|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
2-329 |
0e+00 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 652.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 2 NKKVLTLSAVMSCMLFGTAAQAAD-RIGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
Cdd:PRK15395 1 NKKVLTLSALMASMLFGAAAAAADtRIGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 81 GVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAGWDLNKD 160
Cdd:PRK15395 81 GVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANPAWDLNKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 161 GQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 240
Cdd:PRK15395 161 GKIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 241 VEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTDWKIENKVVRIPYVGV 320
Cdd:PRK15395 241 VEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAEGTNWKIENKVVRVPYVGV 320
|
....*....
gi 490522029 321 DKDNLAEIT 329
Cdd:PRK15395 321 DKDNLAEFT 329
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
26-320 |
2.50e-156 |
|
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: 439.71 E-value: 2.50e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAGWDLNKDGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd01539 82 NIPVIFFNREPSREDLKSYDKAYYVGTDAEESGIMQGEIIADYWKANPEIDKNGDGKIQYVMLKGEPGHQDAIARTKYSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNaNKIEVVIANNDAMAMGAVEALKAHN------KSSIPVFGVDA 259
Cdd:cd01539 162 KTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYG-DKIELVIANNDDMALGAIEALKAAGyntgdgDKYIPVFGVDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490522029 260 LPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTD-WKIENKVVRIPYVGV 320
Cdd:cd01539 241 TPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLETGYkFLVEGKYVRIPYKKV 302
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
26-319 |
4.17e-118 |
|
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: 341.53 E-value: 4.17e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIEKDASAsPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGtVIEKARGQ 105
Cdd:cd01537 1 RIGVTIYSYDDNFMSVIRKAIEQDAKQ-PGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAG-VAEKARGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKEPSRkaldsYDKAYYVGTDSKESGIIQGDLIAKHWkanagwdlnkdgQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd01537 79 NVPVVFFDKEPSR-----YDKAYYVITDSKEGGIIQGDLLAKHG------------HIQIVLLKGPLGHPDAEARLAGVI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPnaNKIEVVIANNDAMAMGAVEALKAHNK---SSIPVFGVDALPE 262
Cdd:cd01537 142 KELNDKGIKTEQLQLDTGDWDTASGKDKMDQWLSGP--NKPTAVIANNDAMAMGAVEALKEHGLrvpSDISVFGYDALPE 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490522029 263 ALalvKSGALAGTVLNDANNQAKATFDLAKNLAagkgaadgTDWKIENKVVRIPYVG 319
Cdd:cd01537 220 AL---KSGPLLTTILQDANNLGKTTFDLLLNLA--------DNWKIDNKVVRVPYVL 265
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
5-325 |
3.53e-60 |
|
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: 195.14 E-value: 3.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 5 VLTLSAVMSCMLFG---------TAAQAADRIGVTIYKYDDNFMSVVRKAIEkDASASPDVQLLMNDSQNDQSKQNDQID 75
Cdd:COG1879 5 LLAAVLALALALAAcgsaaaeaaAAAAKGKTIGFVVKTLGNPFFVAVRKGAE-AAAKELGVELIVVDAEGDAAKQISQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 76 VLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPsrkalDSYDKAYYVGTDSKESGIIQGDLIAKHWKanagw 155
Cdd:COG1879 84 DLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDV-----DGSDRVAYVGSDNYAAGRLAAEYLAKALG----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 156 dlnkdGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGiKTEQLQLDTAMWDTAQAKDKMDAWLSgpnAN-KIEVVIANND 234
Cdd:COG1879 154 -----GKGKVAILTGSPGAPAANERTDGFKEALKEYP-GIKVVAEQYADWDREKALEVMEDLLQ---AHpDIDGIFAAND 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 235 AMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKgaadgtdwKIEnKVV 313
Cdd:COG1879 225 GMALGAAQALKAAGRKGdVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGK--------EVP-KEI 295
|
330
....*....|..
gi 490522029 314 RIPYVGVDKDNL 325
Cdd:COG1879 296 LTPPVLVTKENV 307
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
27-297 |
2.10e-58 |
|
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: 189.36 E-value: 2.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06301 3 IGVSMQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSrkalDSYDKAYYVGTDSKESGIIQGDLIAKhwkanagwdlNKDGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06301 83 IPLVYVNREPD----SKPKGVAFVGSDDIESGELQMEYLAK----------LLGGKGNIAILDGVLGHEAQILRTEGNKD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELND-KGIKTEQLQldTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEAL 264
Cdd:cd06301 149 VLAKyPGMKIVAEQ--TANWSREKAMDIVENWLQ--SGDKIDAIVANNDEMAIGAILALEAAGKKdDILVAGIDATPDAL 224
|
250 260 270
....*....|....*....|....*....|...
gi 490522029 265 ALVKSGALAGTVLNDANNQAKATFDLAKNLAAG 297
Cdd:cd06301 225 KAMKAGRLDATVFQDAAGQGETAVDVAVKAAKG 257
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
26-309 |
2.38e-58 |
|
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: 188.93 E-value: 2.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIEKDAsASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAA-KELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNkepsRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWkanagwdlnkDGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd01536 80 GIPVVAVD----TDIDGGGDVVAFVGTDNYEAGKLAGEYLAEAL----------GGKGKVAILEGPPGSSTAIDRTKGFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDKGiKTEQLQLDTAMWDTAQAKDKMDAWLsgpNAN-KIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEA 263
Cdd:cd01536 146 EALKKYP-DIEIVAEQPANWDRAKALTVTENLL---QANpDIDAVFAANDDMALGAAEALKAAGRTGdIKIVGVDGTPEA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490522029 264 LALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTDWKIE 309
Cdd:cd01536 222 LKAIKDGELDATVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPVT 267
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
27-298 |
4.20e-58 |
|
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: 188.29 E-value: 4.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEpsrkaLDSYDKAYYVGTDSKESGIIQGDLIAKHWKanagwdlnkdGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:pfam13407 81 IPVVTFDSD-----APSSPRLAYVGFDNEAAGEAAGELLAEALG----------GKGKVAILSGSPGDPNANERIDGFKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDK--GIKTEQLQlDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIP-VFGVDALPEA 263
Cdd:pfam13407 146 VLKEKypGIKVVAEV-EGTNWDPEKAQQQMEALLTA-YPNPLDGIISPNDGMAGGAAQALEAAGLAGKVvVTGFDATPEA 223
|
250 260 270
....*....|....*....|....*....|....*
gi 490522029 264 LALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:pfam13407 224 LEAIKDGTIDATVLQDPYGQGYAAVELAAALLKGK 258
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
26-327 |
3.52e-47 |
|
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: 160.51 E-value: 3.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIEKDAsASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVA-KELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKepsrkALDSYDKAYYVGTDSKESGIIQGDLIAKhwkanagwdlNKDGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd06313 80 GIPLVGVNA-----LIENEDLTAYVGSDDVVAGELEGQAVAD----------RLGGKGNVVILEGPIGQSAQIDRGKGIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDK-GIKTeqLQLDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEAL 264
Cdd:cd06313 145 NVLKKYpDIKV--LAEQTANWSRDEAMSLMENWLQA-YGDEIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDAL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490522029 265 ALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGaadgtdwkiENKVVRIPYVGVDKDNLAE 327
Cdd:cd06313 222 QAVKSGELIATVLQDAEAQGKGAVEVAVDAVKGEG---------VEKKYYIPFVLVTKDNVDD 275
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
43-318 |
1.61e-37 |
|
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: 135.40 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 43 RKAIEKDAsASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALD 122
Cdd:cd19992 18 KEYMEEEA-KELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDRLILNADVD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 123 sydkaYYVGTDSKESGIIQGD-LIAKHWKANagwdlnkdgqiqYVLLKGEPGHPDAEARTT---YVIKELNDKG---IKT 195
Cdd:cd19992 97 -----LYVGRDNYKVGQLQAEyALEAVPKGN------------YVILSGDPGDNNAQLITAgamDVLQPAIDSGdikIVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 196 EQLqldTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAG 274
Cdd:cd19992 160 DQY---VKGWSPDEAMKLVENALTA-NNNNIDAVLAPNDGMAGGAIQALKAQGlAGKVFVTGQDAELAALKRIVEGTQTM 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490522029 275 TVLNDANNQAKATFDLAKNLAAGKgAADGTDWKIENKVVRIPYV 318
Cdd:cd19992 236 TVWKDLKELARAAADAAVKLAKGE-KPQTTDETINNGGKDVPAI 278
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
48-328 |
2.86e-34 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 127.56 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 48 KDASASPDVQllmnDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVffnkepsrkaldSYDK- 126
Cdd:COG4213 29 KELGYEVDVQ----NANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVI------------AYDRl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 127 ------AYYVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIQYVLLKGEPGhpDAEARTTY-----VIKELNDKG--- 192
Cdd:COG4213 93 ilnsdvDYYVSFDNVKVGELQGQYLVDG--------LPLKGKGNIELFGGSPT--DNNATLFFegamsVLQPYIDSGklv 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 193 IKTEQlqlDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVF-GVDALPEALALVKSGA 271
Cdd:COG4213 163 VVSGQ---WTLGWDPETAQKRMENLLTA-NGNKVDAVLAPNDGLAGGIIQALKAQGLAGKVVVtGQDAELAAVQRILAGT 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490522029 272 LAGTVLNDANNQAKATFDLAKNLAAGKGAAdgTDWKIENKVVRIPY-----VGVDKDNLAEI 328
Cdd:COG4213 239 QYMTVYKDTRELAEAAAELAVALAKGEKPE--VNGTYDNGKKDVPSyllepVAVTKDNVKET 298
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
35-298 |
2.40e-32 |
|
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: 121.11 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 35 DDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFnk 114
Cdd:cd06308 10 NDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 115 epSRKaLDSYDKAYYVGTDSKESGIIQGDLIAKhwkanagwDLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELND-KGI 193
Cdd:cd06308 88 --DRK-VSGDDYTAFIGADNVEIGRQAGEYIAE--------LLNGKGNV--VEIQGLPGSSPAIDRHKGFLEAIAKyPGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 194 KteQLQLDTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDALPEAL-ALVKSGA 271
Cdd:cd06308 155 K--IVASQDGDWLRDKAIKVMEDLLQ--AHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGLPEAGeKAVKDGI 230
|
250 260
....*....|....*....|....*..
gi 490522029 272 LAGTVLNDANnqAKATFDLAKNLAAGK 298
Cdd:cd06308 231 LAATFLYPTG--GKEAIEAALKILNGE 255
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
48-316 |
6.81e-28 |
|
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380649 [Multi-domain] Cd Length: 304 Bit Score: 110.03 E-value: 6.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 48 KDASASPDVQLlmndSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFnkepSRKALDSYDKA 127
Cdd:cd19994 26 EEAGYTVDLQY----ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAY----DRLIMNTDAVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 128 YYVGTDSKESGIIQGDLIAKHWKANAGwdlnkDGQIQYVLLKGEPGhpDAEARTTY-----VIKELNDKGI------KTE 196
Cdd:cd19994 98 YYVTFDNEKVGELQGQYLVDKLGLKDG-----KGPFNIELFAGSPD--DNNAQLFFkgameVLQPYIDDGTlvvrsgQTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 197 QLQLDTAMWDTAQAKDKMDAWLSGPNA--NKIEVVIANNDAMAMGAVEALKAHNKSSIP---VFGVDALPEALALVKSGA 271
Cdd:cd19994 171 FEQVATPDWDTETAQARMETLLSAYYTggKKLDAVLSPNDGIARGVIEALKAAGYDTGPwpvVTGQDAEDASVKSILDGE 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490522029 272 LAGTVLNDANNQAKATFDLAKNLAAGKGAADGTDWKIENKVVRIP 316
Cdd:cd19994 251 QSMTVFKDTRLLAKATVELVDALLEGEEVEVNDTKTYDNGVKVVP 295
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
38-327 |
2.11e-27 |
|
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: 108.46 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 38 FMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkeps 117
Cdd:cd06309 13 WRVANTKSIKEAAKKR-GYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVD---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 118 rKALDSYDKAYY---VGTDSKESGIIQGDLIAKHWKanagwdlNKDGQIqyVLLKGEPGHPDAEARTT---YVIKELNDK 191
Cdd:cd06309 88 -RTIDGEDGSLYvtfIGSDFVEEGRRAAEWLVKNYK-------GGKGNV--VELQGTAGSSVAIDRSKgfrEVIKKHPNI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 192 GIKTEQlqldTAMWDTAQAKDKMDAWL-SGPnaNKIEVVIANNDAMAMGAVEALKAHNKS---SIPVFGVDALPEALALV 267
Cdd:cd06309 158 KIVASQ----SGNFTREKGQKVMENLLqAGP--GDIDVIYAHNDDMALGAIQALKEAGLKpgkDVLVVGIDGQKDALEAI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 268 KSGALAGTVLNDAnNQAKATFDLAKNLAAGKgaadgtdwKIEnKVVRIPYVGVDKDNLAE 327
Cdd:cd06309 232 KAGELNATVECNP-LFGPTAFDTIAKLLAGE--------KVP-KLIIVEERLFDKDNAAE 281
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
27-276 |
2.27e-27 |
|
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: 108.15 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06323 2 IGLSVSTLNNPFFVSLKDGAQAEAKEL-GVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNkepsRKALDSyDKAYYVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYvIK 186
Cdd:cd06323 81 IPVITVD----RSVTGG-KVVSHIASDNVAGGEMAAEYIAKK--------LGGKGKV--VELQGIPGTSAARERGKG-FH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALA 265
Cdd:cd06323 145 NAIAKYPKINVVASQTADFDRTKGLNVMENLLqAHPD---IDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVK 221
|
250
....*....|.
gi 490522029 266 LVKSGALAGTV 276
Cdd:cd06323 222 AVKDGKLAATV 232
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
27-297 |
2.57e-27 |
|
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: 108.27 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06318 2 IGFSQRTLASPYYAALVAAAKAEAKKL-GVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNkepsRKALDSYDKAYYVGTDSKESGIIQGdliakHWKANAgwdLNKDGqIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06318 81 IPVITVD----SALDPSANVATQVGRDNKQNGVLVG-----KEAAKA---LGGDP-GKIIELSGDKGNEVSRDRRDGFLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIKT------EQLQLDTAMWDTAQAKDKMDAWLSgpnANK-IEVVIANNDAMAMGAVEALKAHNKSSI-PVFGVD 258
Cdd:cd06318 148 GVNEYQLRKygksniKVVAQPYGNWIRSGAVAAMEDLLQ---AHPdINVVYAENDDMALGAMKALKAAGMLDKvKVAGAD 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 490522029 259 ALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAG 297
Cdd:cd06318 225 GQKEALKLIKDGKYVATGLNDPDLLGKTAVDTAAKVVKG 263
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
26-308 |
2.24e-26 |
|
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: 105.55 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIEKDAsASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEA-AKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNkepsRKAlDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAgwdlnkdgqiQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd19968 80 GIPVVTVD----RRA-EGAAPVPHVGADNVAGGREVAKFVVDKLPNGA----------KVIELTGTPGSSPAIDRTKGFH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELnDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAH--NKSSIPVFGVDALPEA 263
Cdd:cd19968 145 EEL-AAGPKIKVVFEQTGNFERDEGLTVMENILTS-LPGPPDAIICANDDMALGAIEAMRAAglDLKKVKVIGFDAVPDA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490522029 264 LALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTDWKI 308
Cdd:cd19968 223 LQAIKDGELYATVEQPPGGQARTALRILVDYLKDKKAPKKVNLKP 267
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
26-325 |
1.85e-25 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380542 [Multi-domain] Cd Length: 278 Bit Score: 103.21 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIeKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGV-QAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFfnkepSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANaGWdlnkdGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd06319 80 KIPVVI-----ADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKEN-GW-----GGGSVGIIAIPQSRVNGQARTAGFE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDKGIKTEQLQLdTAMWDTAQAKDKM-DAWLSGPnanKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEA 263
Cdd:cd06319 149 DALEEAGVEEVALRQ-TPNSTVEETYSAAqDLLAANP---DIKGIFAQNDQMAQGALQAIEEAGRTGdILVVGFDGDPEA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490522029 264 LALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADgtdwkienKVVRIPYVGVDKDNL 325
Cdd:cd06319 225 LDLIKDGKLDGTVAQQPFGMGARAVELAIQALNGDNTVE--------KEIYLPVLLVTSENV 278
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
27-316 |
3.34e-25 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380626 [Multi-domain] Cd Length: 267 Bit Score: 101.89 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEKDASASPDvQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd19971 2 FGFSYMTMNNPFFIAINDGIKKAVEANGD-ELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPS-RKALDSydkayYVGTDSKESGIIQGDLIAKhwkanagwDLNKDGQIqyVLLKgepgHPDAEA---RTT 182
Cdd:cd19971 81 IPVINVDTPVKdTDLVDS-----TIASDNYNAGKLCGEDMVK--------KLPEGAKI--AVLD----HPTAEScvdRID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 183 YVIKEL-NDKGIKTEQlQLDTAMwDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDA 259
Cdd:cd19971 142 GFLDAIkKNPKFEVVA-QQDGKG-QLEVAMPIMEDILqAHPD---LDAVFALNDPSALGALAALKAAGKlGDILVYGVDG 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490522029 260 LPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKgaadgtdwKIEnKVVRIP 316
Cdd:cd19971 217 SPDAKAAIKDGKMTATAAQSPIEIGKKAVETAYKILNGE--------KVE-KEIVVP 264
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
44-318 |
3.73e-25 |
|
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: 102.75 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 44 KAIEKDAsasPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsrKALDS 123
Cdd:cd19995 24 KAMKKLC---PDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYD-----RLILG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 124 YDKAYYVGTDSKESGIIQGDLIAKHWKANAGwdlnKDGQIqyVLLKGEPGHPDA---EARTTYVIKELNDKGIKTEQLQL 200
Cdd:cd19995 96 GPADYYVSFDNVAVGEAQAQSLVDHLKAIGK----KGVNI--VMINGSPTDNNAglfKKGAHEVLDPLGDSGELKLVCEY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 201 DTAMWDTAQAKDKMDAWLSgPNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAGTVLND 279
Cdd:cd19995 170 DTPDWDPANAQTAMEQALT-KLGNNIDGVLSANDGLAGGAIAALKAQGlAGKVPVTGQDATVAGLQRILAGDQYMTVYKP 248
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490522029 280 ANNQAKATFDLAKNLAAGKG-AADGTDWKIENKVVRIPYV 318
Cdd:cd19995 249 IKKEAAAAAKVAVALLKGETpPSDLVTGTVTNGGDKVPAV 288
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
26-326 |
1.40e-24 |
|
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: 100.80 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIEKDASASP-DVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARG 104
Cdd:cd06320 1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGvKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 105 QNIPIVFFNKEPSRKALDSY--DKAYYVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTT 182
Cdd:cd06320 81 KGIPVINLDDAVDADALKKAggKVTSFIGTDNVAAGALAAEYIAEK--------LPGGGKV--AIIEGLPGNAAAEARTK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 183 YVIKELNdKGIKTEQLQLDTAMWDTAQAKDKMDAWLSG-PNANKIevvIANNDAMAMGAVEALKAHNKSS-IPVFGVDAL 260
Cdd:cd06320 151 GFKETFK-KAPGLKLVASQPADWDRTKALDAATAILQAhPDLKGI---YAANDTMALGAVEAVKAAGKTGkVLVVGTDGI 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490522029 261 PEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKgaadgtdwKIENKVVrIPYVGVDKDNLA 326
Cdd:cd06320 227 PEAKKSIKAGELTATVAQYPYLEGAMAVEAALRLLQGQ--------KVPAVVA-TPQALITKDNVD 283
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
62-298 |
2.11e-24 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 100.24 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKepsrkaLDSYDKAYYVGTDSKESGIIQ 141
Cdd:cd19993 36 DAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDR------LIENPIAFYISFDNVEVGRMQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 142 GDLIakhwkanagwdLNKDGQIQYVLLKGEPGHPDAE---ARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWL 218
Cdd:cd19993 110 ARGV-----------LKAKPEGNYVFIKGSPTDPNADflrAGQMEVLQPAIDSGKIKIVGEQYTDGWKPANAQKNMEQIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 219 SGpNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAG 297
Cdd:cd19993 179 TA-NNNKVDAVVASNDGTAGGAVAALAAQGlAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKG 257
|
.
gi 490522029 298 K 298
Cdd:cd19993 258 T 258
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
53-316 |
1.24e-21 |
|
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: 92.87 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 53 SPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsRKALDSyDKAYYVGT 132
Cdd:cd01538 27 EKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYD----RLILNA-DVDYYISF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 133 DSKESGIIQGDLIAKhwkanagwdlnKDGQIQYVLLKGEPGHPDA---EARTTYVIKELNDKGIKTEQLQLDTAMWDTAQ 209
Cdd:cd01538 102 DNEKVGELQAQALLD-----------AKPEGNYVLIGGSPTDNNAklfRDGQMKVLQPAIDSGKIKVVGDQWVDDWLPAN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 210 AKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTVLNDANNQAKATF 288
Cdd:cd01538 171 AQQIMENALTA-NGNNVDAVVASNDGTAGGAIAALKAQGLSGgVPVSGQDADLAAIKRILAGTQTMTVYKDIRLLADAAA 249
|
250 260
....*....|....*....|....*...
gi 490522029 289 DLAknLAAGKGAADGTDWKIENKVVRIP 316
Cdd:cd01538 250 EVA--VALMRGEKPPINGTTNNGLKDVP 275
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
65-321 |
1.96e-21 |
|
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: 92.30 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 65 NDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsRKALDSyDKAYYVGTDSKESGIIQGDL 144
Cdd:cd19991 39 GDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYD----RLILNA-DVDLYVSFDNEKVGELQAEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 145 IAKHwkanagwdlnkDGQIQYVLLKGEPGHPDAE---ARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGp 221
Cdd:cd19991 114 LVKA-----------KPKGNYVLLGGSPTDNNAKlfrEGQMKVLQPLIDSGDIKVVGDQWVDDWDPEEALKIMENALTA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 222 NANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGA 300
Cdd:cd19991 182 NNNKIDAVIASNDGTAGGAIQALAEQGlAGKVAVSGQDADLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKN 261
|
250 260
....*....|....*....|.
gi 490522029 301 ADGTdwKIENKVVRIPYVGVD 321
Cdd:cd19991 262 EANR--TINNGKKEVPSILLD 280
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
38-258 |
4.25e-21 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380651 [Multi-domain] Cd Length: 302 Bit Score: 91.53 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 38 FMSVVRKAIEKDASASPDV--QLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKE 115
Cdd:cd19996 13 WRVQMIAEFEAEAAKLKKLikELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 116 PsrkalDSYDKAYYVGTDSKESGIIQGDLIAKhwkanagwDLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELND-KGIK 194
Cdd:cd19996 93 V-----GSDKYTAFVGVDDAAFGRVGAEWLVK--------QLGGKGNI--IALRGIAGVSVSEDRWAGAKEVFKEyPGIK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490522029 195 TeqLQLDTAMWDTAQAKDKMDAWLS-GPnanKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVD 258
Cdd:cd19996 158 I--VGEVYADWDYAKAKQAVESLLAaYP---DIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTGED 217
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
27-298 |
1.81e-20 |
|
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: 89.26 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAEL-GVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDLIAKHW---KANAGWDLNKDGQIQYVLLKG----EPGHPDAEa 179
Cdd:cd06322 81 IPVFTVDVKADGAKVVT-----HVGTDNYAGGKLAGEYALKALlggGGKIAIIDYPEVESVVLRVNGfkeaIKKYPNIE- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 180 rttyVIKELNDKGIKTEQLQldtAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHNKSS-IPVFGVD 258
Cdd:cd06322 155 ----IVAEQPGDGRREEALA---ATEDMLQANPDLDG------------IFAIGDPAALGALTAIESAGKEDkIKVIGFD 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490522029 259 ALPEAL-ALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:cd06322 216 GNPEAIkAIAKGGKIKADIAQQPDKIGQETVEAIVKYLAGE 256
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-276 |
1.68e-19 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 87.07 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 1 MNKKVLTL-SAVMSCMLFGTAAQAADRIGVTIYKYDDNFMSVVRKAIEKDASaSPDVQLLMNDSQNDQSKQNDQIDVLLA 79
Cdd:PRK10653 2 NMKKLATLvSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEAD-KLGYNLVVLDSQNNPAKELANVQDLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 80 KGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDLIAKHWKANAgwdlnk 159
Cdd:PRK10653 81 RGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVS-----HIASDNVAGGKMAGDFIAKKLGEGA------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 160 dgqiQYVLLKGEPGHPDAEARTTYVIKELndKGIKTEQLQLDTAMWDTAQAKDKMDAWLSgpnAN-KIEVVIANNDAMAM 238
Cdd:PRK10653 150 ----KVIQLEGIAGTSAARERGEGFKQAV--AAHKFNVLASQPADFDRTKGLNVMQNLLT---AHpDVQAVFAQNDEMAL 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 490522029 239 GAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTV 276
Cdd:PRK10653 221 GALRALQTAGKSDVMVVGFDGTPDGIKAVNRGKLAATI 258
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
62-294 |
1.81e-16 |
|
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: 78.13 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEpsrkaLDSYDKAY-YVGTDSKESGII 140
Cdd:cd19967 36 DHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLIDRE-----INAEGVAVaQIVSDNYQGAVL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 141 QGDLIAKhwkanagwDLNKDGQiqYVLLKGEPGHPDAEART---TYVIKELNDKGIKTEQlqldTAMWDTAQAKDKMDAW 217
Cdd:cd19967 111 LAQYFVK--------LMGEKGL--YVELLGKESDTNAQLRSqgfHSVIDQYPELKMVAQQ----SADWDRTEAFEKMESI 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490522029 218 L-SGPnanKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNL 294
Cdd:cd19967 177 LqANP---DIKGVICGNDEMALGAIAALKAAGRAGdVIIVGFDGSNDVRDAIKEGKISATVLQPAKLIARLAVEQADQY 252
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
26-298 |
2.45e-15 |
|
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: 74.69 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIEKdASASPDVQL--LMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKAR 103
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEA-AAKDLGVKIifVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 104 GQNIPIVFFNkepSRKALDSYDKayYVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTY 183
Cdd:cd06310 80 DKGIPVIVID---SGIKGDAYLS--YIATDNYAAGRLAAQKLAEA--------LGGKGKV--AVLSLTAGNSTTDQREEG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 184 VIKEL--NDKGIKTEQLQLdtAMWDTAQAKDKMDAWLSGpnANKIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDAL 260
Cdd:cd06310 145 FKEYLkkHPGGIKVLASQY--AGSDYAKAANETEDLLGK--YPDIDGIFATNEITALGAAVAIKSRKLSgQIKIVGFDSQ 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 490522029 261 PEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:cd06310 221 EELLDALKNGKIDALVVQNPYEIGYEGIKLALKLLKGE 258
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
35-272 |
2.99e-15 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380621 [Multi-domain] Cd Length: 278 Bit Score: 74.67 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 35 DDNFMSVVRKAIeKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGT-VIEKARGQNIPIVFFN 113
Cdd:cd19966 11 GDPFWTVVYNGA-KDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTpLIEAAKKAGIIVTSFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 114 KePSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAGwdlnkdgqiQYVLLKGEPGH-PDAEARTTYVIKELNDKG 192
Cdd:cd19966 90 T-DLPKLEYGDCGLGYVGADLYAAGYTLAKELVKRGGLKTG---------DRVFVPGLLPGqPYRVLRTKGVIDALKEAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 193 IKTEQLQLDTAMWDTAQAKDKMDAWLSgpnANK-IEVVIANNDAMAMGAVEALKAHNK--SSIPVFGVDALPEALALVKS 269
Cdd:cd19966 160 IKVDYLEISLEPNKPAEGIPVMTGYLA---ANPdVKAIVGDGGGLTANVAKYLKAAGKkpGEIPVAGFDLSPATVQAIKS 236
|
...
gi 490522029 270 GAL 272
Cdd:cd19966 237 GYV 239
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
34-276 |
5.16e-15 |
|
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: 73.77 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 34 YDDNFMSVVRKAIEKdASASPDVQLLMNDSQN-DQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFF 112
Cdd:cd06314 9 LNNPFWDLAEAGAEK-AAKELGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 113 NKEpsrkALDSYDKAyYVGTDSKESGIIQGDLIAKhwkanagwDLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELNDKG 192
Cdd:cd06314 88 DSD----APDSKRLA-YIGTDNYEAGREAGELMKK--------ALPGGGKV--AIITGGLGADNLNERIQGFKDALKGSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 193 iKTEQLQLDTAMWDTAQAKDKMDAWLSG-PNANKIEVVIANNdamAMGAVEALKAHNK-SSIPVFGVDALPEALALVKSG 270
Cdd:cd06314 153 -GIEIVDPLSDNDDIAKAVQNVEDILKAnPDLDAIFGVGAYN---GPAIAAALKDAGKvGKVKIVGFDTLPETLQGIKDG 228
|
....*.
gi 490522029 271 ALAGTV 276
Cdd:cd06314 229 VIAATV 234
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
35-276 |
1.10e-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: 380535 [Multi-domain] Cd Length: 272 Bit Score: 73.04 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 35 DDNFMSVVRKAIeKDASASPDVQL-LMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFN 113
Cdd:cd06312 11 SDPFWSVVKKGA-KDAAKDLGVTVqYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAIN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 114 KEPSRKALDSydkAY--YVGTDSKESGiiQGdliakhwkanAGWDLNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDK 191
Cdd:cd06312 90 SGDDRSKERL---GAltYVGQDEYLAG--QA----------AGERALEAGPKNALCVNHEPGNPGLEARCKGFADAFKGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 192 GIKTEQLQLDTamwDTAQAKDKMDAWLsgpNANK-IEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKS 269
Cdd:cd06312 155 GILVELLDVGG---DPTEAQEAIKAYL---QADPdTDAVLTLGPVGADPALKAVKEAGLKGkVKIGTFDLSPETLEAIKD 228
|
....*..
gi 490522029 270 GALAGTV 276
Cdd:cd06312 229 GKILFAI 235
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
27-298 |
3.28e-14 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 71.70 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd19972 2 IGLAVANLQADFFNQIKQSVEAEAKKK-GYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDLIAKHwkanagwdlnKDGQIQYVLLKGEPGHPDAEART---TY 183
Cdd:cd19972 81 IPVIAVDRNPEDAPGDT-----FIATDSVAAAKELGEWVIKQ----------TGGKGEIAILHGQLGTTPEVDRTkgfQE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 184 VIKELNDKGIKTEQlqldTAMWDTAQA-KDKMDAWLSGPNankIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALP 261
Cdd:cd19972 146 ALAEAPGIKVVAEQ----TADWDQDEGfKVAQDMLQANPN---ITVFFGQSDAMALGAAQAVKVAGLDHkIWVVGFDGDV 218
|
250 260 270
....*....|....*....|....*....|....*..
gi 490522029 262 EALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:cd19972 219 AGLKAVKDGVLDATMTQQTQKMGRLAVDSAIDLLNGK 255
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
26-302 |
3.55e-14 |
|
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: 71.55 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIEKDA-SASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARG 104
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAaEINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 105 QNIPIVffnkepsrkALDSYDKAY--YVGTDSKESGIIQGDLIAKhwkanagwDLNKDGQIqyVLLKGEPGHPD------ 176
Cdd:cd06321 81 AGIIVV---------AVDVAAEGAdaTVTTDNVQAGYLACEYLVE--------QLGGKGKV--AIIDGPPVSAVidrvng 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 177 -----AEARTTYVIKELNDKGIKTEQLqldTAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHNKSS 251
Cdd:cd06321 142 ckealAEYPGIKLVDDQNGKGSRAGGL---SVMTRMLTAHPDVDG------------VFAINDPGAIGALLAAQQAGRDD 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490522029 252 IPVFGVDALPEALALVK--SGALAGTVLNDANNQAKATFDLAKNLAAGKGAAD 302
Cdd:cd06321 207 IVITSVDGSPEAVAALKreGSPFIATAAQDPYDMARKAVELALKILNGQEPAP 259
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
20-263 |
6.06e-14 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 71.38 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 20 AAQAADRIGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKslAINLVDPAAAGTVI 99
Cdd:COG1609 57 RTGRTRTIGVVVPDLSNPFFAELLRGIEEAARER-GYQLLLANSDEDPEREREALRLLLSRRVD--GLILAGSRLDDARL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 100 EKARGQNIPIVFFNKEPSRKALDSydkayyVGTDSKESGiiqgDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEA 179
Cdd:COG1609 134 ERLAEAGIPVVLIDRPLPDPGVPS------VGVDNRAGA----RLATEH--------LIELGHRRIAFIGGPADSSSARE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 180 RTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNKsSIP----VF 255
Cdd:COG1609 196 RLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGP--RPTAIFCANDLMALGALRALREAGL-RVPedvsVV 272
|
....*...
gi 490522029 256 GVDALPEA 263
Cdd:COG1609 273 GFDDIPLA 280
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
63-256 |
2.75e-13 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380654 [Multi-domain] Cd Length: 313 Bit Score: 69.26 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 63 SQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPsrkaldSYDKAYYVGTDSKESGIIQG 142
Cdd:cd19999 42 ADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPV------SSPDAINVVIDQYKWAAIQA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 143 DLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEAR---TTYVIKElnDKGIKTeqLQLDTAMWDTAQAKDKMDAWLS 219
Cdd:cd19999 116 QWLAEQ--------LGGKGNI--VAINGVAGNPANEARvkaADDVFAK--YPGIKV--LASVPGGWDQATAQQVMATLLA 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 490522029 220 gpNANKIEVVIaNNDAMAMGAVEALKAHNKSSIPVFG 256
Cdd:cd19999 182 --TYPDIDGVL-TQDGMAEGVLRAFQAAGKDPPVMTG 215
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
34-276 |
2.85e-13 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380620 [Multi-domain] Cd Length: 272 Bit Score: 68.84 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 34 YDDNFMSVVRKAIeKDASASPDVQLLMNDSQN-DQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFF 112
Cdd:cd19965 9 TTNPFFQPVKKGM-DDACELLGAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 113 NKEpsrkALDSYDKAY-YVGTDSKESGIIQGDLIAKhwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDK 191
Cdd:cd19965 88 NVD----APGGENARLaFVGQDLYPAGYVLGKRIAE---------KFKPGGGHVLLGISTPGQSALEQRLDGIKQALKEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 192 GIKTEQLQLDTAMwDTAQAKDKMDAWLSG-PNANkieVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKS 269
Cdd:cd19965 155 GRGITYDVIDTGT-DLAEALSRIEAYYTAhPDIK---AIFATGAFDTAGAGQAIKDLGlKGKVLVGGFDLVPEVLQGIKA 230
|
....*..
gi 490522029 270 GALAGTV 276
Cdd:cd19965 231 GYIDFTI 237
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
26-297 |
3.70e-13 |
|
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380528 [Multi-domain] Cd Length: 273 Bit Score: 68.48 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIEKDASAsPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEK-LGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKEPSRKAL---DSYDKAyyVGTDSkesgiiqGDLIAKhwkanagwDLNKDGQIQYVLLKGEPghPDAEARTT 182
Cdd:cd06305 80 GIPVVTFDTDSQVPGVnniTQDDYA--LGTLS-------LGQLVK--------DLNGEGNIAVFNVFGVP--PLDKRYDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 183 YVIKELNDKGIKTEQLQLDTAMWDTAQ-AKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALP 261
Cdd:cd06305 141 YKAVLKANPGIKKIVAELGDVTPNTAAdAQTQVEALLKKYPEGGIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISN 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 490522029 262 EALALVK--SGALAGTVLNDANNQAKATFDLAKNLAAG 297
Cdd:cd06305 221 QDLELMAdeGSPWVATAAQDPALIGTVAVRNVARKLAG 258
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
38-276 |
4.59e-13 |
|
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: 68.43 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 38 FMSVVRKAIEKDASASPDVQLLMNDSQNDQS--KQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKE 115
Cdd:cd19970 13 FFIEMEKGARKHAKEANGYELLVKGIKQETDieQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 116 PSRKALDSYDKAY-YVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELNDKGIK 194
Cdd:cd19970 93 LDADALKEGGINVpFVGPDNRQGAYLAGDYLAKK--------LGKGGKV--AIIEGIPGADNAQQRKAGFLKAFEEAGMK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 195 TEQLQldTAMWDTAQAKDKMDAWLSG-PNankIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGAL 272
Cdd:cd19970 163 IVASQ--SANWEIDEANTVAANLLTAhPD---IRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKM 237
|
....
gi 490522029 273 AGTV 276
Cdd:cd19970 238 LATI 241
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
27-263 |
8.06e-13 |
|
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: 67.54 E-value: 8.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKslAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAARER-GYSLLLCNTDEDPEREREYLRLLLSRRVD--GIILAPSSLDDELLEELLAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayyVGTDSKESGIIQGD-LIAK-HWKanagwdlnkdgqIqyVLLKGEPGHPDAEARTTYV 184
Cdd:cd06267 79 IPVVLIDRRLDGLGVDS------VVVDNYAGAYLATEhLIELgHRR------------I--AFIGGPLDLSTSRERLEGY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 185 IKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNKsSIP----VFGVDAL 260
Cdd:cd06267 139 RDALAEAGLPVDPELVVEGDFSEESGYEAARELLALPP--RPTAIFAANDLMAIGALRALRELGL-RVPedisVVGFDDI 215
|
...
gi 490522029 261 PEA 263
Cdd:cd06267 216 PLA 218
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
36-276 |
1.01e-12 |
|
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: 67.63 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 36 DNFMsvvrkaieKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVD-PAAAGTVIEKARGQNIPIVFFNK 114
Cdd:cd06324 19 TRFM--------QAAAKDLGIELEVLYANRNRFKMLELAEELLARPPKPDYLILVNeKGVAPELLELAEQAKIPVFLINN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 115 EPSRKALDSYDK-----AYYVGT---DSKESGIiqgdLIAKHWkANAGWDLNKDGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06324 91 DLTDEERALLGKprekfKYWLGSivpDNEQAGY----LLAKAL-IKAARKKSDDGKIRVLAISGDKSTPASILREQGLRD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIkTEQLQLDTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNK---SSIPVFGVDALPEA 263
Cdd:cd06324 166 ALAEHPD-VTLLQIVYANWSEDEAYQKTEKLLQ--RYPDIDIVWAANDAMALGAIDALEEAGLkpgKDVLVGGIDWSPEA 242
|
250
....*....|...
gi 490522029 264 LALVKSGALAGTV 276
Cdd:cd06324 243 LQAVKDGELTASV 255
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
62-325 |
1.03e-11 |
|
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380523 [Multi-domain] Cd Length: 302 Bit Score: 64.65 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsrKALDSYDkAYYVGTDSKESGIIQ 141
Cdd:cd06300 41 NSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFD-----GAVTSPD-AYNVSNDQVEWGRLG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 142 GDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELnDKGIKTEQLQLDTAMWDTAQAKDKMDAWL-SG 220
Cdd:cd06300 115 AKWLFEA--------LGGKGNV--LVVRGIAGAPASADRHAGVKEAL-AEYPGIKVVGEVFGGWDEATAQTAMLDFLaTH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 221 PNANKievvIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKsgalagtvLNDANNQAKATF----DLAKNLAA 296
Cdd:cd06300 184 PQVDG----VWTQGGEDTGVLQAFQQAGRPPVPIVGGDENGFAKQWWK--------HPKKGLTGAAVWpppaIGAAGLEV 251
|
250 260
....*....|....*....|....*....
gi 490522029 297 GKGAADGTDWKIenKVVRIPYVGVDKDNL 325
Cdd:cd06300 252 ALRLLEGQGPKP--QSVLLPPPLITNDDA 278
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
27-325 |
1.07e-11 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 64.32 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAieKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06317 3 ALVQINQQAQFFNQINQGA--QAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNkepsrKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06317 81 IPVIAYD-----AVIPSDFQAAQVGVDNLEGGKEIGKYAADYIKAE----LGGQAKIGVVGALSSLIQNQRQKGFEEALK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIKTE---QLQLDTAMwdtAQAKDKMDAwlsgpNANkIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPE 262
Cdd:cd06317 152 ANPGVEIVATvdgQNVQEKAL---SAAENLLTA-----NPD-LDAIYATGEPALLGAVAAVRSQGRQgKIKVFGWDLTKQ 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490522029 263 -ALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKgaadgtdwKIEnKVVRIPYVGVDKDNL 325
Cdd:cd06317 223 aIFLGIDEGVLQAVVQQDPEKMGYEAVKAAVKAIKGE--------DVE-KTIDVPPTIVTKENV 277
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
62-276 |
1.16e-11 |
|
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 64.28 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEpsrkALDSyDKAYYVGTDSKESGIIQ 141
Cdd:cd19969 37 PATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSD----APES-KRISYVGTDNYEAGYAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 142 GDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPD---------AEARTTYVIKELNDKGIKTEQLQLDTAMwdtAQAKD 212
Cdd:cd19969 112 AEKLAEL--------LGGKGKVAVLTGPGQPNHEErvegfkeafAEYPGIEVVAVGDDNDDPEKAAQNTSAL---LQAHP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490522029 213 KMDAWLsGPNANKievvianndamAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTV 276
Cdd:cd19969 181 DLVGIF-GVDASG-----------GVGAAQAVREAGKTGkVKIVAFDDDPETLDLIKDGVIDASI 233
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
1-279 |
2.17e-11 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 63.74 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 1 MNKKVLTLSAVMSCMLFGTAAQAADRIGVTIYKYDDNFMSVVRKAIEKDASASP-DVQLLMNDSQNDQSKQNDQIDVLLA 79
Cdd:PRK09701 1 MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGvSVDIFASPSEGDFQSQLQLFEDLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 80 KGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDSYDKAY--YVGTDSKESGIIQGDLIAKHWKANAGwdl 157
Cdd:PRK09701 81 KNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKKAGGNVeaFVTTDNVAVGAKGASFIIDKLGAEGG--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 158 nkdgqiQYVLLKGEPGHPDAEAR---TTYVIKElnDKGIKTEQLQldTAMWDTAQAKDKMDAWLS-GPNankIEVVIANN 233
Cdd:PRK09701 158 ------EVAIIEGKAGNASGEARrngATEAFKK--ASQIKLVASQ--PADWDRIKALDVATNVLQrNPN---IKAIYCAN 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490522029 234 DAMAMGAVEALK-AHNKSSIPVFGVDALPEALALVKSGALAGTVLND 279
Cdd:PRK09701 225 DTMAMGVAQAVAnAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQN 271
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
62-323 |
3.60e-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: 380660 [Multi-domain] Cd Length: 274 Bit Score: 59.56 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsrKALDSYDKAYYVGTDSKESGIIQ 141
Cdd:cd20005 38 DTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFD-----SGVPSDLPLATVATDNYAAGALA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 142 GDLIAKhwkanagwdlNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDK--GIKTEQLQLDTAmwDTAQAKDKMDAWLS 219
Cdd:cd20005 113 ADHLAE----------LIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKypDIKVVNVQYGVG--DHAKAADIAKAILQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 220 G-PNankIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAG 297
Cdd:cd20005 181 AnPD---LKGIYATNEGAAIGVANALKEMGKlGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAAVKALKG 257
|
250 260
....*....|....*....|....*.
gi 490522029 298 KGAAdgtdwkienKVVRIPYVGVDKD 323
Cdd:cd20005 258 EEVE---------KLIDTGAKWYDKD 274
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
64-280 |
1.27e-08 |
|
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: 54.93 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 64 QNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsrKALDSYDKAYYVGTDSKESGIIQGD 143
Cdd:cd20004 40 EDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIID-----SDLGGDAVISFVATDNYAAGRLAAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 144 LIAKhwkanagwDLNKDGQIqyVLLKGEPGHPDAEART---TYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSG 220
Cdd:cd20004 115 RMAK--------LLNGKGKV--ALLRLAKGSASTTDRErgfLEALKKLAPGLKVVDDQYAGGTVGEARSSAENLLNQYPD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490522029 221 PNAnkievVIANNDAMAMGAVEALKAHNKSSIPVF-GVDALPEALALVKSGALAGTVLNDA 280
Cdd:cd20004 185 VDG-----IFTPNESTTIGALRALRRLGLAGKVKFiGFDASDLLLDALRAGEISALVVQDP 240
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
65-298 |
2.14e-08 |
|
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.
Pssm-ID: 380529 [Multi-domain] Cd Length: 269 Bit Score: 54.51 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 65 NDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDL 144
Cdd:cd06306 41 TNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNGIDSPKVAA-----RVLVDFYDMGYLAGEY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 145 IAKHwkanagwdlNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTeqlqLDTAMWDT--AQAKDKMDAWL-SGP 221
Cdd:cd06306 116 LVEH---------HPGKPVKVAWFPGPAGAGWAEDREKGFKEALAGSNVEI----VATKYGDTgkAVQLNLVEDALqAHP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490522029 222 NANkievVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:cd06306 183 DID----YIVGNAVAAEAAVGALREAGLTGkVKVVSTYLTPGVYRGIKRGKILAAPSDQPVLQGRIAVDQAVRALEGK 256
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
26-302 |
9.69e-08 |
|
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: 52.62 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 26 RIGVTIYKYDDNFMSVVRKAIEKdASASPDVQLLMN--DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKAR 103
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEK-AAKELGVEVTFLgpATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 104 gQNIPIVFFNkepSRKALDSYDKAYyvGTDSKESGIIQGDLIAKHWKANAGwdlnKDGQIqyVLLKGEPGHPDAEARTTY 183
Cdd:cd20008 80 -AGIPVVLVD---SGANTDDYDAFL--ATDNVAAGALAADELAELLKASGG----GKGKV--AIISFQAGSQTLVDREEG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 184 VIKEL--NDKGIKTEQLQLDTAmwDTAQAKDKM-DAWLSGPNANKIevvIANNDAMAMGAVEALKAHNKS-SIPVFGVDA 259
Cdd:cd20008 148 FRDYIkeKYPDIEIVDVQYSDG--DIAKALNQTtDLLTANPDLVGI---FGANNPSAVGVAQALAEAGKAgKIVLVGFDS 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490522029 260 LPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAAD 302
Cdd:cd20008 223 SPDEVALLKSGVIKALVVQDPYQMGYEGVKTAVKALKGEEIVE 265
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
1-325 |
1.29e-07 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 52.44 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 1 MNKKVLTLSAVMSCMLFGTAAQAAD-RIGVTIykyDDNFMSVVRK--AIEKDASASPDVQLLMNDSQNDQSKQNDQIDVL 77
Cdd:PRK10355 1 MKIKNILLTLCASLLLTSVAAHAKEvKIGMAI---DDLRLERWQKdrDIFVKKAESLGAKVFVQSANGNEETQMSQIENM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 78 LAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDsydkaYYVGTDSKESGIIQGDLIakhwkanagwdL 157
Cdd:PRK10355 78 INRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADID-----FYISFDNEKVGELQAKAL-----------V 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 158 NKDGQIQYVLLKGEPGHPDAE---ARTTYVIKELNDKG-IKTEQLQLDTAmWDTAQAKDKMDAWLSGpNANKIEVVIANN 233
Cdd:PRK10355 142 DKVPQGNYFLMGGSPVDNNAKlfrAGQMKVLKPYIDSGkIKVVGDQWVDG-WLPENALKIMENALTA-NNNKIDAVVASN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 234 DAMAMGAVEALKAHNKS-SIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLaaGKGAADGTDWKIENKV 312
Cdd:PRK10355 220 DATAGGAIQALSAQGLSgKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVEL--GNGEEPKANTTLNNGL 297
|
330
....*....|....*...
gi 490522029 313 VRIPY-----VGVDKDNL 325
Cdd:PRK10355 298 KDVPSrlltpIDVNKNNI 315
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
58-263 |
3.21e-07 |
|
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: 50.64 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 58 LLMNDSQNDQSKQNDQIDVLLAKGVKSLAINlvdpAAAGT---VIEKARGQNIPIVFFNKEPSRKALDsydkayYVGTDS 134
Cdd:cd06289 32 VFLANTGEDPERQRRFLRRMLEQGVDGLILS----PAAGTtaeLLRRLKAWGIPVVLALRDVPGSDLD------YVGIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 135 KESGiiqgDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARttyviKELNDKGIKTEQLQLDTAMW-----DTAQ 209
Cdd:cd06289 102 RLGA----QLATEH--------LIALGHRRIAFLGGLSDSSTRRER-----LAGFRAALAEAGLPLDESLIvpgpaTREA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490522029 210 AKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKSS---IPVFGVDALPEA 263
Cdd:cd06289 165 GAEAARELLD--AAPPPTAVVCFNDLVALGAMLALRRRGLEPgrdIAVVGFDDVPEA 219
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
27-246 |
5.31e-07 |
|
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: 50.33 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEkDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLainLVDPAAAGT-VIEKARGQ 105
Cdd:cd06280 2 IGLIVPDITNPFFTTIARGIE-DAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGI---ILAPSAGPSrELKRLLKH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKEPSRKALDSydkayyVGTDSKESGIIqgdlIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd06280 78 GIPIVLIDREVEGLELDL------VAGDNREGAYK----AVKH--------LIELGHRRIGLITGPLEISTTRERLAGYR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490522029 186 KELNDKGIKTEQ---LQLDTAMWDTAQAkdkMDAWLSGPNAnkIEVVIANNDAMAMGAVEALKA 246
Cdd:cd06280 140 EALAEAGIPVDEsliFEGDSTIEGGYEA---VKALLDLPPR--PTAIFATNNLMAVGALRALRE 198
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
27-254 |
5.49e-07 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 50.06 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQsKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06311 2 IGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNAN-EQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEpsrkaLDSYDKAYYVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06311 81 IPVVNFDRG-----LNVLIYDLYVAGDNPGMGVVSAEYIGKK--------LGGKGNV--VVLEVPSSGSVNEERVAGFKE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490522029 187 ELNDK-GIKTEQLQLDTAMWDTAqAKDKMDAWLSGPnanKIEVVIANNDAMAMGAVEALKAHNKSSIPV 254
Cdd:cd06311 146 VIKGNpGIKILAMQAGDWTREDG-LKVAQDILTKNK---KIDAVWAADDDMAIGVLQAIKEAGRTDIKV 210
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
24-263 |
5.57e-07 |
|
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: 50.20 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 24 ADRIGVtIYKYDDN--FMSVVrKAIEKDASASP-DVQLLMNDSQNDQSKQndQIDVLLAKGVKSLAINLVDPAAAgTVIE 100
Cdd:pfam00532 1 TLKLGA-LVPQLDEpfFQDLV-KGITKAAKDHGfDVFLLAVGDGEDTLTN--AIDLLLASGADGIIITTPAPSGD-DITA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 101 KARGQNIPIVFFNKepsrkALDSYDKAYYVGTDSKESGiiqgdliakhwkANAGWDLNKDGQIQYVLLKGEP-GHPDAEA 179
Cdd:pfam00532 76 KAEGYGIPVIAADD-----AFDNPDGVPCVMPDDTQAG------------YESTQYLIAEGHKRPIAVMAGPaSALTARE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 180 RTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNKSSIP----- 253
Cdd:pfam00532 139 RVQGFMAALAAAGREVKIYHVATGDNDIPDAALAANAMLvSHPT---IDAIVAMNDEAAMGAVRALLKQGRVKIPdivgi 215
|
250
....*....|....
gi 490522029 254 ----VFGVDALPEA 263
Cdd:pfam00532 216 ginsVVGFDGLSKA 229
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
58-253 |
1.10e-06 |
|
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: 49.06 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 58 LLMNdSQNDQSKQNDQIDVLLAkgvkslaiNLVD---PAAAGTVIEKARGQNIPIVFFNKEPSrkaldsyDKAYYVGTDS 134
Cdd:cd06291 33 ILCN-SNEDEEKEKEYLEMLKR--------NKVDgiiLGSHSLDIEEYKKLNIPIVSIDRYLS-------EGIPSVSSDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 135 KESGIiqgdLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKM 214
Cdd:cd06291 97 YQGGR----LAAEH--------LIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFSEEDAYELA 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 490522029 215 DAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKsSIP 253
Cdd:cd06291 165 KELLE--KYPDIDGIFASNDLLAIGVLKALQKLGI-RVP 200
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
27-263 |
1.11e-06 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 49.15 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEkDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKslAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIE-DAARERGYTVLLADTGDDPERELAALDSLLSRRVD--GLIITPARDDAPDLQELAARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayyVGTDSkESGiiqGDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06285 79 VPVVLVDRRIGDTALPS------VTVDN-ELG---GRLATRH--------LLELGHRRIAVVAGPLNASTGRDRLRGYRR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPN---AnkievVIANNDAMAMGAVEALKAHNKsSIP----VFGVDA 259
Cdd:cd06285 141 ALAEAGLPVPDERIVPGGFTIEAGREAAYRLLSRPErptA-----VFAANDLMAIGVLRAARDLGL-RVPedlsVVGFDD 214
|
....
gi 490522029 260 LPEA 263
Cdd:cd06285 215 IPLA 218
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
63-316 |
1.15e-06 |
|
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380525 [Multi-domain] Cd Length: 296 Bit Score: 49.16 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 63 SQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDsydkaYYV-GTDSKESGIIQ 141
Cdd:cd06302 38 TQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSDAPPSARD-----YFVnQADDEGLGEAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 142 GDLIAKhwkanagwdlNKDGQIQYVLLKGEPGHPD----AEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAW 217
Cdd:cd06302 113 VDSLAK----------EIGGKGKVAILSGSLTATNlnawIKAMKEYLKSKYPDIELVDTYYTDDDQQKAYTQAQNLIQAY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 218 lsgPNankIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVdALP-EALALVKSGALAGTVLNDANNQAKATFDLAKNLA 295
Cdd:cd06302 183 ---PD---LKGIIGVSTTAPPAAAQAVEEAGKTgKVAVTGI-GLPnTARPYLKDGSVKEGVLWDPAKLGYLTVYAAYQLL 255
|
250 260
....*....|....*....|.
gi 490522029 296 AGKGAADGTDWKIENKVVRIP 316
Cdd:cd06302 256 KGKGFTEDSDDVGTGGKVKVD 276
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
38-247 |
4.81e-06 |
|
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: 47.25 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 38 FMSVVRkAIEkDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLainLVDPAAAGTVIEK--ARGQNIPIVFFNKE 115
Cdd:cd06275 14 FAEVVR-GVE-DACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGL---LLMCSEMTDDDAEllAALRSIPVVVLDRE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 116 PSRKALDSydkayyVGTDSkESGiiqGDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKT 195
Cdd:cd06275 89 IAGDNADA------VLDDS-FQG---GYLATRH--------LIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490522029 196 EQLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAH 247
Cdd:cd06275 151 PPSWIVEGDFEPEGGYEAMQRLLSQPP--RPTAVFACNDMMALGALRAAQEQ 200
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
63-256 |
5.70e-06 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380653 [Multi-domain] Cd Length: 302 Bit Score: 47.28 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 63 SQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPsrkaldSYDKAYYVGTDSKESGIIQG 142
Cdd:cd19998 41 SGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVV------DEPCAYNVNTDQAKAGEQTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 143 DLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEART---TYVIKELNDKGIKTEQlqldTAMWDTAQAKDKMDAWLs 219
Cdd:cd19998 115 QWLVDK--------LGGKGNI--LMVRGVPGTSVDRDRYegaKEVFKKYPDIKVVAEY----YGNWDDGTAQKAVADAL- 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 490522029 220 gPNANKIEVVIAnNDAMAmGAVEALKAHNKSSIPVFG 256
Cdd:cd19998 180 -AAHPDVDGVWT-QGGET-GVIKALQAAGHPLVPVGG 213
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
27-267 |
6.98e-06 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380513 [Multi-domain] Cd Length: 267 Bit Score: 46.84 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLainLVDPAAAGTVIEKARGQN 106
Cdd:cd06290 2 IGVLVPDIDSPFYSEILNGIEEVLAES-GYTLIVSTSHWNADRELEILRLLLARKVDGI---IVVGGFGDEELLKLLAEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayyVGTDSKESGIIqgdlIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06290 78 IPVVLVDRELEGLNLPV------VNVDNEQGGYN----ATNH--------LIDLGHRRIVHISGPEDHPDAQERYAGYRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIK-----------TEQLQLDtAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHnKSSIP-- 253
Cdd:cd06290 140 ALEDAGLEvdprlivegdfTEESGYE-AMKKLLKRGGPFTA------------IFAANDLMALGAMKALREA-GIRVPdd 205
|
250
....*....|....*.
gi 490522029 254 --VFGVDALPEALALV 267
Cdd:cd06290 206 vsVIGFDDLPFSKYTT 221
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
58-263 |
2.06e-05 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 45.22 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 58 LLMNDSQNDQskQNDQIDVLLAKGVKSLAINLVDPAAAgtVIEKARGQNIPIVFFNKEPSRKALDSydkayyVGTDSKES 137
Cdd:cd06278 33 LLFNVDDEDD--VDDALRQLLQYRVDGVIVTSATLSSE--LAEECARRGIPVVLFNRVVEDPGVDS------VSCDNRAG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 138 GiiqgDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIktEQLQLDTAMWDTAQAKDKMDAW 217
Cdd:cd06278 103 G----RLAADL--------LLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGL--PPPAVEAGDYSYEGGYEAARRL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490522029 218 LSGPNAnkIEVVIANNDAMAMGAVEALKAHNKSSIP----VFGVDALPEA 263
Cdd:cd06278 169 LAAPDR--PDAIFCANDLMALGALDAARQEGGLVVPedisVVGFDDIPMA 216
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
62-327 |
3.72e-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: 380539 [Multi-domain] Cd Length: 294 Bit Score: 44.54 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPS-RKALDSYdkAYYVGTDSKESGII 140
Cdd:cd06316 37 DANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKLVFMDNVPDgLEAGKDY--VSVVSSDNRGNGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 141 QGDLIAKHwkanagwdLNKDGQIQYVllkgepGHP---------DAEARTTyvIKELNDkGIKTEQLQLDTAMWDTAQ-A 210
Cdd:cd06316 115 AAELLAEA--------IGGKGKVGII------YHDadfyatnqrDKAFKDT--LKEKYP-DIKIVAEQGFADPNDAEEvA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 211 KDKMDAWlsgPNANKIEVVIannDAMAMGAVEALKAHNKSSIPVFGVDALPE-ALALVKSGALAGTVLNDANNQAKATFD 289
Cdd:cd06316 178 SAMLTAN---PDIDGIYVSW---DTPALGVISALRAAGRSDIKITTVDLGTEiALDMAKGGNVKGIGAQRPYDQGVAEAL 251
|
250 260 270
....*....|....*....|....*....|....*...
gi 490522029 290 LAKNLAAGKGAAdgtdwkienKVVRIPYVGVDKDNLAE 327
Cdd:cd06316 252 AAALALLGKEVP---------PFIGVPPLAVTKDNLLE 280
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
173-263 |
7.84e-05 |
|
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: 43.67 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 173 GHPDAEARTTYVIKELNDKGIKTEQLQLDTAmWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKsSI 252
Cdd:cd01544 129 GEEIEDPRLRAFREYMKEKGLYNEEYIYIGE-FSVESGYEAMKELLK--EGDLPTAFFVASDPMAIGALRALQEAGI-KV 204
|
90
....*....|....*
gi 490522029 253 P----VFGVDALPEA 263
Cdd:cd01544 205 PedisIISFNDIEVA 219
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
163-263 |
1.71e-04 |
|
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: 41.55 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 163 IQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSG-PNAnkievVIANNDAMAMGAV 241
Cdd:pfam13377 10 IALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGAlPTA-----VFVANDEVALGVL 84
|
90 100
....*....|....*....|....*.
gi 490522029 242 EALKAHNKsSIP----VFGVDALPEA 263
Cdd:pfam13377 85 QALREAGL-RVPedlsVIGFDDSPLA 109
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
31-275 |
2.53e-04 |
|
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: 42.07 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 31 IYKYDDN-FMSVVRKAIEKDASA-SPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIP 108
Cdd:cd19973 5 ITKTDTNpFFVKMKEGAQKAAKAlGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 109 IVFFNK--EPsrkaLDSYDKAYyvGTDSKESGIiqgdLIAKHWKANAGwdlNKDGQIqyVLLKGEPGHPDAEAR-----T 181
Cdd:cd19973 85 VIALDTptDP----IDAADATF--ATDNFKAGV----LIGEWAKAALG---AKDAKI--ATLDLTPGHTVGVLRhqgflK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 182 TYVIKELNDKGIKTEQ----LQLDTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFG 256
Cdd:cd19973 150 GFGIDEKDPESNEDEDdsqvVGSADTNGDQAKGQTAMENLLQ--KDPDINLVYTINEPAAAGAYQALKAAGKEKgVLIVS 227
|
250
....*....|....*....
gi 490522029 257 VDALPEALALVKSGALAGT 275
Cdd:cd19973 228 VDGGCPGVKDVKDGIIGAT 246
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
55-277 |
3.29e-04 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 41.81 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 55 DVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEpsrkaLDSYDKAYYVGTDS 134
Cdd:cd20006 33 DLEFLGPESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSP-----VNSKKADSFVATDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 135 KESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELNDKG---IKTEQLQLDtamwDTAQAK 211
Cdd:cd20006 108 YEAGKKAGEKLASL--------LGEKGKV--AIVSFVKGSSTAIEREEGFKQALAEYPnikIVETEYCDS----DEEKAY 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490522029 212 DKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKA-HNKSSIPVFGVDALPEALALVKSGALAGTVL 277
Cdd:cd20006 174 EITKELLS--KYPDINGIVALNEQSTLGAARALKElGLGGKVKVVGFDSSVEEIQLLEEGIIDALVV 238
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
27-246 |
1.97e-03 |
|
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: 39.46 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 27 IGVTIYKYDDNFMSVVRKAIEkDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVdpAAAGTVIEKARGQN 106
Cdd:cd06283 2 IGVIVADITNPFSSLLLKGIE-DVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPT--GNNNDAYLELAQKG 78
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayyVGTDSKESGIIQGDLIAKHwkanaGWDlnkdgqiQYVLLKGEPGHPDA-EARTTYVI 185
Cdd:cd06283 79 LPVVLVDRQIEPLNWDT------VVTDNYDATYEATEHLKEQ-----GYE-------RIVFVTEPIKGISTrRERLQGFL 140
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170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490522029 186 KELNDKGIKTEQLQLDTAmwDTAQAKDKMDAWLSGPNANKIeVVIANNDAMAMGAVEALKA 246
Cdd:cd06283 141 DALARYNIEGDVYVIEIE--DTEDLQQALAAFLSQHDGGKT-AIFAANGVVLLRVLRALKA 198
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| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
66-298 |
3.54e-03 |
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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: 38.37 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 66 DQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFfnkepsrkaLDSY--DKAY---YVGTDSKESGII 140
Cdd:cd20007 41 DPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVT---------VDTTlgDPSFvlsQIASDNVAGGAL 111
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 141 QGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELnDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSg 220
Cdd:cd20007 112 AAEALAEL--------IGGKGKV--LVINSTPGVSTTDARVKGFAEEM-KKYPGIKVLGVQYSENDPAKAASIVAAALQ- 179
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 221 pnANK-IEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:cd20007 180 --ANPdLAGIFGTNTFSAEGAAAALRNAGKTgKVKVVGFDASPAQVEQLKAGTIDALIAQKPAEIGYLAVEQAVAALTGK 257
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| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
170-258 |
4.00e-03 |
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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: 38.30 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 170 GEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNK 249
Cdd:cd06288 124 GPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHGDWGRESGYEAAKRLLSAPD--RPTAIFCGNDRMAMGVYQAAAELGL 201
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90
....*....|...
gi 490522029 250 sSIP----VFGVD 258
Cdd:cd06288 202 -RVPedlsVVGFD 213
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| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
170-277 |
5.64e-03 |
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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: 38.00 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 170 GEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHN 248
Cdd:cd06295 131 GDPPHPEVADRLQGYRDALAEAGLEADPSLLLSCDFTEESGYAAMRALLdSGTA---FDAIFAASDLIAMGAIRALRERG 207
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90 100 110 120
....*....|....*....|....*....|....*....|
gi 490522029 249 KsSIP----VFGVDALPEA------LALVK-SGALAGTVL 277
Cdd:cd06295 208 I-SVPgdvaVVGYDDIPLAayfrppLTTVRqDLALAGRLL 246
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