYLVEQlgGKGKVA-IIDGPPVSAVIDRVNGCKEALAEYPgIKLVD- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 213 yIEYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQ---------APDKMSIIGFDDGLIARyvhp 283
Cdd:cd06321 157 -DQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDdivitsvdgSPEAVAALKREGSPFIA---- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 515634216 284 klTTIRYPiQMMAEKATRLALHLAKGENTSTEPMMFSPTLV 324
Cdd:cd06321 232 --TAAQDP-YDMARKAVELALKILNGQEPAPELVLIPSTLV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-311 |
6.23e-15 |
|
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: 73.39 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIH---SKGLTD--EEL---- 131
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNpvdSEGIRPalEAAkeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 132 ---IAYAKEVKGLVLINRYIAEianhciflDNKKGAYLATEYLIRHGHK--NIACIASShSIEDADERIQGYLAALSDYK 206
Cdd:cd19971 81 ipvINVDTPVKDTDLVDSTIAS--------DNYNAGKLCGEDMVKKLPEgaKIAVLDHP-TAESCVDRIDGFLDAIKKNP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 207 ----IALSDsyieySAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFD--------- 273
Cdd:cd19971 152 kfevVAQQD-----GKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKL--GDILVYGVDgspdakaai 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 515634216 274 -DGLIAryvhpkLTTIRYPIQmMAEKATRLALHLAKGEN 311
Cdd:cd19971 225 kDGKMT------ATAAQSPIE-IGKKAVETAYKILNGEK 256
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
61-329 |
1.97e-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: 72.39 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVI---HSKGLTDeeLIAYAKE 137
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIIsptNSSAAPT--VLDLANE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 138 VKglvlINRYIAEIANH------CIFLDNKKGAYLATEYLIRH------GHKNIACIASSHSIEDADERIQGYLAAL--S 203
Cdd:cd06319 79 AK----IPVVIADIGTGggdyvsYIISDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQARTAGFEDALeeA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 204 DYKIALSDSYIEYSAptsDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFD---------- 273
Cdd:cd06319 155 GVEEVALRQTPNSTV---EETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDgdpealdlik 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 515634216 274 DGLIARyvhpklTTIRYPIqMMAEKATRLALHLAKGENTSTEPMMFSPTLVRRNSV 329
Cdd:cd06319 230 DGKLDG------TVAQQPF-GMGARAVELAIQALNGDNTVEKEIYLPVLLVTSENV 278
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
61-310 |
4.50e-14 |
|
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: 71.04 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFgtlVKAVDNVARENGKH----ILVGNGSHDREEERQAIELLINSRCDALVI---HSKGLTDEELIA 133
Cdd:cd06308 1 VIGFSQCSLNDPWR---AAMNEEIKAEAAKYpnveLIVTDAQGDAAKQIADIEDLIAQGVDLLIVspnEADALTPVVKKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 134 YAKEVKgLVLINR------YIAEIANhciflDNKKGAYLATEYLIR--HGHKNIACI----ASSHSIEdadeRIQGYLAA 201
Cdd:cd06308 78 YDAGIP-VIVLDRkvsgddYTAFIGA-----DNVEIGRQAGEYIAEllNGKGNVVEIqglpGSSPAID----RHKGFLEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 202 LSDY-KIALSDSYieYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFD------- 273
Cdd:cd06308 148 IAKYpGIKIVASQ--DGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGRE--KEIKIIGVDglpeage 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 515634216 274 ----DGLIAryvhpklTTIRYPIqmMAEKATRLALHLAKGE 310
Cdd:cd06308 224 kavkDGILA-------ATFLYPT--GGKEAIEAALKILNGE 255
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-310 |
1.01e-13 |
|
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: 70.06 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENG-KHILVGNGSH-DREEERQAIELLINSRCDALVIHSkgLTDEELIAYAKEV 138
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGvKIIFVGPESEeDVAGQNSLLEELINKKPDAIVVAP--LDSEDLVDPLKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 139 KG----LVLINRYIAEIANHC-IFLDNKKGAYLATEYLIRH-GHK-NIACIASSHSIEDADERIQG---YLAALSDYKIA 208
Cdd:cd06310 79 KDkgipVIVIDSGIKGDAYLSyIATDNYAAGRLAAQKLAEAlGGKgKVAVLSLTAGNSTTDQREEGfkeYLKKHPGGIKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 209 LSDSYieysaPTSDGGEYA--MTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKmsIIGFD----------DGL 276
Cdd:cd06310 159 LASQY-----AGSDYAKAAneTEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIK--IVGFDsqeelldalkNGK 231
|
250 260 270
....*....|....*....|....*....|....
gi 515634216 277 IARYVHPKLTTIRYpiqmmaeKATRLALHLAKGE 310
Cdd:cd06310 232 IDALVVQNPYEIGY-------EGIKLALKLLKGE 258
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
61-273 |
1.82e-11 |
|
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: 63.78 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVI---HSKGLTDEELIAYAKE 137
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILIspiDATGWDPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 138 VKgLVLINR---------YIAEIANHCIFLDNKKGAYLATEYLIRHGhkNIACIASSHSIEDADERIQGYLAAL---SDY 205
Cdd:cd06309 81 IP-VILVDRtidgedgslYVTFIGSDFVEEGRRAAEWLVKNYKGGKG--NVVELQGTAGSSVAIDRSKGFREVIkkhPNI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 206 KIALSDSyieySAPTSDGGEYAMTNLLtKSLP--ITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFD 273
Cdd:cd06309 158 KIVASQS----GNFTREKGQKVMENLL-QAGPgdIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGID 222
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
68-273 |
3.08e-10 |
|
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: 59.92 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 68 DISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQaIELL---INSRCDALVIHSkgLTDEELIAYAKEVK----G 140
Cdd:cd20006 10 DPNSDFWQTVKSGAEAAAKEYGVDLEFLGPESEEDIDGQ-IELIeeaIAQKPDAIVLAA--SDYDRLVEAVERAKkagiP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLINRYIAEIANHC-IFLDNKKGAYLATEYLIRHGHKN--IACIASSHSIEDADERIQGYLAALSDYKIALSDSyIEYS 217
Cdd:cd20006 87 VITIDSPVNSKKADSfVATDNYEAGKKAGEKLASLLGEKgkVAIVSFVKGSSTAIEREEGFKQALAEYPNIKIVE-TEYC 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515634216 218 APTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFD 273
Cdd:cd20006 166 DSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLG--GKVKVVGFD 219
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
61-273 |
6.61e-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 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: 59.15 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLV-GDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINS--RCDALVIHS-KGLTDEEL-IAYA 135
Cdd:cd06324 1 RVVFINpGKEDEPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARppKPDYLILVNeKGVAPELLeLAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 136 KEVKgLVLINRYI--AEIANH------------CIFLDNKKGAYLATEYLIRHGHK-------NIACIASSHSIEDADER 194
Cdd:cd06324 81 AKIP-VFLINNDLtdEERALLgkprekfkywlgSIVPDNEQAGYLLAKALIKAARKksddgkiRVLAISGDKSTPASILR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 195 IQGYLAALSDY-KIALSDsyIEYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFD 273
Cdd:cd06324 160 EQGLRDALAEHpDVTLLQ--IVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKPGKDVLVGGID 237
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
100-314 |
7.89e-10 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 58.75 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 100 DREEERQA--IELLINSRCDALVI--HSKGlTDEELIAYAKEVKGLVL-INRYI--AEIANHCIFlDNKKGAYLATEYLI 172
Cdd:cd19992 38 DNDAKTQAsqVENLLAQGIDVLIIapVDAG-AAANIVDKAKAAGVPVIsYDRLIlnADVDLYVGR-DNYKVGQLQAEYAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 173 RHGHK-NIACIASSHSIEDADERIQGYLAALSDYKIA-----LSDSYIEYSAPtsdggEYAM---TNLLTKS-LPITGIV 242
Cdd:cd19992 116 EAVPKgNYVILSGDPGDNNAQLITAGAMDVLQPAIDSgdikiVLDQYVKGWSP-----DEAMklvENALTANnNNIDAVL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515634216 243 AYNDYMAAGALSVLDENGIQapDKMSIIGFDDGLIA--RYVHPKLT-TIRYPIQMMAEKATRLALHLAKGENTST 314
Cdd:cd19992 191 APNDGMAGGAIQALKAQGLA--GKVFVTGQDAELAAlkRIVEGTQTmTVWKDLKELARAAADAAVKLAKGEKPQT 263
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
100-311 |
1.11e-09 |
|
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: 58.40 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 100 DREEERQAIELLINSRCDALVI---HSKGLTD--EELIAYAKEVkglVLINRYIAEiANHCIFL--DNKKGAYLATEYLI 172
Cdd:cd20004 42 DVEAQIQIIEYFIDQGVDGIVLaplDRKALVApvERARAQGIPV---VIIDSDLGG-DAVISFVatDNYAAGRLAAKRMA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 173 R--HGHKNIACIASSHSIEDADERIQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAA 250
Cdd:cd20004 118 KllNGKGKVALLRLAKGSASTTDRERGFLEALKKLAPGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTI 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515634216 251 GALSVLDENGiqAPDKMSIIGFD----------DGLIARYVhpklttIRYPIQmMAEKATRLALHLAKGEN 311
Cdd:cd20004 198 GALRALRRLG--LAGKVKFIGFDasdllldalrAGEISALV------VQDPYR-MGYLGVKTAVAALRGKP 259
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
61-273 |
1.61e-09 |
|
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: 57.69 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSkglTD-EELIAYAKEVK 139
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINP---TDsDAVSPAVEEAN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 140 G----LVLINRYIA--EIANHcIFLDNKKGAYLATEYLIR--HGHKNIACIASSHSIEDADERIQGYLAALSDY---KIA 208
Cdd:cd06323 78 EagipVITVDRSVTggKVVSH-IASDNVAGGEMAAEYIAKklGGKGKVVELQGIPGTSAARERGKGFHNAIAKYpkiNVV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515634216 209 LSDSyIEYSaptSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGiqaPDKMSIIGFD 273
Cdd:cd06323 157 ASQT-ADFD---RTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFD 214
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
85-311 |
4.89e-09 |
|
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380646 [Multi-domain] Cd Length: 284 Bit Score: 56.48 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 85 ARENGKHILVGNGSHDREEERQAIELLINSRCDALVI---HSKGLTDEELIAYAKEVKgLVLINRYIaeiaNHC-----I 156
Cdd:cd19991 25 AKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVvpnNGEALAPIVKEAKKAGVP-VLAYDRLI----LNAdvdlyV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 157 FLDNKKGAYLATEYLIRHGHK-NIACIASSHSIEDADERIQGYLAALS------DYKIALSDSYIEYSAPTSdggEYAMT 229
Cdd:cd19991 100 SFDNEKVGELQAEALVKAKPKgNYVLLGGSPTDNNAKLFREGQMKVLQplidsgDIKVVGDQWVDDWDPEEA---LKIME 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 230 NLLTK-SLPITGIVAYNDYMAAGALSVLDENGIQApdKMSIIGFDDGLIA--RYVHPKLT-TIRYPIQMMAEKATRLALH 305
Cdd:cd19991 177 NALTAnNNKIDAVIASNDGTAGGAIQALAEQGLAG--KVAVSGQDADLAAcqRIVEGTQTmTIYKPIKELAEKAAELAVA 254
|
....*.
gi 515634216 306 LAKGEN 311
Cdd:cd19991 255 LAKGEK 260
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
61-317 |
4.99e-09 |
|
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: 56.51 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALV---IHSKGLTDEelIAYAKE 137
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIvvpVDADALAPA--VEKAKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 138 vKG--LVLINRYIA-EIANHCIFLDNKKGAYLATEYLIRH--GHKNIACIASSHSIEDADERIQGYLAALSDY-KIALSD 211
Cdd:cd06313 79 -AGipLVGVNALIEnEDLTAYVGSDDVVAGELEGQAVADRlgGKGNVVILEGPIGQSAQIDRGKGIENVLKKYpDIKVLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 212 SyieysaPTSD-GGEYAMT---NLLTKSLP-ITGIVAYNDYMAAGALSVLDENGIqapDKMSIIGFD---DGLIARYVHP 283
Cdd:cd06313 158 E------QTANwSRDEAMSlmeNWLQAYGDeIDGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDgieDALQAVKSGE 228
|
250 260 270
....*....|....*....|....*....|....
gi 515634216 284 KLTTIRYPIQMMAEKATRLALHLAKGENTSTEPM 317
Cdd:cd06313 229 LIATVLQDAEAQGKGAVEVAVDAVKGEGVEKKYY 262
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-273 |
8.23e-09 |
|
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: 55.70 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILV--GNGSHDREEERQAIELLINSRCDALVIHSkglTDEELIAYAKEV 138
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFlgPATEADIAGQVNLVENAISRKPDAIVLAP---NDTAALVPAVEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 139 --KGL--VLINRYIA-EIANHCIFLDNKKGAYLATEYLIRHGHKN------IACIASSHSIEDADERIQGYLAALSDYKI 207
Cdd:cd20008 78 adAGIpvVLVDSGANtDDYDAFLATDNVAAGALAADELAELLKASgggkgkVAIISFQAGSQTLVDREEGFRDYIKEKYP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515634216 208 ALSDSYIEYS---APTSDGgeyAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGiqAPDKMSIIGFD 273
Cdd:cd20008 158 DIEIVDVQYSdgdIAKALN---QTTDLLTANPDLVGIFGANNPSAVGVAQALAEAG--KAGKIVLVGFD 221
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
69-324 |
2.13e-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: 54.51 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 69 ISDPFFGTLVKAVDNVARENG-KHILVGNGSHDREEERQAIELLINSRCDALVIH---SKGLTDeeLIAYAKEvKGLVLI 144
Cdd:cd06314 9 LNNPFWDLAEAGAEKAAKELGvNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISpndPEAVTP--VINKAAD-KGIPVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 145 ---------NR--YIAeianhcifLDNKKGAYLATEYLIR-HGHK-NIACIASSHSIEDADERIQGYLAALSDYKIalsd 211
Cdd:cd06314 86 tfdsdapdsKRlaYIG--------TDNYEAGREAGELMKKaLPGGgKVAIITGGLGADNLNERIQGFKDALKGSPG---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 212 syIEYSAPTSD-----GGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFDD------GLIARY 280
Cdd:cd06314 154 --IEIVDPLSDnddiaKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKV--GKVKIVGFDTlpetlqGIKDGV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 515634216 281 VHpkLTTIRYPIQmMAEKATRLALHLAKGENtSTEPMMFSPTLV 324
Cdd:cd06314 230 IA--ATVGQRPYE-MGYLSVKLLYKLLKGGK-PVPDVIDTGVDV 269
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
61-324 |
2.34e-08 |
|
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380622 [Multi-domain] Cd Length: 272 Bit Score: 54.25 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLtdEELIAYAKEVKG 140
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADA--DASIAAVKKAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 ----LVLINRYIAE--IANHCIFLDNKKGAYLATEYLIRH-GHK-NIACIASSHSIEDADERIQGYLAALSDYkialsdS 212
Cdd:cd19967 79 agipVFLIDREINAegVAVAQIVSDNYQGAVLLAQYFVKLmGEKgLYVELLGKESDTNAQLRSQGFHSVIDQY------P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 213 YIEYSAPTSDGGEYA-----MTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIqaPDKMSIIGFD--DGLIARYVHPKL 285
Cdd:cd19967 153 ELKMVAQQSADWDRTeafekMESILQANPDIKGVICGNDEMALGAIAALKAAGR--AGDVIIVGFDgsNDVRDAIKEGKI 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 515634216 286 T-TIRYPIQMMAEKATRLALHLAKGENT-STEPMMFSPTLV 324
Cdd:cd19967 231 SaTVLQPAKLIARLAVEQADQYLKGGSTgKEEKQLFDCVLI 271
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
163-328 |
8.16e-08 |
|
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: 52.81 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 163 GAYLATEYLIRHGHKNIACI---ASSHSIEDAdERIQGYLAALSDYKIALsdsyieYSAPTSDG--GEYAMTNLLTKSLP 237
Cdd:cd06287 105 TARLLLEHLHGAGARQVALLtgsSRRNSSLES-EAAYLRFAQEYGTTPVV------YKVPESEGerAGYEAAAALLAAHP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 238 -ITGIVAYNDYMAAGALSVLDENGIQAPDKMSIIGFDDGLIARYVHPKLTTIRYPIQMMAEKATRLALHLAKGENTSTEp 316
Cdd:cd06287 178 dIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSVE- 256
|
170
....*....|..
gi 515634216 317 MMFSPTLVRRNS 328
Cdd:cd06287 257 VGPAPELVVRAS 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
61-273 |
2.17e-07 |
|
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: 51.51 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVI---HSKGLTdeELIAYAKE 137
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILapvDSGGIV--PAIEAANE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 138 VKGLVLINRYIAEIAN--HCIFLDNKKGAYLATEYLIRH---GHKNIACI---ASSHSIEdadeRIQGYLAALSDYKial 209
Cdd:cd06322 79 AGIPVFTVDVKADGAKvvTHVGTDNYAGGKLAGEYALKAllgGGGKIAIIdypEVESVVL----RVNGFKEAIKKYP--- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515634216 210 sDSYIEYSAPTSDGGEYAMT---NLLTKSLPITGIVAYNDYMAAGALSVLDENGiqAPDKMSIIGFD 273
Cdd:cd06322 152 -NIEIVAEQPGDGRREEALAateDMLQANPDLDGIFAIGDPAALGALTAIESAG--KEDKIKVIGFD 215
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
69-308 |
5.06e-07 |
|
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: 50.35 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 69 ISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRC----------DALVIHSKG-LTDEELIAYAKE 137
Cdd:cd01391 12 IREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIagvigpgsssVAIVIQNLAqLFDIPQLALDAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 138 VKGLVLINRYIAEIAnhcIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEdADERIQGYLAALSDYKIALSDSYIEYS 217
Cdd:cd01391 92 SQDLSDKTLYKYFLS---VVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNS-GELRMAGFKELAKQEGICIVASDKADW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 218 APTSDGGEYAMtNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQApdKMSIIGFDDGLIARYVH-----PKLTTIRYPI 292
Cdd:cd01391 168 NAGEKGFDRAL-RKLREGLKARVIVCANDMTARGVLSAMRRLGLVG--DVSVIGSDGWADRDEVGyeveaNGLTTIKQQK 244
|
250
....*....|....*.
gi 515634216 293 QMMAEKATRLALHLAK 308
Cdd:cd01391 245 MGFGITAIKAMADGSQ 260
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-273 |
7.30e-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: 380662 [Multi-domain] Cd Length: 271 Bit Score: 49.93 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENG-KHILVGNGSHDREEERQAIELLINSRCDALVIhskGLTDEE-LIAYAKEV 138
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGvELDVQGPPTFDPTLQTPIVNAVIAKKPDALLI---APTDPQaLIAPLKRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 139 KG----LVLINRYIAE--IANHCIFLDNKKGAYLATEYLIR--HGHKNIACIASSHSIEDADERIQGYLAAL-SDYKIal 209
Cdd:cd20007 78 ADagikVVTVDTTLGDpsFVLSQIASDNVAGGALAAEALAEliGGKGKVLVINSTPGVSTTDARVKGFAEEMkKYPGI-- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515634216 210 sdSYI--EYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGiqAPDKMSIIGFD 273
Cdd:cd20007 156 --KVLgvQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAG--KTGKVKVVGFD 217
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-312 |
3.74e-06 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380628 [Multi-domain] Cd Length: 285 Bit Score: 47.85 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQ--AIELLINSRCDALVI---HSKGLTDEelIAYA 135
Cdd:cd19973 1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKIDGDNATQvtAIENMIAAGAKGILItpsDTKAIVPA--VKKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 136 KEVKGLVlinryIA--------EIANHCIFLDNKKGAYLATEYL-IRHGHKN--IACIASSHSIEDADERIQGYLAAlsd 204
Cdd:cd19973 79 RDAGVLV-----IAldtptdpiDAADATFATDNFKAGVLIGEWAkAALGAKDakIATLDLTPGHTVGVLRHQGFLKG--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 205 YKIAL---------SDSYIEYSAPT---SDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGF 272
Cdd:cd19973 151 FGIDEkdpesnedeDDSQVVGSADTngdQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKE--KGVLIVSV 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 515634216 273 D----------DGLIARyvhpklTTIRYPIQmMAEKATRLALHLAKGENT 312
Cdd:cd19973 229 DggcpgvkdvkDGIIGA------TSQQYPLR-MAALGVEAIAAFAKTGGT 271
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
61-273 |
1.19e-05 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 46.23 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIH---SKGLTD--EELIaya 135
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSpidVKALVPaiEAAI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 136 KEVKGLVLINRYiAEIANHCIFL--DNKKGAYLATEYLIRH--GHKNIACIASSHSIEDADERIQGY---LAALSDYKIA 208
Cdd:cd19968 78 KAGIPVVTVDRR-AEGAAPVPHVgaDNVAGGREVAKFVVDKlpNGAKVIELTGTPGSSPAIDRTKGFheeLAAGPKIKVV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515634216 209 LSDSyieySAPTSDGGEYAMTNLLTK-SLPITGIVAYNDYMAAGALSVLDENGIQAPDKMsIIGFD 273
Cdd:cd19968 157 FEQT----GNFERDEGLTVMENILTSlPGPPDAIICANDDMALGAIEAMRAAGLDLKKVK-VIGFD 217
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
67-273 |
1.38e-05 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380535 [Multi-domain] Cd Length: 272 Bit Score: 46.07 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 67 GDISDPFFGTLVKAVDNVARE-NGKHILVGNGSHDREEERQAIELLINSRCDALVIhskGLTD----EELIAYAKEvKGL 141
Cdd:cd06312 8 GSPSDPFWSVVKKGAKDAAKDlGVTVQYLGPQNNDIADQARLIEQAIAAKPDGIIV---TIPDpdalEPALKRAVA-AGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 142 VLI------------NRYIAEIANhciflDNKKGAYLATEYLIRHGHKNIACI---ASSHSIEDadeRIQGYLAALSDYK 206
Cdd:cd06312 84 PVIainsgddrskerLGALTYVGQ-----DEYLAGQAAGERALEAGPKNALCVnhePGNPGLEA---RCKGFADAFKGAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515634216 207 IALSdsyieysaPTSDGGEY-----AMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGiqAPDKMSIIGFD 273
Cdd:cd06312 156 ILVE--------LLDVGGDPteaqeAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAG--LKGKVKIGTFD 217
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
98-260 |
2.67e-05 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 45.05 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 98 SHDREEERQAIELLINSRCDALVIHSKglTDEELIAYAKEVKG----LVLINRYI-AEIANHCIFLDNKKGAYLATEYLI 172
Cdd:cd06311 38 SSNANEQVSQLEDLIAQKVDAIVILPQ--DSEELTVAAQKAKDagipVVNFDRGLnVLIYDLYVAGDNPGMGVVSAEYIG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 173 RH--GHKNIAC--IASSHSIEDadERIQGYLAALSD-YKIALSDSYieYSAPTSDGGEYAMTNLLTKSLPITGIVAYNDY 247
Cdd:cd06311 116 KKlgGKGNVVVleVPSSGSVNE--ERVAGFKEVIKGnPGIKILAMQ--AGDWTREDGLKVAQDILTKNKKIDAVWAADDD 191
|
170
....*....|...
gi 515634216 248 MAAGALSVLDENG 260
Cdd:cd06311 192 MAIGVLQAIKEAG 204
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
61-315 |
1.65e-04 |
|
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: 42.57 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGK-HILVGNGSHDREEERQAIELLINSRCDALVIhskGLTD----EELIAYA 135
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGKiELEIYDAQNDQSTQNDQIDTMIAKGVDLLVV---NLVDrtaaQTIIDKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 136 KEVKG-LVLINRYIAEIA----NHCIF--LDNKKGAYL----ATEYLIRHGH--KN----IACIA----SSHsiEDADER 194
Cdd:cd01539 79 KAANIpVIFFNREPSREDlksyDKAYYvgTDAEESGIMqgeiIADYWKANPEidKNgdgkIQYVMlkgePGH--QDAIAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 195 IQGYLAALSDYKIALSDSYIEYSAPTSDGGEYAMTNLLTK-SLPITGIVAYNDYMAAGALSVLDENG--IQAPDK-MSII 270
Cdd:cd01539 157 TKYSVKTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKyGDKIELVIANNDDMALGAIEALKAAGynTGDGDKyIPVF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 515634216 271 GFD----------DGLIaryvhpkLTTIRYPIQMMAEKATRLALHLAKGENTSTE 315
Cdd:cd01539 237 GVDatpealeaikEGKM-------LGTVLNDAKAQAKAIYELAKNLANGKEPLET 284
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-310 |
3.36e-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: 380627 [Multi-domain] Cd Length: 269 Bit Score: 41.66 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSKGLTDEELIAYAKEVKG 140
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 141 LVLIN-----------RYIAEianhciflDNKKGAYLATEYLIRH--GHKNIACIASSHSIEDADERIQGYLAALSDY-- 205
Cdd:cd19972 81 IPVIAvdrnpedapgdTFIAT--------DSVAAAKELGEWVIKQtgGKGEIAILHGQLGTTPEVDRTKGFQEALAEApg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 206 --KIAlsdsyiEYSAPTS-DGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIqaPDKMSIIGFD--------- 273
Cdd:cd19972 153 ikVVA------EQTADWDqDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGL--DHKIWVVGFDgdvaglkav 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 515634216 274 -DGLIAryvhpklTTIRYPIQMMAEKATRLALHLAKGE 310
Cdd:cd19972 225 kDGVLD-------ATMTQQTQKMGRLAVDSAIDLLNGK 255
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
56-278 |
6.16e-04 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 40.84 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 56 SQSTNTVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHSkglTDEEL---- 131
Cdd:PRK10653 23 AMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINP---TDSDAvgna 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 132 IAYAKEVKGLVL-INRYIA--EIANHcIFLDNKKGAYLATEYL---IRHGHKNIAC--IASSHSiedADERIQGYLAALS 203
Cdd:PRK10653 100 VKMANQANIPVItLDRGATkgEVVSH-IASDNVAGGKMAGDFIakkLGEGAKVIQLegIAGTSA---ARERGEGFKQAVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515634216 204 DYKIALSDSYIEYSAPTSdgGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGiqaPDKMSIIGFD---DGLIA 278
Cdd:PRK10653 176 AHKFNVLASQPADFDRTK--GLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDgtpDGIKA 248
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
86-310 |
6.81e-04 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380651 [Multi-domain] Cd Length: 302 Bit Score: 40.69 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 86 RENGKHILVGNGSHDreEERQA--IELLINSRCDALVIHSkgLTDEELIAYAKEV--KGLVLIN--------RYIAEIAn 153
Cdd:cd19996 29 KKLIKELIYTDAQGD--TQKQIadIQDLIAQGVDAIIVSP--NSPTALLPAIEKAaaAGIPVVLfdsgvgsdKYTAFVG- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 154 hcifLDNKKGAYLATEYLIR--HGHKNIACIASSHSIEDADERIQGYLAALSDYKI--ALSDSYIEYSaptSDGGEYAMT 229
Cdd:cd19996 104 ----VDDAAFGRVGAEWLVKqlGGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYPGikIVGEVYADWD---YAKAKQAVE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 230 NLLTKSLPITGIVAYNDYMAAGALSVLDENGIQAPdKMSiiGFDD-GLIARYV-HPKLTTIRYPIQ-MMAEKATRLALHL 306
Cdd:cd19996 177 SLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLV-PMT--GEDNnGFLKAWKeLPGFKSIAPSYPpWLGATALDAALAA 253
|
....
gi 515634216 307 AKGE 310
Cdd:cd19996 254 LEGE 257
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
61-310 |
7.16e-04 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380480 [Multi-domain] Cd Length: 283 Bit Score: 40.87 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARENGKHILVGNGSHDREEERQAIELLINSRCDALVIHS-KGLTDEELIAYAKEvK 139
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPvDGQALSPVVAEAKA-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 140 GLVLI--NRYI--AEIANHCIFLDNKKGAYLATEYLIRHGHKNIACIASSHSIEDADERIQGYLAALSDY----KI-ALS 210
Cdd:cd01538 80 GIKVIayDRLIlnADVDYYISFDNEKVGELQAQALLDAKPEGNYVLIGGSPTDNNAKLFRDGQMKVLQPAidsgKIkVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 211 DSYIEYSAPtsDGGEYAMTNLLTKS-LPITGIVAYNDYMAAGALSVLDENGIQApdKMSIIGFDDGLIA--RYVHPKLT- 286
Cdd:cd01538 160 DQWVDDWLP--ANAQQIMENALTANgNNVDAVVASNDGTAGGAIAALKAQGLSG--GVPVSGQDADLAAikRILAGTQTm 235
|
250 260
....*....|....*....|....
gi 515634216 287 TIRYPIQMMAEKATRLALHLAKGE 310
Cdd:cd01538 236 TVYKDIRLLADAAAEVAVALMRGE 259
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
62-324 |
8.37e-04 |
|
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: 40.32 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 62 VGVLVGDISDPFFGTLVKAVDNVARENGKHILV--GNGSHDREEERQAIELLINSRCDALVIHSkgLTDEELIAYAKEV- 138
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVqaAPSETDTQGQLNLLETMLNKGYDAILVSP--ISDTNLIPPIEKAn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 139 -KGLVLIN---RYIAEIANHC-------IFLDNKKGAYLATEYLIR--HGHKNIACIASSHSIEDADERIQGY---LAAL 202
Cdd:cd06320 80 kKGIPVINlddAVDADALKKAggkvtsfIGTDNVAAGALAAEYIAEklPGGGKVAIIEGLPGNAAAEARTKGFketFKKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 203 SDYKIALS-----DSYIEYSAptsdggeyaMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFD---- 273
Cdd:cd06320 160 PGLKLVASqpadwDRTKALDA---------ATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKT--GKVLVVGTDgipe 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 515634216 274 ------DGliaryvhpKLT-TIRYPIQMMAEKATRLALHLAKGEntSTEPMMFSPTLV 324
Cdd:cd06320 229 akksikAG--------ELTaTVAQYPYLEGAMAVEAALRLLQGQ--KVPAVVATPQAL 276
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
228-310 |
3.09e-03 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 38.96 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 228 MTNLLT-KSLPITGIVAYNDYMAAGALSVLDENGIQApdKMSIIGFDDGL--IARYVHPKLT-TIRYPIQMMAEKATRLA 303
Cdd:PRK10355 201 MENALTaNNNKIDAVVASNDATAGGAIQALSAQGLSG--KVAISGQDADLaaIKRIVAGTQTmTVYKPITKLANTAAEIA 278
|
....*..
gi 515634216 304 LHLAKGE 310
Cdd:PRK10355 279 VELGNGE 285
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
61-278 |
5.02e-03 |
|
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: 37.98 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 61 TVGVLVGDISDPFFGTLVKAVDNVARE-NGKHILVGNGSHDREEERQAIELLINSRCDALVIH------SKGLTDeeLIA 133
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNpvdtdaSAPAVD--AAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 134 YAKevKGLVLINRYIAEIANHCIFL--DNKKGAYLATEYLIR--HGHKNIACIASSHSIEDADERIQGYLAALSDY---K 206
Cdd:cd06301 80 DAG--IPLVYVNREPDSKPKGVAFVgsDDIESGELQMEYLAKllGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYpgmK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515634216 207 IALSDSyIEYSaptSDGGEYAMTNLLTKSLPITGIVAYNDYMAAGALSVLDENGIQapDKMSIIGFD---DGLIA 278
Cdd:cd06301 158 IVAEQT-ANWS---REKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKK--DDILVAGIDatpDALKA 226
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
238-332 |
6.10e-03 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380650 [Multi-domain] Cd Length: 294 Bit Score: 38.04 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515634216 238 ITGIVAYNDYMAAGALSVLDENGIqAPDKMsiIGFDDGLIA--RYVhpkLT-----TIRYPIQMMAEKATRLALHLAKGE 310
Cdd:cd19995 194 IDGVLSANDGLAGGAIAALKAQGL-AGKVP--VTGQDATVAglQRI---LAgdqymTVYKPIKKEAAAAAKVAVALLKGE 267
|
90 100
....*....|....*....|..
gi 515634216 311 ntstEPMMFSPTLVRRNSVEKV 332
Cdd:cd19995 268 ----TPPSDLVTGTVTNGGDKV 285
|
|
| |
