|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
2-331 |
0e+00 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 657.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 2 NKKVLTLSAVMASMLFGAAAHAADTRIGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAK 81
Cdd:PRK15395 1 NKKVLTLSALMASMLFGAAAAAADTRIGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 82 GVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANPNWDLNKD 161
Cdd:PRK15395 81 GVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANPAWDLNKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 162 GQIQFVLLKGEPGHPDAEARTTYVVKELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 241
Cdd:PRK15395 161 GKIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 242 VEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKIVRVPYVGV 321
Cdd:PRK15395 241 VEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAEGTNWKIENKVVRVPYVGV 320
|
330
....*....|
gi 504645589 322 DQSNLAEFIG 331
Cdd:PRK15395 321 DKDNLAEFTK 330
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
27-321 |
3.30e-157 |
|
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: 442.02 E-value: 3.30e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQ 106
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 107 NVPIVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANPNWDLNKDGQIQFVLLKGEPGHPDAEARTTYVV 186
Cdd:cd01539 82 NIPVIFFNREPSREDLKSYDKAYYVGTDAEESGIMQGEIIADYWKANPEIDKNGDGKIQYVMLKGEPGHQDAIARTKYSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 187 KELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSGPNaNKIEVVIANNDAMAMGAVEALKAHN------KSSIPVFGVDA 260
Cdd:cd01539 162 KTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYG-DKIELVIANNDDMALGAIEALKAAGyntgdgDKYIPVFGVDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504645589 261 LPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAADGTN-WKIDNKIVRVPYVGV 321
Cdd:cd01539 241 TPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLETGYkFLVEGKYVRIPYKKV 302
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
27-320 |
4.79e-119 |
|
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: 343.84 E-value: 4.79e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAaPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGtVIEKARGQ 106
Cdd:cd01537 1 RIGVTIYSYDDNFMSVIRKAIEQDAKQ-PGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAG-VAEKARGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 107 NVPIVFFNKEPSRkaldsYDKAYYVGTDSKESGIIQGDLIAKHWaanpnwdlnkdgQIQFVLLKGEPGHPDAEARTTYVV 186
Cdd:cd01537 79 NVPVVFFDKEPSR-----YDKAYYVITDSKEGGIIQGDLLAKHG------------HIQIVLLKGPLGHPDAEARLAGVI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 187 KELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSGPnaNKIEVVIANNDAMAMGAVEALKAHNK---SSIPVFGVDALPE 263
Cdd:cd01537 142 KELNDKGIKTEQLQLDTGDWDTASGKDKMDQWLSGP--NKPTAVIANNDAMAMGAVEALKEHGLrvpSDISVFGYDALPE 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 504645589 264 ALalvKSGAMAGTVLNDANNQAKATFDLAKNLADgkgaadgtNWKIDNKIVRVPYVG 320
Cdd:cd01537 220 AL---KSGPLLTTILQDANNLGKTTFDLLLNLAD--------NWKIDNKVVRVPYVL 265
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
5-326 |
6.45e-61 |
|
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: 197.07 E-value: 6.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 5 VLTLSAVMASMLFGAAAHAADTRIGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVK 84
Cdd:COG1879 13 ALALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKEL-GVELIVVDAEGDAAKQISQIEDLIAQGVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 85 ALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPsrkalDSYDKAYYVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQI 164
Cdd:COG1879 92 AIIVSPVDPDALAPALKKAKAAGIPVVTVDSDV-----DGSDRVAYVGSDNYAAGRLAAEYLAKA--------LGGKGKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 165 qfVLLKGEPGHPDAEARTTYVVKELNDKGlKTQQLALDTAMWDTAQAKDKMDAWLSgpnAN-KIEVVIANNDAMAMGAVE 243
Cdd:COG1879 159 --AILTGSPGAPAANERTDGFKEALKEYP-GIKVVAEQYADWDREKALEVMEDLLQ---AHpDIDGIFAANDGMALGAAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 244 ALKAHNKSS-IPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAdgtnwkidnKIVRVPYVGVD 322
Cdd:COG1879 233 ALKAAGRKGdVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVP---------KEILTPPVLVT 303
|
....
gi 504645589 323 QSNL 326
Cdd:COG1879 304 KENV 307
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
27-299 |
5.32e-59 |
|
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: 190.86 E-value: 5.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQ 106
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKEL-GVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 107 NVPIVFFNkepsRKALDSYDKAYYVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTTYVV 186
Cdd:cd01536 80 GIPVVAVD----TDIDGGGDVVAFVGTDNYEAGKLAGEYLAEA--------LGGKGKV--AILEGPPGSSTAIDRTKGFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 187 KELNDKGlKTQQLALDTAMWDTAQAKDKMDAWLsgpNAN-KIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEA 264
Cdd:cd01536 146 EALKKYP-DIEIVAEQPANWDRAKALTVTENLL---QANpDIDAVFAANDDMALGAAEALKAAGRTGdIKIVGVDGTPEA 221
|
250 260 270
....*....|....*....|....*....|....*
gi 504645589 265 LALVKSGAMAGTVLNDANNQAKATFDLAKNLADGK 299
Cdd:cd01536 222 LKAIKDGELDATVAQDPYLQGYLAVEAAVKLLNGE 256
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
28-299 |
2.04e-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: 189.06 E-value: 2.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQN 107
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNKEpsrkaLDSYDKAYYVGTDSKESGIIQGDLIAKHWaanpnwdlnkDGQIQFVLLKGEPGHPDAEARTTYVVK 187
Cdd:pfam13407 81 IPVVTFDSD-----APSSPRLAYVGFDNEAAGEAAGELLAEAL----------GGKGKVAILSGSPGDPNANERIDGFKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 188 ELNDKGLKTQQLAL-DTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIP-VFGVDALPEAL 265
Cdd:pfam13407 146 VLKEKYPGIKVVAEvEGTNWDPEKAQQQMEALLTA-YPNPLDGIISPNDGMAGGAAQALEAAGLAGKVvVTGFDATPEAL 224
|
250 260 270
....*....|....*....|....*....|....
gi 504645589 266 ALVKSGAMAGTVLNDANNQAKATFDLAKNLADGK 299
Cdd:pfam13407 225 EAIKDGTIDATVLQDPYGQGYAAVELAAALLKGK 258
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
28-298 |
9.49e-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: 187.44 E-value: 9.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQN 107
Cdd:cd06301 3 IGVSMQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNKEPSrkalDSYDKAYYVGTDSKESGIIQGDLIAKhwaanpnwdlNKDGQIQFVLLKGEPGHPDAEARTTYVVK 187
Cdd:cd06301 83 IPLVYVNREPD----SKPKGVAFVGSDDIESGELQMEYLAK----------LLGGKGNIAILDGVLGHEAQILRTEGNKD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 188 ELND-KGLKTqqLALDTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEAL 265
Cdd:cd06301 149 VLAKyPGMKI--VAEQTANWSREKAMDIVENWLQ--SGDKIDAIVANNDEMAIGAILALEAAGKKdDILVAGIDATPDAL 224
|
250 260 270
....*....|....*....|....*....|...
gi 504645589 266 ALVKSGAMAGTVLNDANNQAKATFDLAKNLADG 298
Cdd:cd06301 225 KAMKAGRLDATVFQDAAGQGETAVDVAVKAAKG 257
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
27-330 |
1.90e-46 |
|
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: 158.59 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAaPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQ 106
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKE-LNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 107 NVPIVFFNKepsrkALDSYDKAYYVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTTYVV 186
Cdd:cd06313 80 GIPLVGVNA-----LIENEDLTAYVGSDDVVAGELEGQAVADR--------LGGKGNV--VILEGPIGQSAQIDRGKGIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 187 KELNDK-GLKTqqLALDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEAL 265
Cdd:cd06313 145 NVLKKYpDIKV--LAEQTANWSRDEAMSLMENWLQA-YGDEIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDAL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504645589 266 ALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAadgtnwkidNKIVRVPYVGVDQSNLAEFI 330
Cdd:cd06313 222 QAVKSGELIATVLQDAEAQGKGAVEVAVDAVKGEGV---------EKKYYIPFVLVTKDNVDDYL 277
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
44-319 |
4.64e-38 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 136.95 E-value: 4.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 44 RKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPSRKALD 123
Cdd:cd19992 18 KEYMEEEAKEL-GVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDRLILNADVD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 124 sydkaYYVGTDSKESGIIQGDLIAKhWAANPNWdlnkdgqiqfVLLKGEPGHPDAEARTTYVVKELNDKGLKTQ-QLALD 202
Cdd:cd19992 97 -----LYVGRDNYKVGQLQAEYALE-AVPKGNY----------VILSGDPGDNNAQLITAGAMDVLQPAIDSGDiKIVLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 203 TAM--WDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGAMAGTVLN 279
Cdd:cd19992 161 QYVkgWSPDEAMKLVENALTA-NNNNIDAVLAPNDGMAGGAIQALKAQGlAGKVFVTGQDAELAALKRIVEGTQTMTVWK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 504645589 280 DANNQAKATFDLAKNLADGKgAADGTNWKIDNKIVRVPYV 319
Cdd:cd19992 240 DLKELARAAADAAVKLAKGE-KPQTTDETINNGGKDVPAI 278
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
44-328 |
5.40e-34 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 126.79 E-value: 5.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 44 RKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVffnkepsrkald 123
Cdd:COG4213 21 GDNFKAALKEL-GYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVI------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 124 SYDK-------AYYVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQIQFVLLKGEPGhpDAEARTTY-----VVKELND 191
Cdd:COG4213 88 AYDRlilnsdvDYYVSFDNVKVGELQGQYLVDG--------LPLKGKGNIELFGGSPT--DNNATLFFegamsVLQPYID 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 192 KG---LKTQQLALDtamWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVF-GVDALPEALAL 267
Cdd:COG4213 158 SGklvVVSGQWTLG---WDPETAQKRMENLLTA-NGNKVDAVLAPNDGLAGGIIQALKAQGLAGKVVVtGQDAELAAVQR 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504645589 268 VKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAdgTNWKIDNKIVRVPY-----VGVDQSNLAE 328
Cdd:COG4213 234 ILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPE--VNGTYDNGKKDVPSyllepVAVTKDNVKE 297
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
36-299 |
2.55e-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: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 36 DDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFnk 115
Cdd:cd06308 10 NDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 116 epSRKaLDSYDKAYYVGTDSKESGIIQGDLIAKhwaanpnwDLNKDGQIqfVLLKGEPGHPDAEARTTYVVKELNdKGLK 195
Cdd:cd06308 88 --DRK-VSGDDYTAFIGADNVEIGRQAGEYIAE--------LLNGKGNV--VEIQGLPGSSPAIDRHKGFLEAIA-KYPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 196 TQQLALDTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDALPEAL-ALVKSGAM 273
Cdd:cd06308 154 IKIVASQDGDWLRDKAIKVMEDLLQ--AHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGLPEAGeKAVKDGIL 231
|
250 260
....*....|....*....|....*.
gi 504645589 274 AGTVLNDANnqAKATFDLAKNLADGK 299
Cdd:cd06308 232 AATFLYPTG--GKEAIEAALKILNGE 255
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
28-277 |
8.13e-30 |
|
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: 114.70 E-value: 8.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQN 107
Cdd:cd06323 2 IGLSVSTLNNPFFVSLKDGAQAEAKEL-GVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNkepsRKALDSyDKAYYVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTTYVVK 187
Cdd:cd06323 81 IPVITVD----RSVTGG-KVVSHIASDNVAGGEMAAEYIAKK--------LGGKGKV--VELQGIPGTSAARERGKGFHN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 188 ELnDKGLKTQQLALDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALA 266
Cdd:cd06323 146 AI-AKYPKINVVASQTADFDRTKGLNVMENLLqAHPD---IDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVK 221
|
250
....*....|.
gi 504645589 267 LVKSGAMAGTV 277
Cdd:cd06323 222 AVKDGKLAATV 232
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
49-317 |
2.74e-29 |
|
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: 113.88 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 49 KDAKAAPDVQLlmndSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFnkepSRKALDSYDKA 128
Cdd:cd19994 26 EEAGYTVDLQY----ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAY----DRLIMNTDAVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 129 YYVGTDSKESGIIQGDLIAKHWAANpnwdlNKDGQIQFVLLKGEPGhpDAEARTTY-----VVKELNDKG---LKTQQLA 200
Cdd:cd19994 98 YYVTFDNEKVGELQGQYLVDKLGLK-----DGKGPFNIELFAGSPD--DNNAQLFFkgameVLQPYIDDGtlvVRSGQTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 201 LD---TAMWDTAQAKDKMDAWLSGPNA--NKIEVVIANNDAMAMGAVEALKAHNKSSIP---VFGVDALPEALALVKSGA 272
Cdd:cd19994 171 FEqvaTPDWDTETAQARMETLLSAYYTggKKLDAVLSPNDGIARGVIEALKAAGYDTGPwpvVTGQDAEDASVKSILDGE 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 504645589 273 MAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKIVRVP 317
Cdd:cd19994 251 QSMTVFKDTRLLAKATVELVDALLEGEEVEVNDTKTYDNGVKVVP 295
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
28-298 |
7.29e-29 |
|
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: 112.50 E-value: 7.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQN 107
Cdd:cd06318 2 IGFSQRTLASPYYAALVAAAKAEAKKL-GVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNkepsRKALDSYDKAYYVGTDSKESGIIQGdliakHWAAnpnwDLNKDGQIQFVLLKGEPGHPDAEARTTYVVK 187
Cdd:cd06318 81 IPVITVD----SALDPSANVATQVGRDNKQNGVLVG-----KEAA----KALGGDPGKIIELSGDKGNEVSRDRRDGFLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 188 ELNDKGLKTQQ------LALDTAMWDTAQAKDKMDAWLSgpnANK-IEVVIANNDAMAMGAVEALKAHNKSSI-PVFGVD 259
Cdd:cd06318 148 GVNEYQLRKYGksnikvVAQPYGNWIRSGAVAAMEDLLQ---AHPdINVVYAENDDMALGAMKALKAAGMLDKvKVAGAD 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 504645589 260 ALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADG 298
Cdd:cd06318 225 GQKEALKLIKDGKYVATGLNDPDLLGKTAVDTAAKVVKG 263
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
39-330 |
3.21e-28 |
|
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: 110.77 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 39 FMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNkeps 118
Cdd:cd06309 13 WRVANTKSIKEAAKKR-GYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVD---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 119 rKALDSYDKAYY---VGTDSKESGIIQGDLIAKHwaanpnwdlNKDGQIQFVLLKGEPGHPDAEART----TYVVKELND 191
Cdd:cd06309 88 -RTIDGEDGSLYvtfIGSDFVEEGRRAAEWLVKN---------YKGGKGNVVELQGTAGSSVAIDRSkgfrEVIKKHPNI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 192 KGLKTQqlaldTAMWDTAQAKDKMDAWL-SGPnaNKIEVVIANNDAMAMGAVEALKAHNKS---SIPVFGVDALPEALAL 267
Cdd:cd06309 158 KIVASQ-----SGNFTREKGQKVMENLLqAGP--GDIDVIYAHNDDMALGAIQALKEAGLKpgkDVLVVGIDGQKDALEA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504645589 268 VKSGAMAGTVLNDAnNQAKATFDLAKNLADGKgaadgtnwKIDnKIVRVPYVGVDQSNLAEFI 330
Cdd:cd06309 231 IKAGELNATVECNP-LFGPTAFDTIAKLLAGE--------KVP-KLIIVEERLFDKDNAAEEL 283
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
27-310 |
1.36e-27 |
|
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: 108.63 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQ 106
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKL-GVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 107 NVPIVFFNkepsRKAlDSYDKAYYVGTDSKESGIIQGDLIAKhwaanpnwDLNKDGQIqfVLLKGEPGHPDAEARTTYVV 186
Cdd:cd19968 80 GIPVVTVD----RRA-EGAAPVPHVGADNVAGGREVAKFVVD--------KLPNGAKV--IELTGTPGSSPAIDRTKGFH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 187 KELnDKGLKTQQLALDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAH--NKSSIPVFGVDALPEA 264
Cdd:cd19968 145 EEL-AAGPKIKVVFEQTGNFERDEGLTVMENILTS-LPGPPDAIICANDDMALGAIEAMRAAglDLKKVKVIGFDAVPDA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 504645589 265 LALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKID 310
Cdd:cd19968 223 LQAIKDGELYATVEQPPGGQARTALRILVDYLKDKKAPKKVNLKPK 268
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-299 |
6.50e-26 |
|
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: 103.82 E-value: 6.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAAPDvQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQN 107
Cdd:cd19971 2 FGFSYMTMNNPFFIAINDGIKKAVEANGD-ELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNKEPS-RKALDSydkayYVGTDSKESGIIQGDLIAKhwaanpnwDLNKDGQIqfVLLKgepgHPDAEA---RTT 183
Cdd:cd19971 81 IPVINVDTPVKdTDLVDS-----TIASDNYNAGKLCGEDMVK--------KLPEGAKI--AVLD----HPTAEScvdRID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 184 ------------YVVKELNDKGlktqqlALDTAMwdtAQAKDKMDAwlsGPNankIEVVIANNDAMAMGAVEALKAHNK- 250
Cdd:cd19971 142 gfldaikknpkfEVVAQQDGKG------QLEVAM---PIMEDILQA---HPD---LDAVFALNDPSALGALAALKAAGKl 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 504645589 251 SSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGK 299
Cdd:cd19971 207 GDILVYGVDGSPDAKAAIKDGKMTATAAQSPIEIGKKAVETAYKILNGE 255
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
52-319 |
1.93e-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: 103.52 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 52 KAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNkepsrKALDSYDKAYYV 131
Cdd:cd19995 28 KLCPDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYD-----RLILGGPADYYV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 132 GTDSKESGIIQGDLIAKHWAAnpnwdlNKDGQIQFVLLKGEPGHPDA---EARTTYVVKELNDKGLKTQQLALDTAMWDT 208
Cdd:cd19995 103 SFDNVAVGEAQAQSLVDHLKA------IGKKGVNIVMINGSPTDNNAglfKKGAHEVLDPLGDSGELKLVCEYDTPDWDP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 209 AQAKDKMDAWLSgPNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKA 287
Cdd:cd19995 177 ANAQTAMEQALT-KLGNNIDGVLSANDGLAGGAIAALKAQGlAGKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAAA 255
|
250 260 270
....*....|....*....|....*....|...
gi 504645589 288 TFDLAKNLADGKG-AADGTNWKIDNKIVRVPYV 319
Cdd:cd19995 256 AAKVAVALLKGETpPSDLVTGTVTNGGDKVPAV 288
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
27-327 |
8.17e-25 |
|
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: 101.57 E-value: 8.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAAP-DVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARG 105
Cdd:cd06320 1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGvKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 106 QNVPIVFFNKEPSRKALDSY--DKAYYVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTT 183
Cdd:cd06320 81 KGIPVINLDDAVDADALKKAggKVTSFIGTDNVAAGALAAEYIAEK--------LPGGGKV--AIIEGLPGNAAAEARTK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 184 YVVKELNdKGLKTQQLALDTAMWDTAQAKDKMDAWLSG-PNANKIevvIANNDAMAMGAVEALKAHNKSS-IPVFGVDAL 261
Cdd:cd06320 151 GFKETFK-KAPGLKLVASQPADWDRTKALDAATAILQAhPDLKGI---YAANDTMALGAVEAVKAAGKTGkVLVVGTDGI 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504645589 262 PEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKgaadgtnwKIDNKIVrVPYVGVDQSNLA 327
Cdd:cd06320 227 PEAKKSIKAGELTATVAQYPYLEGAMAVEAALRLLQGQ--------KVPAVVA-TPQALITKDNVD 283
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
27-303 |
1.27e-23 |
|
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: 98.20 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQ 106
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEEL-GYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 107 NVPIVFfnkepSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANPnWdlnKDGQIqfVLLKGEPGHPDAEARTTYVV 186
Cdd:cd06319 80 KIPVVI-----ADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKENG-W---GGGSV--GIIAIPQSRVNGQARTAGFE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 187 KELNDKGLKTQQLALdTAMWDTAQAKDKM-DAWLSGPnanKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEA 264
Cdd:cd06319 149 DALEEAGVEEVALRQ-TPNSTVEETYSAAqDLLAANP---DIKGIFAQNDQMAQGALQAIEEAGRTGdILVVGFDGDPEA 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 504645589 265 LALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAD 303
Cdd:cd06319 225 LDLIKDGKLDGTVAQQPFGMGARAVELAIQALNGDNTVE 263
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
63-299 |
2.00e-23 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 97.55 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 63 DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKepsrkaLDSYDKAYYVGTDSKESGIIQ 142
Cdd:cd19993 36 DAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDR------LIENPIAFYISFDNVEVGRMQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 143 GDLIakhwaanpnwdLNKDGQIQFVLLKGEPGHPDAE---ARTTYVVKELNDKGLKTQQLALDTAMWDTAQAKDKMDAWL 219
Cdd:cd19993 110 ARGV-----------LKAKPEGNYVFIKGSPTDPNADflrAGQMEVLQPAIDSGKIKIVGEQYTDGWKPANAQKNMEQIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 220 SGpNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADG 298
Cdd:cd19993 179 TA-NNNKVDAVVASNDGTAGGAVAALAAQGlAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKG 257
|
.
gi 504645589 299 K 299
Cdd:cd19993 258 T 258
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
66-322 |
1.03e-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: 93.07 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 66 NDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNkepsRKALDSyDKAYYVGTDSKESGIIQGDL 145
Cdd:cd19991 39 GDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYD----RLILNA-DVDLYVSFDNEKVGELQAEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 146 IAKHwaanpnwdlnkDGQIQFVLLKGEPGHPDAE---ARTTYVVKELNDKGlkTQQLALDTAM--WDTAQAKDKMDAWLS 220
Cdd:cd19991 114 LVKA-----------KPKGNYVLLGGSPTDNNAKlfrEGQMKVLQPLIDSG--DIKVVGDQWVddWDPEEALKIMENALT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 221 GpNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGK 299
Cdd:cd19991 181 A-NNNKIDAVIASNDGTAGGAIQALAEQGlAGKVAVSGQDADLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGE 259
|
250 260
....*....|....*....|...
gi 504645589 300 GAAdgTNWKIDNKIVRVPYVGVD 322
Cdd:cd19991 260 KNE--ANRTINNGKKEVPSILLD 280
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
33-317 |
1.68e-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: 92.49 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 33 YKYDDNFMsvVRKAIEKDAKaapdvqLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVF 112
Cdd:cd01538 14 WQTDRDIM--VEQLEEKGAK------VLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 113 FNkepsRKALDSyDKAYYVGTDSKESGIIQGDLIAKhwaanpnwdlnKDGQIQFVLLKGEPGHPDA---EARTTYVVKEL 189
Cdd:cd01538 86 YD----RLILNA-DVDYYISFDNEKVGELQAQALLD-----------AKPEGNYVLIGGSPTDNNAklfRDGQMKVLQPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 190 NDKGLKTQQLALDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALV 268
Cdd:cd01538 150 IDSGKIKVVGDQWVDDWLPANAQQIMENALTA-NGNNVDAVVASNDGTAGGAIAALKAQGLSGgVPVSGQDADLAAIKRI 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 504645589 269 KSGAMAGTVLNDANNQAKATFDLAKNLADGKGAadGTNWKIDNKIVRVP 317
Cdd:cd01538 229 LAGTQTMTVYKDIRLLADAAAEVAVALMRGEKP--PINGTTNNGLKDVP 275
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
39-259 |
2.80e-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: 91.92 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 39 FMSVVRKAIEKDAKAAPDV--QLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKE 116
Cdd:cd19996 13 WRVQMIAEFEAEAAKLKKLikELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 117 PsrkalDSYDKAYYVGTDSKESGIIQGDLIAKhwaanpnwDLNKDGQIqfVLLKGEPGHPDAEARTTYVVKELND-KGLK 195
Cdd:cd19996 93 V-----GSDKYTAFVGVDDAAFGRVGAEWLVK--------QLGGKGNI--IALRGIAGVSVSEDRWAGAKEVFKEyPGIK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504645589 196 TqqLALDTAMWDTAQAKDKMDAWLS-GPnanKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVD 259
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 ... |
28-299 |
3.07e-21 |
|
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: 91.18 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQN 107
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAEL-GVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDLIAKHWaanpnwdLNKDGQIQFVllkgepGHPDA--------- 178
Cdd:cd06322 81 IPVFTVDVKADGAKVVT-----HVGTDNYAGGKLAGEYALKAL-------LGGGGKIAII------DYPEVesvvlrvng 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 179 --EARTTY----VVKELNDKGLKTQQLAldtAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHNKSS 252
Cdd:cd06322 143 fkEAIKKYpnieIVAEQPGDGRREEALA---ATEDMLQANPDLDG------------IFAIGDPAALGALTAIESAGKED 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 504645589 253 -IPVFGVDALPEAL-ALVKSGAMAGTVLNDANNQAKATFDLAKNLADGK 299
Cdd:cd06322 208 kIKVIGFDGNPEAIkAIAKGGKIKADIAQQPDKIGQETVEAIVKYLAGE 256
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-277 |
4.79e-20 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 88.61 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 1 MNKKVLTL-SAVMASMLFGAAAHAADTrIGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLL 79
Cdd:PRK10653 2 NMKKLATLvSAVALSATVSANAMAKDT-IALVVSTLNNPFFVSLKDGAQKEADKL-GYNLVVLDSQNNPAKELANVQDLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 80 AKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDLIAKHWAANPnwdln 159
Cdd:PRK10653 80 VRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVS-----HIASDNVAGGKMAGDFIAKKLGEGA----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 160 kdgqiQFVLLKGEPGHPDAEARTTYVVKELndKGLKTQQLALDTAMWDTAQAKDKMDAWLSgpnAN-KIEVVIANNDAMA 238
Cdd:PRK10653 150 -----KVIQLEGIAGTSAARERGEGFKQAV--AAHKFNVLASQPADFDRTKGLNVMQNLLT---AHpDVQAVFAQNDEMA 219
|
250 260 270
....*....|....*....|....*....|....*....
gi 504645589 239 MGAVEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTV 277
Cdd:PRK10653 220 LGALRALQTAGKSDVMVVGFDGTPDGIKAVNRGKLAATI 258
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
27-295 |
2.71e-17 |
|
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: 80.44 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQ 106
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKEL-GYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 107 NVPIVFFNKEpsrkaLDSYDKAYYVGTDSKESGiiqGDLIAKHWAAnpnwDLNKDGQiqFVLLKGEPGHPDAEART---T 183
Cdd:cd19967 80 GIPVFLIDRE-----INAEGVAVAQIVSDNYQG---AVLLAQYFVK----LMGEKGL--YVELLGKESDTNAQLRSqgfH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 184 YVVKELNDkglkTQQLALDTAMWDTAQAKDKMDAWL-SGPnanKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDAL 261
Cdd:cd19967 146 SVIDQYPE----LKMVAQQSADWDRTEAFEKMESILqANP---DIKGVICGNDEMALGAIAALKAAGRAGdVIIVGFDGS 218
|
250 260 270
....*....|....*....|....*....|....
gi 504645589 262 PEALALVKSGAMAGTVLNDANNQAKATFDLAKNL 295
Cdd:cd19967 219 NDVRDAIKEGKISATVLQPAKLIARLAVEQADQY 252
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
27-299 |
5.17e-17 |
|
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: 79.69 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAAP-DVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARG 105
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGvKIIFVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 106 QNVPIVFFNkepSRKALDSYDKayYVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTTYV 185
Cdd:cd06310 81 KGIPVIVID---SGIKGDAYLS--YIATDNYAAGRLAAQKLAEA--------LGGKGKV--AVLSLTAGNSTTDQREEGF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 186 VKELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSGpnANKIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEA 264
Cdd:cd06310 146 KEYLKKHPGGIKVLASQYAGSDYAKAANETEDLLGK--YPDIDGIFATNEITALGAAVAIKSRKLSgQIKIVGFDSQEEL 223
|
250 260 270
....*....|....*....|....*....|....*
gi 504645589 265 LALVKSGAMAGTVLNDANNQAKATFDLAKNLADGK 299
Cdd:cd06310 224 LDALKNGKIDALVVQNPYEIGYEGIKLALKLLKGE 258
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
39-277 |
4.02e-15 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380625 [Multi-domain] Cd Length: 275 Bit Score: 74.21 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 39 FMSVVRKAIEKDAKAAPDVQLLMNDSQNDQS--KQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKE 116
Cdd:cd19970 13 FFIEMEKGARKHAKEANGYELLVKGIKQETDieQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 117 PSRKALDSYDKAY-YVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTTYVVKELNDKGLK 195
Cdd:cd19970 93 LDADALKEGGINVpFVGPDNRQGAYLAGDYLAKK--------LGKGGKV--AIIEGIPGADNAQQRKAGFLKAFEEAGMK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 196 TqqLALDTAMWDTAQAKDKMDAWLSG-PNankIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGAM 273
Cdd:cd19970 163 I--VASQSANWEIDEANTVAANLLTAhPD---IRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKM 237
|
....
gi 504645589 274 AGTV 277
Cdd:cd19970 238 LATI 241
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
27-303 |
4.64e-15 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380544 [Multi-domain] Cd Length: 270 Bit Score: 73.86 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAA-PDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARG 105
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEInPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 106 QNVPIVffnkepsrkALDSYDKAY--YVGTDSKESGIIQGDLIAKhwaanpnwDLNKDGQIqfVLLKGEPGHPD------ 177
Cdd:cd06321 81 AGIIVV---------AVDVAAEGAdaTVTTDNVQAGYLACEYLVE--------QLGGKGKV--AIIDGPPVSAVidrvng 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 178 -----AEARTTYVVKELNDKGLKTQQLaldTAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHNKSS 252
Cdd:cd06321 142 ckealAEYPGIKLVDDQNGKGSRAGGL---SVMTRMLTAHPDVDG------------VFAINDPGAIGALLAAQQAGRDD 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 504645589 253 IPVFGVDALPEALALVK--SGAMAGTVLNDANNQAKATFDLAKNLADGKGAAD 303
Cdd:cd06321 207 IVITSVDGSPEAVAALKreGSPFIATAAQDPYDMARKAVELALKILNGQEPAP 259
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
35-277 |
1.46e-14 |
|
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: 72.61 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 35 YDDNFMSVVRKAIEKDAKAaPDVQLLMNDSQN-DQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFF 113
Cdd:cd06314 9 LNNPFWDLAEAGAEKAAKE-LGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 114 NKEpsrkALDSYDKAyYVGTDSKESGIIQGDLIAKhwaanpnwDLNKDGQIqfVLLKGEPGHPDAEARTTYVVKELNDKG 193
Cdd:cd06314 88 DSD----APDSKRLA-YIGTDNYEAGREAGELMKK--------ALPGGGKV--AIITGGLGADNLNERIQGFKDALKGSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 194 lKTQQLALDTAMWDTAQAKDKMDAWLSG-PNANKIEVVIANNdamAMGAVEALKAHNK-SSIPVFGVDALPEALALVKSG 271
Cdd:cd06314 153 -GIEIVDPLSDNDDIAKAVQNVEDILKAnPDLDAIFGVGAYN---GPAIAAALKDAGKvGKVKIVGFDTLPETLQGIKDG 228
|
....*.
gi 504645589 272 AMAGTV 277
Cdd:cd06314 229 VIAATV 234
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
28-264 |
1.49e-14 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 73.31 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALaInLVDPAAAGTVIEKARGQN 107
Cdd:COG1609 64 IGVVVPDLSNPFFAELLRGIEEAARER-GYQLLLANSDEDPEREREALRLLLSRRVDGL-I-LAGSRLDDARLERLAEAG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNKEPSRKALDSydkayyVGTDSKESGiiqgDLIAKHwaanpnwdLNKDGQIQFVLLKGEPGHPDAEARTTYVVK 187
Cdd:COG1609 141 IPVVLIDRPLPDPGVPS------VGVDNRAGA----RLATEH--------LIELGHRRIAFIGGPADSSSARERLAGYRE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 188 ELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNKsSIP----VFGVDALPE 263
Cdd:COG1609 203 ALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGP--RPTAIFCANDLMALGALRALREAGL-RVPedvsVVGFDDIPL 279
|
.
gi 504645589 264 A 264
Cdd:COG1609 280 A 280
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
36-277 |
3.57e-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: 71.49 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 36 DDNFMSVVRKAIeKDAKAAPDVQL-LMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFN 114
Cdd:cd06312 11 SDPFWSVVKKGA-KDAAKDLGVTVqYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAIN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 115 KEPSRKALDSydkAY--YVGTDSKESGIIQGDLIAKHWAANpnwdlnkdgqiqFVLLKGEPGHPDAEARTTYVVKELNDK 192
Cdd:cd06312 90 SGDDRSKERL---GAltYVGQDEYLAGQAAGERALEAGPKN------------ALCVNHEPGNPGLEARCKGFADAFKGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 193 GLKTQQLALDTamwDTAQAKDKMDAWLsgpNANK-IEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKS 270
Cdd:cd06312 155 GILVELLDVGG---DPTEAQEAIKAYL---QADPdTDAVLTLGPVGADPALKAVKEAGLKGkVKIGTFDLSPETLEAIKD 228
|
....*..
gi 504645589 271 GAMAGTV 277
Cdd:cd06312 229 GKILFAI 235
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
28-299 |
4.17e-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: 71.32 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQN 107
Cdd:cd19972 2 IGLAVANLQADFFNQIKQSVEAEAKKK-GYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDLIAKHwaanpnwdlnKDGQIQFVLLKGEPGHPDAEARTTYVVK 187
Cdd:cd19972 81 IPVIAVDRNPEDAPGDT-----FIATDSVAAAKELGEWVIKQ----------TGGKGEIAILHGQLGTTPEVDRTKGFQE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 188 EL-NDKGLKTQqlALDTAMWDTAQA-KDKMDAWLSGPNankIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEA 264
Cdd:cd19972 146 ALaEAPGIKVV--AEQTADWDQDEGfKVAQDMLQANPN---ITVFFGQSDAMALGAAQAVKVAGLDHkIWVVGFDGDVAG 220
|
250 260 270
....*....|....*....|....*....|....*
gi 504645589 265 LALVKSGAMAGTVLNDANNQAKATFDLAKNLADGK 299
Cdd:cd19972 221 LKAVKDGVLDATMTQQTQKMGRLAVDSAIDLLNGK 255
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
64-257 |
3.61e-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: 68.87 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 64 SQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPsrkaldSYDKAYYVGTDSKESGIIQG 143
Cdd:cd19999 42 ADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPV------SSPDAINVVIDQYKWAAIQA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 144 DLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTTyVVKELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSgpN 223
Cdd:cd19999 116 QWLAEQ--------LGGKGNI--VAINGVAGNPANEARVK-AADDVFAKYPGIKVLASVPGGWDQATAQQVMATLLA--T 182
|
170 180 190
....*....|....*....|....*....|....
gi 504645589 224 ANKIEVVIaNNDAMAMGAVEALKAHNKSSIPVFG 257
Cdd:cd19999 183 YPDIDGVL-TQDGMAEGVLRAFQAAGKDPPVMTG 215
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
28-264 |
8.95e-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: 67.16 E-value: 8.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALaInLVDPAAAGTVIEKARGQN 107
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAARER-GYSLLLCNTDEDPEREREYLRLLLSRRVDGI-I-LAPSSLDDELLEELLAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNKEPSRKALDSydkayyVGTDSKESGIiqgdLIAKHwaanpnwdLNKDGQIQFVLLKGEPGHPDAEARTTYVVK 187
Cdd:cd06267 79 IPVVLIDRRLDGLGVDS------VVVDNYAGAY----LATEH--------LIELGHRRIAFIGGPLDLSTSRERLEGYRD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 188 ELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSGPnaNKIEVVIANNDAMAMGAVEALKAHNKsSIP----VFGVDALPE 263
Cdd:cd06267 141 ALAEAGLPVDPELVVEGDFSEESGYEAARELLALP--PRPTAIFAANDLMAIGALRALRELGL-RVPedisVVGFDDIPL 217
|
.
gi 504645589 264 A 264
Cdd:cd06267 218 A 218
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
35-277 |
2.10e-12 |
|
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: 66.14 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 35 YDDNFMSVVRKAIeKDAKAAPDVQLLMNDSQN-DQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFF 113
Cdd:cd19965 9 TTNPFFQPVKKGM-DDACELLGAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 114 NKEpsrkALDSYDKAY-YVGTDSKESGIIQGDLIAKhwaanpnwdLNKDGQIQFVLLKGEPGHPDAEARTTYVVKELNDK 192
Cdd:cd19965 88 NVD----APGGENARLaFVGQDLYPAGYVLGKRIAE---------KFKPGGGHVLLGISTPGQSALEQRLDGIKQALKEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 193 GLKTQQLALDTAMwDTAQAKDKMDAWLSG-PNANkieVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKS 270
Cdd:cd19965 155 GRGITYDVIDTGT-DLAEALSRIEAYYTAhPDIK---AIFATGAFDTAGAGQAIKDLGlKGKVLVGGFDLVPEVLQGIKA 230
|
....*..
gi 504645589 271 GAMAGTV 277
Cdd:cd19965 231 GYIDFTI 237
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
36-273 |
2.97e-12 |
|
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: 65.81 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 36 DDNFMSVVRKAIeKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGT-VIEKARGQNVPIVFFN 114
Cdd:cd19966 11 GDPFWTVVYNGA-KDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTpLIEAAKKAGIIVTSFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 115 KePSRKALDSYDKAYYVGTDSKESGIIQGDLIAKhwaanpNWDLnKDGqiQFVLLKGEPGH-PDAEARTTYVVKELNDKG 193
Cdd:cd19966 90 T-DLPKLEYGDCGLGYVGADLYAAGYTLAKELVK------RGGL-KTG--DRVFVPGLLPGqPYRVLRTKGVIDALKEAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 194 LKTQQLALDTAMWDTAQAKDKMDAWLSgpnANK-IEVVIANNDAMAMGAVEALKAHNK--SSIPVFGVDALPEALALVKS 270
Cdd:cd19966 160 IKVDYLEISLEPNKPAEGIPVMTGYLA---ANPdVKAIVGDGGGLTANVAKYLKAAGKkpGEIPVAGFDLSPATVQAIKS 236
|
...
gi 504645589 271 GAM 273
Cdd:cd19966 237 GYV 239
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
26-299 |
3.69e-12 |
|
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: 65.86 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 26 TRIGVTIYKyDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARG 105
Cdd:cd06317 1 TIALVQINQ-QAQFFNQINQGAQAAAKDL-GVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 106 QNVPIVFFNkepsrKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANpnwdLNKDGQIQFVLLKGEpghPDAEARTTYV 185
Cdd:cd06317 79 AGIPVIAYD-----AVIPSDFQAAQVGVDNLEGGKEIGKYAADYIKAE----LGGQAKIGVVGALSS---LIQNQRQKGF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 186 VKELND----KGLKTQ--QLALDTAMwdtAQAKDKMDAwlsgpNANkIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGV 258
Cdd:cd06317 147 EEALKAnpgvEIVATVdgQNVQEKAL---SAAENLLTA-----NPD-LDAIYATGEPALLGAVAAVRSQGRQgKIKVFGW 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 504645589 259 DALPE-ALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGK 299
Cdd:cd06317 218 DLTKQaIFLGIDEGVLQAVVQQDPEKMGYEAVKAAVKAIKGE 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
63-269 |
1.13e-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: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 63 DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNkepsrKALDSYDkAYYVGTDSKESGIIQ 142
Cdd:cd06300 41 NSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFD-----GAVTSPD-AYNVSNDQVEWGRLG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 143 GDLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTTYVVKELnDKGLKTQQLALDTAMWDTAQAKDKMDAWL-SG 221
Cdd:cd06300 115 AKWLFEA--------LGGKGNV--LVVRGIAGAPASADRHAGVKEAL-AEYPGIKVVGEVFGGWDEATAQTAMLDFLaTH 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504645589 222 PNANKievvIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVK 269
Cdd:cd06300 184 PQVDG----VWTQGGEDTGVLQAFQQAGRPPVPIVGGDENGFAKQWWK 227
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
1-280 |
1.94e-11 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 63.74 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 1 MNK-KVLTLSAVMASMLFGAAAHAADtrIGVTIYKYDDNFMSVVRKAIEKDAKA-APDVQLLMNDSQNDQSKQNDQIDVL 78
Cdd:PRK09701 1 MNKyLKYFSGTLVGLMLSTSAFAAAE--YAVVLKTLSNPFWVDMKKGIEDEAKTlGVSVDIFASPSEGDFQSQLQLFEDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 79 LAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPSRKALDSYDKAY--YVGTDSKESGIIQGDLIAKHWAAnpnw 156
Cdd:PRK09701 79 SNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKKAGGNVeaFVTTDNVAVGAKGASFIIDKLGA---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 157 dlnKDGQIqfVLLKGEPGHPDAEARTTYVvKELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLS-GPNankIEVVIANND 235
Cdd:PRK09701 155 ---EGGEV--AIIEGKAGNASGEARRNGA-TEAFKKASQIKLVASQPADWDRIKALDVATNVLQrNPN---IKAIYCAND 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 504645589 236 AMAMGAVEALK-AHNKSSIPVFGVDALPEALALVKSGAMAGTVLND 280
Cdd:PRK09701 226 TMAMGVAQAVAnAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQN 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
56-277 |
2.07e-11 |
|
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: 63.78 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 56 DVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVD-PAAAGTVIEKARGQNVPIVFFNKEPSRKALDSYDK-----AY 129
Cdd:cd06324 30 GIELEVLYANRNRFKMLELAEELLARPPKPDYLILVNeKGVAPELLELAEQAKIPVFLINNDLTDEERALLGKprekfKY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 130 YVGT---DSKESG--IIQgDLIAKHWAanpnwdLNKDGQIQFVLLKGEPGHPDAEARTtyvvkelndKGLKtQQLALDT- 203
Cdd:cd06324 110 WLGSivpDNEQAGylLAK-ALIKAARK------KSDDGKIRVLAISGDKSTPASILRE---------QGLR-DALAEHPd 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 204 --------AMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNK---SSIPVFGVDALPEALALVKSGA 272
Cdd:cd06324 173 vtllqivyANWSEDEAYQKTEKLLQ--RYPDIDIVWAANDAMALGAIDALEEAGLkpgKDVLVGGIDWSPEALQAVKDGE 250
|
....*
gi 504645589 273 MAGTV 277
Cdd:cd06324 251 LTASV 255
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
27-280 |
1.08e-10 |
|
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: 61.16 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKAaPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQ 106
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEK-LGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 107 NVPIVFFNKEPSRKAL---DSYDKAyyVGTDSkesgiiqGDLIAKhwaanpnwDLNKDGQIQFVLLKGEPghPDAEARTT 183
Cdd:cd06305 80 GIPVVTFDTDSQVPGVnniTQDDYA--LGTLS-------LGQLVK--------DLNGEGNIAVFNVFGVP--PLDKRYDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 184 YVVKELNDKGLKTQQLALDTAMWDTAQ-AKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALP 262
Cdd:cd06305 141 YKAVLKANPGIKKIVAELGDVTPNTAAdAQTQVEALLKKYPEGGIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISN 220
|
250 260
....*....|....*....|
gi 504645589 263 EALALVK--SGAMAGTVLND 280
Cdd:cd06305 221 QDLELMAdeGSPWVATAAQD 240
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
63-277 |
1.16e-09 |
|
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 58.12 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 63 DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEpsrkALDSyDKAYYVGTDSKESGIIQ 142
Cdd:cd19969 37 PATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSD----APES-KRISYVGTDNYEAGYAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 143 GDLIAKHwaanpnwdLNKDGQIQFVLLKGEPGHPD---------AEARTTYVVKELNDKG--LKTQQLAldTAMwdtAQA 211
Cdd:cd19969 112 AEKLAEL--------LGGKGKVAVLTGPGQPNHEErvegfkeafAEYPGIEVVAVGDDNDdpEKAAQNT--SAL---LQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504645589 212 KDKMDAWLsGPNANKievvianndamAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGAMAGTV 277
Cdd:cd19969 179 HPDLVGIF-GVDASG-----------GVGAAQAVREAGKTGkVKIVAFDDDPETLDLIKDGVIDASI 233
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
45-277 |
1.25e-09 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 58.02 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 45 KAIEKDAKAAPD---VQLLMN--DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNkepsr 119
Cdd:cd20005 15 KAVKKGAEQAAKelgVKITFEgpDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFD----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 120 KALDSYDKAYYVGTDSKESGIIQGDLIAKhwaanpnwdlNKDGQIQFVLLKGEPGHPDAEARTTYVVKELNDKGLKTQQL 199
Cdd:cd20005 90 SGVPSDLPLATVATDNYAAGALAADHLAE----------LIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDIKVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 200 ALDTAMWDTAQAKDKMDAWLSG-PNankIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDALPEALALVKSGAMAGTV 277
Cdd:cd20005 160 NVQYGVGDHAKAADIAKAILQAnPD---LKGIYATNEGAAIGVANALKEMGKlGKIKVVGFDSGEAQIDAIKNGVIAGSV 236
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-255 |
1.53e-08 |
|
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: 54.68 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQsKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQN 107
Cdd:cd06311 2 IGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNAN-EQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNKEpsrkaLDSYDKAYYVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTT---- 183
Cdd:cd06311 81 IPVVNFDRG-----LNVLIYDLYVAGDNPGMGVVSAEYIGKK--------LGGKGNV--VVLEVPSSGSVNEERVAgfke 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504645589 184 YVVKELNDKGLKTQQlaldtAMWDTAQA-KDKMDAWLSGPnanKIEVVIANNDAMAMGAVEALKAHNKSSIPV 255
Cdd:cd06311 146 VIKGNPGIKILAMQA-----GDWTREDGlKVAQDILTKNK---KIDAVWAADDDMAIGVLQAIKEAGRTDIKV 210
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-264 |
2.59e-08 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 54.15 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAInlVDPAAAGTVIEKARGQN 107
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARER-GYTVLLADTGDDPERELAALDSLLSRRVDGLII--TPARDDAPDLQELAARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNKEPSRKALDSydkayyVGTDSkESGiiqGDLIAKHWAANpnwdlnkdGQIQFVLLKGEPGHPDAEARTTYVVK 187
Cdd:cd06285 79 VPVVLVDRRIGDTALPS------VTVDN-ELG---GRLATRHLLEL--------GHRRIAVVAGPLNASTGRDRLRGYRR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 188 ELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSGPN---AnkievVIANNDAMAMGAVEALKAHNKsSIP----VFGVDA 260
Cdd:cd06285 141 ALAEAGLPVPDERIVPGGFTIEAGREAAYRLLSRPErptA-----VFAANDLMAIGVLRAARDLGL-RVPedlsVVGFDD 214
|
....
gi 504645589 261 LPEA 264
Cdd:cd06285 215 IPLA 218
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
66-309 |
3.04e-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: 53.74 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 66 NDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDL 145
Cdd:cd06306 41 TNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNGIDSPKVAA-----RVLVDFYDMGYLAGEY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 146 IAKHwaanpnwdlNKDGQIQFVLLKGEPGHPDAEARTTYVVKELNDKGLKTqqlaLDTAMWDT--AQAKDKMDAWL-SGP 222
Cdd:cd06306 116 LVEH---------HPGKPVKVAWFPGPAGAGWAEDREKGFKEALAGSNVEI----VATKYGDTgkAVQLNLVEDALqAHP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 223 NANkievVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGA 301
Cdd:cd06306 183 DID----YIVGNAVAAEAAVGALREAGLTGkVKVVSTYLTPGVYRGIKRGKILAAPSDQPVLQGRIAVDQAVRALEGKPV 258
|
....*...
gi 504645589 302 ADGTNWKI 309
Cdd:cd06306 259 PKHVGPPI 266
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
59-264 |
4.37e-08 |
|
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: 53.34 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 59 LLMNDSQNDQSKQNDQIDVLLAKGVKALAINlvdpAAAGT---VIEKARGQNVPIVFFNKEPSRKALDsydkayYVGTDS 135
Cdd:cd06289 32 VFLANTGEDPERQRRFLRRMLEQGVDGLILS----PAAGTtaeLLRRLKAWGIPVVLALRDVPGSDLD------YVGIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 136 KESGiiqgDLIAKHwaanpnwdLNKDGQIQFVLLKGEPGHPDAEARttyvvKELNDKGLKTQQLALDTAMW-----DTAQ 210
Cdd:cd06289 102 RLGA----QLATEH--------LIALGHRRIAFLGGLSDSSTRRER-----LAGFRAALAEAGLPLDESLIvpgpaTREA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504645589 211 AKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKSS---IPVFGVDALPEA 264
Cdd:cd06289 165 GAEAARELLD--AAPPPTAVVCFNDLVALGAMLALRRRGLEPgrdIAVVGFDDVPEA 219
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
1-326 |
5.72e-08 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 53.59 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 1 MNKKVLTLSAVMASMLFGAAAHAADTRIGVTI--------YKYDDNFmsvVRKAIEKDAKaapdvqLLMNDSQNDQSKQN 72
Cdd:PRK10355 1 MKIKNILLTLCASLLLTSVAAHAKEVKIGMAIddlrlerwQKDRDIF---VKKAESLGAK------VFVQSANGNEETQM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 73 DQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPSRKALDsydkaYYVGTDSKESGIIQGDLIakhwaa 152
Cdd:PRK10355 72 SQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADID-----FYISFDNEKVGELQAKAL------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 153 npnwdLNKDGQIQFVLLKGEPGHPDAE---ARTTYVVKELNDKGlKTQQLALDTAM-WDTAQAKDKMDAWLSGpNANKIE 228
Cdd:PRK10355 141 -----VDKVPQGNYFLMGGSPVDNNAKlfrAGQMKVLKPYIDSG-KIKVVGDQWVDgWLPENALKIMENALTA-NNNKID 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 229 VVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLadGKGAADGTNW 307
Cdd:PRK10355 214 AVVASNDATAGGAIQALSAQGLSgKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVEL--GNGEEPKANT 291
|
330 340
....*....|....*....|....
gi 504645589 308 KIDNKIVRVPY-----VGVDQSNL 326
Cdd:PRK10355 292 TLNNGLKDVPSrlltpIDVNKNNI 315
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
27-280 |
9.26e-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: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 27 RIGVTIYKYDDNFMSVVRKAIEKDAKA-APDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARg 105
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKElGVEVTFLGPATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 106 QNVPIVFFNkepSRKALDSYDKAYyvGTDSKESGIIQGDLIAKHWAANPNwdlnKDGQIqfVLLKGEPGHPDAEARTTYV 185
Cdd:cd20008 80 AGIPVVLVD---SGANTDDYDAFL--ATDNVAAGALAADELAELLKASGG----GKGKV--AIISFQAGSQTLVDREEGF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 186 VKELNDKGLKTQQLALDTAMWDTAQAKDKM-DAWLSGPNANKIevvIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPE 263
Cdd:cd20008 149 RDYIKEKYPDIEIVDVQYSDGDIAKALNQTtDLLTANPDLVGI---FGANNPSAVGVAQALAEAGKAgKIVLVGFDSSPD 225
|
250
....*....|....*..
gi 504645589 264 ALALVKSGAMAGTVLND 280
Cdd:cd20008 226 EVALLKSGVIKALVVQD 242
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
65-281 |
9.88e-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: 52.24 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 65 QNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNkepsrKALDSYDKAYYVGTDSKESGIIQGD 144
Cdd:cd20004 40 EDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIID-----SDLGGDAVISFVATDNYAAGRLAAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 145 LIAKhwaanpnwDLNKDGQIqfVLLKGEPGHPDAEART---TYVVKELNDkGLK--TQQLAlDTAMWDTAQAKDKMDAWL 219
Cdd:cd20004 115 RMAK--------LLNGKGKV--ALLRLAKGSASTTDRErgfLEALKKLAP-GLKvvDDQYA-GGTVGEARSSAENLLNQY 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504645589 220 SGPNAnkievVIANNDAMAMGAVEALKAHNKSSIPVF-GVDALPEALALVKSGAMAGTVLNDA 281
Cdd:cd20004 183 PDVDG-----IFTPNESTTIGALRALRRLGLAGKVKFiGFDASDLLLDALRAGEISALVVQDP 240
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
59-264 |
2.01e-07 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 51.38 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 59 LLMNDSQNDQskQNDQIDVLLAKGVKALAINLVDPAAAgtVIEKARGQNVPIVFFNKEPSRKALDSydkayyVGTDSKES 138
Cdd:cd06278 33 LLFNVDDEDD--VDDALRQLLQYRVDGVIVTSATLSSE--LAEECARRGIPVVLFNRVVEDPGVDS------VSCDNRAG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 139 GiiqgDLIAKHWAANpnwdlnkdGQIQFVLLKGEPGHPDAEARTTYVVKELNDKGLKTQqlALDTAMWDTAQAKDKMDAW 218
Cdd:cd06278 103 G----RLAADLLLAA--------GHRRIAFLGGPEGTSTSRERERGFRAALAELGLPPP--AVEAGDYSYEGGYEAARRL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504645589 219 LSGPNAnkIEVVIANNDAMAMGAVEALKAHNKSSIP----VFGVDALPEA 264
Cdd:cd06278 169 LAAPDR--PDAIFCANDLMALGALDAARQEGGLVVPedisVVGFDDIPMA 216
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
49-307 |
2.75e-07 |
|
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: 51.09 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 49 KDAKAAPDVQLLMN-DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPSRKALDsydk 127
Cdd:cd06302 22 KKAAKELGVEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSDAPPSARD---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 128 aYYV-GTDSKESGIIQGDLIAKhwaanpnwdlNKDGQIQFVLLKGEPGHPD----AEARTTYVVKELNDKGLKTQQLALD 202
Cdd:cd06302 98 -YFVnQADDEGLGEALVDSLAK----------EIGGKGKVAILSGSLTATNlnawIKAMKEYLKSKYPDIELVDTYYTDD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 203 TAMWDTAQAKDKMDAWlsgPNankIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVdALP-EALALVKSGAMAGTVLND 280
Cdd:cd06302 167 DQQKAYTQAQNLIQAY---PD---LKGIIGVSTTAPPAAAQAVEEAGKTgKVAVTGI-GLPnTARPYLKDGSVKEGVLWD 239
|
250 260
....*....|....*....|....*..
gi 504645589 281 ANNQAKATFDLAKNLADGKGAADGTNW 307
Cdd:cd06302 240 PAKLGYLTVYAAYQLLKGKGFTEDSDD 266
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
39-248 |
1.73e-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: 48.79 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 39 FMSVVRkAIEkDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALainLVDPAAAGTVIEK--ARGQNVPIVFFNKE 116
Cdd:cd06275 14 FAEVVR-GVE-DACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGL---LLMCSEMTDDDAEllAALRSIPVVVLDRE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 117 PSRKALDSydkayyVGTDSkESGiiqGDLIAKHwaanpnwdLNKDGQIQFVLLKGEPGHPDAEARTTYVVKELNDKGLK- 195
Cdd:cd06275 89 IAGDNADA------VLDDS-FQG---GYLATRH--------LIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEv 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504645589 196 TQQLALDTAMwDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAH 248
Cdd:cd06275 151 PPSWIVEGDF-EPEGGYEAMQRLLSQPP--RPTAVFACNDMMALGALRAAQEQ 200
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
28-247 |
1.98e-06 |
|
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: 48.41 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALainLVDPAAAGT-VIEKARGQ 106
Cdd:cd06280 2 IGLIVPDITNPFFTTIARGIEDAAEKH-GYQVILANTDEDPEKEKRYLDSLLSKQVDGI---ILAPSAGPSrELKRLLKH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 107 NVPIVFFNKEPSRKALDSydkayyVGTDSKESGIIqgdlIAKHwaanpnwdLNKDGQIQFVLLKGEPGHPDAEARTTYVV 186
Cdd:cd06280 78 GIPIVLIDREVEGLELDL------VAGDNREGAYK----AVKH--------LIELGHRRIGLITGPLEISTTRERLAGYR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504645589 187 KELNDKGLKTQQ---LALDTAMWDTAQAkdkMDAWLSGPNAnkIEVVIANNDAMAMGAVEALKA 247
Cdd:cd06280 140 EALAEAGIPVDEsliFEGDSTIEGGYEA---VKALLDLPPR--PTAIFATNNLMAVGALRALRE 198
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
32-264 |
2.46e-06 |
|
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: 48.28 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 32 IYKYDDN--FMSVVrKAIEKDAKA-APDVQLLMNDSQNDQSKQndQIDVLLAKGVKALAINLVDPAAAgTVIEKARGQNV 108
Cdd:pfam00532 7 LVPQLDEpfFQDLV-KGITKAAKDhGFDVFLLAVGDGEDTLTN--AIDLLLASGADGIIITTPAPSGD-DITAKAEGYGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 109 PIVFFNkepsrkalDSYDKAYYVGTDSKEsgiiqgdliAKHWAANPNWDLNKDGQIQFVLLKGEP-GHPDAEARTTYVVK 187
Cdd:pfam00532 83 PVIAAD--------DAFDNPDGVPCVMPD---------DTQAGYESTQYLIAEGHKRPIAVMAGPaSALTARERVQGFMA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 188 ELNDKGLKTQQLALDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNKSSIP---------VFG 257
Cdd:pfam00532 146 ALAAAGREVKIYHVATGDNDIPDAALAANAMLvSHPT---IDAIVAMNDEAAMGAVRALLKQGRVKIPdivgiginsVVG 222
|
....*..
gi 504645589 258 VDALPEA 264
Cdd:pfam00532 223 FDGLSKA 229
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
64-257 |
4.63e-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: 47.67 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 64 SQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPsrkaldSYDKAYYVGTDSKESGIIQG 143
Cdd:cd19998 41 SGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVV------DEPCAYNVNTDQAKAGEQTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 144 DLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTTyVVKELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLsgPN 223
Cdd:cd19998 115 QWLVDK--------LGGKGNI--LMVRGVPGTSVDRDRYE-GAKEVFKKYPDIKVVAEYYGNWDDGTAQKAVADAL--AA 181
|
170 180 190
....*....|....*....|....*....|....
gi 504645589 224 ANKIEVVIAnNDAMAmGAVEALKAHNKSSIPVFG 257
Cdd:cd19998 182 HPDVDGVWT-QGGET-GVIKALQAAGHPLVPVGG 213
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
59-254 |
1.10e-05 |
|
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: 45.97 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 59 LLMNdSQNDQSKQNDQIDVLLAKGVKALAInlvdpAAAGTVIEKARGQNVPIVFFNKEPSrkaldsyDKAYYVGTDSKES 138
Cdd:cd06291 33 ILCN-SNEDEEKEKEYLEMLKRNKVDGIIL-----GSHSLDIEEYKKLNIPIVSIDRYLS-------EGIPSVSSDNYQG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 139 GIiqgdLIAKHwaanpnwdLNKDGQIQFVLLKGEPGHPDAEARTTYVVKELNDKGLKTQQLALDTAMWDTAQAKDKMDAW 218
Cdd:cd06291 100 GR----LAAEH--------LIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFSEEDAYELAKEL 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 504645589 219 LSgpNANKIEVVIANNDAMAMGAVEALKAHNKsSIP 254
Cdd:cd06291 168 LE--KYPDIDGIFASNDLLAIGVLKALQKLGI-RVP 200
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-268 |
2.39e-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: 380513 [Multi-domain] Cd Length: 267 Bit Score: 45.30 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALainLVDPAAAGTVIEKARGQN 107
Cdd:cd06290 2 IGVLVPDIDSPFYSEILNGIEEVLAES-GYTLIVSTSHWNADRELEILRLLLARKVDGI---IVVGGFGDEELLKLLAEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 108 VPIVFFNKEPSRKALDSydkayyVGTDSKESGIIqgdlIAKHwaanpnwdLNKDGQIQFVLLKGEPGHPDAEARTTYVVK 187
Cdd:cd06290 78 IPVVLVDRELEGLNLPV------VNVDNEQGGYN----ATNH--------LIDLGHRRIVHISGPEDHPDAQERYAGYRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 188 ELNDKGLK-TQQLALD---------TAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHnKSSIP--- 254
Cdd:cd06290 140 ALEDAGLEvDPRLIVEgdfteesgyEAMKKLLKRGGPFTA------------IFAANDLMALGAMKALREA-GIRVPddv 206
|
250
....*....|....*
gi 504645589 255 -VFGVDALPEALALV 268
Cdd:cd06290 207 sVIGFDDLPFSKYTT 221
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
45-278 |
5.80e-05 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 44.13 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 45 KAIEKDAKAAP-----DVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEpsr 119
Cdd:cd20006 17 QTVKSGAEAAAkeygvDLEFLGPESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSP--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 120 kaLDSYDKAYYVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQIQFV---------------LLKGEPGHPDAEARTTY 184
Cdd:cd20006 94 --VNSKKADSFVATDNYEAGKKAGEKLASL--------LGEKGKVAIVsfvkgsstaiereegFKQALAEYPNIKIVETE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 185 VVKElndkglktqqlaldtamwDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKA-HNKSSIPVFGVDALPE 263
Cdd:cd20006 164 YCDS------------------DEEKAYEITKELLS--KYPDINGIVALNEQSTLGAARALKElGLGGKVKVVGFDSSVE 223
|
250
....*....|....*
gi 504645589 264 ALALVKSGAMAGTVL 278
Cdd:cd20006 224 EIQLLEEGIIDALVV 238
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
164-264 |
1.26e-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: 41.94 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 164 IQFVLLKGEPGHPDAEARTTYVVKELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSG-PNAnkievVIANNDAMAMGAV 242
Cdd:pfam13377 10 IALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGAlPTA-----VFVANDEVALGVL 84
|
90 100
....*....|....*....|....*.
gi 504645589 243 EALKAHNKsSIP----VFGVDALPEA 264
Cdd:pfam13377 85 QALREAGL-RVPedlsVIGFDDSPLA 109
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
174-264 |
1.63e-04 |
|
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: 42.51 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 174 GHPDAEARTTYVVKELNDKGLKTQQLALDTAmWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKsSI 253
Cdd:cd01544 129 GEEIEDPRLRAFREYMKEKGLYNEEYIYIGE-FSVESGYEAMKELLK--EGDLPTAFFVASDPMAIGALRALQEAGI-KV 204
|
90
....*....|....*
gi 504645589 254 P----VFGVDALPEA 264
Cdd:cd01544 205 PedisIISFNDIEVA 219
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
32-276 |
2.29e-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: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 32 IYKYDDN-FMSVVRKAIEKDAKA-APDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVP 109
Cdd:cd19973 5 ITKTDTNpFFVKMKEGAQKAAKAlGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 110 IVFFNK--EPsrkaLDSYDKAYyvGTDSKESGIIQGDLIAKHWAAnpnwdlnKDGQIqfVLLKGEPGHPDAEAR------ 181
Cdd:cd19973 85 VIALDTptDP----IDAADATF--ATDNFKAGVLIGEWAKAALGA-------KDAKI--ATLDLTPGHTVGVLRhqgflk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 182 ---TTYVVKELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFG 257
Cdd:cd19973 150 gfgIDEKDPESNEDEDDSQVVGSADTNGDQAKGQTAMENLLQ--KDPDINLVYTINEPAAAGAYQALKAAGKEKgVLIVS 227
|
250
....*....|....*....
gi 504645589 258 VDALPEALALVKSGAMAGT 276
Cdd:cd19973 228 VDGGCPGVKDVKDGIIGAT 246
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
37-322 |
2.74e-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: 380662 [Multi-domain] Cd Length: 271 Bit Score: 41.84 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 37 DNFMSVVRKAIEKDAKAApDVQLLMN-DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNK 115
Cdd:cd20007 11 DPFYITMQCGAEAAAKEL-GVELDVQgPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 116 EPSrkalDSYDKAYYVGTDSKESGIIQGDLIAKHwaanpnwdLNKDGQIqfVLLKGEPGHPDAEARTTYVVKELnDKGLK 195
Cdd:cd20007 90 TLG----DPSFVLSQIASDNVAGGALAAEALAEL--------IGGKGKV--LVINSTPGVSTTDARVKGFAEEM-KKYPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 196 TQQLALDTAMWDTAQAKDKMDAWLSgpnANK-IEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEALALVKSGAM 273
Cdd:cd20007 155 IKVLGVQYSENDPAKAASIVAAALQ---ANPdLAGIFGTNTFSAEGAAAALRNAGKTgKVKVVGFDASPAQVEQLKAGTI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 504645589 274 AGTVLNDANNQAKATFDLAKNLADGKgaadgtnwKIDNKIVrVPYVGVD 322
Cdd:cd20007 232 DALIAQKPAEIGYLAVEQAVAALTGK--------PVPKDIL-TPFVVIT 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
63-328 |
7.84e-04 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380539 [Multi-domain] Cd Length: 294 Bit Score: 40.68 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 63 DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEPS-RKALDSYdkAYYVGTDSKESGII 141
Cdd:cd06316 37 DANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKLVFMDNVPDgLEAGKDY--VSVVSSDNRGNGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 142 QGDLIAKHwaanpnwdLNKDGQIQFVllkgepgHPDAEarttYVVKELNDKGLKTQ--------QLALDTAMWDTAQAKD 213
Cdd:cd06316 115 AAELLAEA--------IGGKGKVGII-------YHDAD----FYATNQRDKAFKDTlkekypdiKIVAEQGFADPNDAEE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 214 KMDAWLSG-PNANKIEVVIannDAMAMGAVEALKAHNKSSIPVFGVDALPE-ALALVKSGAMAGTVLNDANNQAKATFDL 291
Cdd:cd06316 176 VASAMLTAnPDIDGIYVSW---DTPALGVISALRAAGRSDIKITTVDLGTEiALDMAKGGNVKGIGAQRPYDQGVAEALA 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 504645589 292 AKNLADGKGAAdgtnwkidnKIVRVPYVGVDQSNLAE 328
Cdd:cd06316 253 AALALLGKEVP---------PFIGVPPLAVTKDNLLE 280
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
39-259 |
1.88e-03 |
|
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380507 [Multi-domain] Cd Length: 267 Bit Score: 39.44 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 39 FMSVVRkAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKAlAInLVDPAAAGTVIEKARGqNVPIVFFNKEPS 118
Cdd:cd06284 14 YSEILR-GIEDAAAEA-GYDVLLGDTDSDPEREDDLLDMLRSRRVDG-VI-LLSGRLDAELLSELSK-RYPIVQCCEYIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 119 RKALdsydkaYYVGTDSKESGIIQGD-LIAKhwaanpnwdlnkdGQIQFVLLKGEPGHPDAEARTTYVVKELNDKGLKTQ 197
Cdd:cd06284 89 DSGV------PSVSIDNEAAAYDATEyLISL-------------GHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504645589 198 QLALDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNKsSIP----VFGVD 259
Cdd:cd06284 150 EDLIIEGDFSFEAGYAAARALLALPE--RPTAIFCASDELAIGAIKALRRAGL-RVPedvsVIGFD 212
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
28-138 |
3.17e-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: 38.69 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 28 IGVTIYKYDDNFMSVVRKAIEKDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVdpAAAGTVIEKARGQN 107
Cdd:cd06283 2 IGVIVADITNPFSSLLLKGIEDVCREA-GYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPT--GNNNDAYLELAQKG 78
|
90 100 110
....*....|....*....|....*....|.
gi 504645589 108 VPIVFFNKEPSRKALDSydkayyVGTDSKES 138
Cdd:cd06283 79 LPVVLVDRQIEPLNWDT------VVTDNYDA 103
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
39-305 |
4.34e-03 |
|
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380658 Cd Length: 298 Bit Score: 38.41 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 39 FMSVVRKAIEKDAKAaPDVQLLMND-SQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPIVFFNKEP 117
Cdd:cd20003 13 YFTAAGQGAQEAAKE-LGVDVTYDGpTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVTWDSDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 118 SRKALDsydkaYYVG-TDSKESGIIQGDLIAKHwaanpnwdLNKDGQIQFVllKGEPGHPD----AEARTTYVVKELNDK 192
Cdd:cd20003 92 NPDARD-----FFVNqATPEGIGKTLVDMVAEQ--------TGEKGKVAIV--TSSPTATNqnawIKAMKAYIAEKYPDM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 193 GLKTQQLALDTAMWDTAQAKDKMDAWlsgPNANKIEVVIANNDAMAMGAVEALKAHNKssIPVFGVdALPEAL-ALVKSG 271
Cdd:cd20003 157 KIVTTQYGQEDPAKSLQVAENILKAY---PDLKAIIAPDSVALPGAAEAVEQLGRTGK--VAVTGL-STPNVMrPYVKDG 230
|
250 260 270
....*....|....*....|....*....|....
gi 504645589 272 AMAGTVLNDANNQAKATFDLAKNLADGKGAADGT 305
Cdd:cd20003 231 TVKSVVLWDVVDLGYLAVYVARALADGTLLKVGD 264
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
171-259 |
7.79e-03 |
|
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: 37.53 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 171 GEPGHPDAEARTTYVVKELNDKGLKTQQLALDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNK 250
Cdd:cd06288 124 GPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHGDWGRESGYEAAKRLLSAPD--RPTAIFCGNDRMAMGVYQAAAELGL 201
|
90
....*....|...
gi 504645589 251 sSIP----VFGVD 259
Cdd:cd06288 202 -RVPedlsVVGFD 213
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
101-264 |
8.22e-03 |
|
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: 37.23 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 101 EKARGQNVPIVFFNKEPSRKALDSydkayyVGTDSKESGIiqgdLIAKHwaanpnwdLNKDGQIQFVLLkGEPGHPDAEA 180
Cdd:cd06295 80 RELAQQGLPMVVWGAPEDGQSYCS------VGSDNVKGGA----LATEH--------LIEIGRRRIAFL-GDPPHPEVAD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504645589 181 RTTYVVKELNDKGLKTQQLALDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNKsSIP----V 255
Cdd:cd06295 141 RLQGYRDALAEAGLEADPSLLLSCDFTEESGYAAMRALLdSGTA---FDAIFAASDLIAMGAIRALRERGI-SVPgdvaV 216
|
....*....
gi 504645589 256 FGVDALPEA 264
Cdd:cd06295 217 VGYDDIPLA 225
|
|
| |
