|
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: 624.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 2 NKKVFTLTALVASMMLGAAAHAADTKIGVTIYKYDDNFMSMVRKDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAK 81
Cdd:PRK15395 1 NKKVLTLSALMASMLFGAAAAAADTRIGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 82 GVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAKALASYDKAYYVGTDSKESGVIQGQLIEKHWKASPQWDLNKD 161
Cdd:PRK15395 81 GVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANPAWDLNKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 162 GVIQYVLLKGEPGHPDAEARTKYVIETLNKDGIKTKQLALDTAMWDTAQAKDKTDAWLSGPNADKIEVVISNNDAMAMGA 241
Cdd:PRK15395 161 GKIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 242 IEALKAHNKKSIPVFGVDALPEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAATDGTDFKIENKIVRIPYVPV 321
Cdd:PRK15395 241 VEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAEGTNWKIENKVVRVPYVGV 320
|
330
....*....|
gi 1274735229 322 DKDNLSQFTK 331
Cdd:PRK15395 321 DKDNLAEFTK 330
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
27-321 |
4.96e-156 |
|
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380481 [Multi-domain] Cd Length: 302 Bit Score: 438.94 E-value: 4.96e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKEPNAKALASYDKAYYVGTDSKESGVIQGQLIEKHWKASPQWDLNKDGVIQYVLLKGEPGHPDAEARTKYVI 186
Cdd:cd01539 82 NIPVIFFNREPSREDLKSYDKAYYVGTDAEESGIMQGEIIADYWKANPEIDKNGDGKIQYVMLKGEPGHQDAIARTKYSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLNKDGIKTKQLALDTAMWDTAQAKDKTDAWLSGPNaDKIEVVISNNDAMAMGAIEALKAHN------KKSIPVFGVDA 260
Cdd:cd01539 162 KTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYG-DKIELVIANNDDMALGAIEALKAAGyntgdgDKYIPVFGVDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274735229 261 LPEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAATDGTD-FKIENKIVRIPYVPV 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 ... |
28-319 |
2.17e-95 |
|
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: 283.75 E-value: 2.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 28 IGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVvISKAKAAD 107
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPG-VQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGV-AEKARGQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 108 IPVVFFNKEPnakalASYDKAYYVGTDSKESGVIQGQLIEKHWKaspqwdlnkdgvIQYVLLKGEPGHPDAEARTKYVIE 187
Cdd:cd01537 80 VPVVFFDKEP-----SRYDKAYYVITDSKEGGIIQGDLLAKHGH------------IQIVLLKGPLGHPDAEARLAGVIK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 188 TLNKDGIKTKQLALDTAMWDTAQAKDKTDAWLSGPNadKIEVVISNNDAMAMGAIEALKAHNKK---SIPVFGVDALPEA 264
Cdd:cd01537 143 ELNDKGIKTEQLQLDTGDWDTASGKDKMDQWLSGPN--KPTAVIANNDAMAMGAVEALKEHGLRvpsDISVFGYDALPEA 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1274735229 265 LaqiKAGNMAGTVLNDAENQAKATLLMAKNLAAGKaatdgtdfKIENKIVRIPYV 319
Cdd:cd01537 221 L---KSGPLLTTILQDANNLGKTTFDLLLNLADNW--------KIDNKVVRVPYV 264
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
3-326 |
1.39e-63 |
|
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: 203.62 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 3 KKVFTLTALVASMML----------GAAAHAADTKIGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQN 72
Cdd:COG1879 1 KRLALLAAVLALALAlaacgsaaaeAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELG-VELIVVDAEGDAAKQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 73 DQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAKalasyDKAYYVGTDSKESGVIQGQLIEKHWKA 152
Cdd:COG1879 80 SQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGS-----DRVAYVGSDNYAAGRLAAEYLAKALGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 153 SPqwdlnkdgviQYVLLKGEPGHPDAEARTKYVIETLNKDGiKTKQLALDTAMWDTAQAKDKTDAWLSgpNADKIEVVIS 232
Cdd:COG1879 155 KG----------KVAILTGSPGAPAANERTDGFKEALKEYP-GIKVVAEQYADWDREKALEVMEDLLQ--AHPDIDGIFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 233 NNDAMAMGAIEALKAHNKKS-IPVFGVDALPEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAATdgtdfkien 311
Cdd:COG1879 222 ANDGMALGAAQALKAAGRKGdVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVP--------- 292
|
330
....*....|....*
gi 1274735229 312 KIVRIPYVPVDKDNL 326
Cdd:COG1879 293 KEILTPPVLVTKENV 307
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
27-321 |
3.13e-60 |
|
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: 193.99 E-value: 3.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKEPNAKAlasyDKAYYVGTDSKESGVIQGQLIEKhwkaspqwdlNKDGVIQYVLLKGEPGHPDAEARTKYVI 186
Cdd:cd06301 82 GIPLVYVNREPDSKP----KGVAFVGSDDIESGELQMEYLAK----------LLGGKGNIAILDGVLGHEAQILRTEGNK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLNK-DGIKTkqLALDTAMWDTAQAKDKTDAWLSgpNADKIEVVISNNDAMAMGAIEALKAHNKK-SIPVFGVDALPEA 264
Cdd:cd06301 148 DVLAKyPGMKI--VAEQTANWSREKAMDIVENWLQ--SGDKIDAIVANNDEMAIGAILALEAAGKKdDILVAGIDATPDA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1274735229 265 LAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAatdgtdfkiENKIVRIPYVPV 321
Cdd:cd06301 224 LKAMKAGRLDATVFQDAAGQGETAVDVAVKAAKGEE---------VESDIWIPFELV 271
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
28-300 |
3.97e-60 |
|
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: 193.29 E-value: 3.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 28 IGVTIYKYDDNFMSMVRKDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAAD 107
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 108 IPVVFFNKEPNakalaSYDKAYYVGTDSKESGVIQGQLIEKHWKaspqwdlnkdGVIQYVLLKGEPGHPDAEARTKYVIE 187
Cdd:pfam13407 81 IPVVTFDSDAP-----SSPRLAYVGFDNEAAGEAAGELLAEALG----------GKGKVAILSGSPGDPNANERIDGFKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 188 TLNKDGIKTKQLAL-DTAMWDTAQAKDKTDAWLSGpNADKIEVVISNNDAMAMGAIEALKAHNKKSIP-VFGVDALPEAL 265
Cdd:pfam13407 146 VLKEKYPGIKVVAEvEGTNWDPEKAQQQMEALLTA-YPNPLDGIISPNDGMAGGAAQALEAAGLAGKVvVTGFDATPEAL 224
|
250 260 270
....*....|....*....|....*....|....*
gi 1274735229 266 AQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKA 300
Cdd:pfam13407 225 EAIKDGTIDATVLQDPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
27-310 |
2.98e-58 |
|
periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380478 [Multi-domain] Cd Length: 268 Bit Score: 188.93 E-value: 2.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDArETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAA-KELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKEPNAKAlasyDKAYYVGTDSKESGVIQGQLIEKHWkaspqwdlnkDGVIQYVLLKGEPGHPDAEARTKYVI 186
Cdd:cd01536 80 GIPVVAVDTDIDGGG----DVVAFVGTDNYEAGKLAGEYLAEAL----------GGKGKVAILEGPPGSSTAIDRTKGFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLNKDGiKTKQLALDTAMWDTAQAKDKTDAWL-SGPNadkIEVVISNNDAMAMGAIEALKAHNK-KSIPVFGVDALPEA 264
Cdd:cd01536 146 EALKKYP-DIEIVAEQPANWDRAKALTVTENLLqANPD---IDAVFAANDDMALGAAEALKAAGRtGDIKIVGVDGTPEA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1274735229 265 LAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAATDGTDFKIE 310
Cdd:cd01536 222 LKAIKDGELDATVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPVT 267
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
27-329 |
3.81e-53 |
|
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: 175.92 E-value: 3.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDAREtGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKE-LNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVffnkEPNAKaLASYDKAYYVGTDSKESGVIQGQ-LIEKhwkaspqwdLNKDGviQYVLLKGEPGHPDAEARTKYV 185
Cdd:cd06313 80 GIPLV----GVNAL-IENEDLTAYVGSDDVVAGELEGQaVADR---------LGGKG--NVVILEGPIGQSAQIDRGKGI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 186 IETLNKD-GIKTkqLALDTAMWDTAQAKDKTDAWLSGpNADKIEVVISNNDAMAMGAIEALKAHNKKSIPVFGVDALPEA 264
Cdd:cd06313 144 ENVLKKYpDIKV--LAEQTANWSRDEAMSLMENWLQA-YGDEIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDA 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274735229 265 LAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAatdgtdfkiENKIVRIPYVPVDKDNLSQF 329
Cdd:cd06313 221 LQAVKSGELIATVLQDAEAQGKGAVEVAVDAVKGEG---------VEKKYYIPFVLVTKDNVDDY 276
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
27-322 |
1.50e-37 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 135.40 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTI-------YKYDDNFMsmvrkdiEKDAREtGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVV 99
Cdd:cd19992 1 KIGVSFptqqeerWQKDKEYM-------EEEAKE-LGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 100 ISKAKAADIPVVFFNKEPNAKalasyDKAYYVGTDSKESGVIQGQ-LIEKHWKASpqwdlnkdgviqYVLLKGEPGHPDA 178
Cdd:cd19992 73 VDKAKAAGVPVISYDRLILNA-----DVDLYVGRDNYKVGQLQAEyALEAVPKGN------------YVILSGDPGDNNA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 179 EARTKYVIETLNKDGIKTK-QLALDTAM--WDTAQAKDKTDAWLSGpNADKIEVVISNNDAMAMGAIEALKAHN-KKSIP 254
Cdd:cd19992 136 QLITAGAMDVLQPAIDSGDiKIVLDQYVkgWSPDEAMKLVENALTA-NNNNIDAVLAPNDGMAGGAIQALKAQGlAGKVF 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274735229 255 VFGVDALPEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAATDgTDFKIENKIVRIPYVPVD 322
Cdd:cd19992 215 VTGQDAELAALKRIVEGTQTMTVWKDLKELARAAADAAVKLAKGEKPQT-TDETINNGGKDVPAILIP 281
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
44-326 |
1.07e-34 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 128.71 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 44 RKDIEKDARETGGVALLMNdSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVffnkepnakala 123
Cdd:COG4213 21 GDNFKAALKELGYEVDVQN-ANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVI------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 124 SYDK-------AYYVGTDSKESGVIQGQLIEKHwkaspqwdLNKDGVIQYVLLKGEPGhpDAEARTKY-----VIETLNK 191
Cdd:COG4213 88 AYDRlilnsdvDYYVSFDNVKVGELQGQYLVDG--------LPLKGKGNIELFGGSPT--DNNATLFFegamsVLQPYID 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 192 DG---IKTKQLALDtamWDTAQAKDKTDAWLSGpNADKIEVVISNNDAMAMGAIEALKAHNKKSIPVF-GVDALPEALAQ 267
Cdd:COG4213 158 SGklvVVSGQWTLG---WDPETAQKRMENLLTA-NGNKVDAVLAPNDGLAGGIIQALKAQGLAGKVVVtGQDAELAAVQR 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274735229 268 IKAGNMAGTVLNDAENQAKATLLMAKNLAAG-KAATDGTdfkIENKIVRIPY-----VPVDKDNL 326
Cdd:COG4213 234 ILAGTQYMTVYKDTRELAEAAAELAVALAKGeKPEVNGT---YDNGKKDVPSyllepVAVTKDNV 295
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
43-279 |
1.38e-33 |
|
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: 124.58 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 43 VRKDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEpnakaL 122
Cdd:cd06308 17 MNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVLDRK-----V 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 123 ASYDKAYYVGTDSKESGVIQGQLIEKhwkaspqwDLNKDGVIqyVLLKGEPGHPDAEARTKYVIETLNK-DGIktKQLAL 201
Cdd:cd06308 92 SGDDYTAFIGADNVEIGRQAGEYIAE--------LLNGKGNV--VEIQGLPGSSPAIDRHKGFLEAIAKyPGI--KIVAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 202 DTAMWDTAQAKDKTDAWLSgpNADKIEVVISNNDAMAMGAIEALKAHNK-KSIPVFGVDALPEALAQ-IKAGNMAGTVLN 279
Cdd:cd06308 160 QDGDWLRDKAIKVMEDLLQ--AHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGLPEAGEKaVKDGILAATFLY 237
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
27-325 |
2.81e-31 |
|
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: 118.86 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRG-YELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFnkepnAKALASYDKAYY---VGTDSKESGVIQGQLIEKHWKaspqwdlNKDGVIqyVLLKGEPGHPDAEARTK 183
Cdd:cd06309 80 GIPVILV-----DRTIDGEDGSLYvtfIGSDFVEEGRRAAEWLVKNYK-------GGKGNV--VELQGTAGSSVAIDRSK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 184 YVIETLNKDGiKTKQLALDTAMWDTAQAKDKTDAWL-SGPnaDKIEVVISNNDAMAMGAIEALKAHNK---KSIPVFGVD 259
Cdd:cd06309 146 GFREVIKKHP-NIKIVASQSGNFTREKGQKVMENLLqAGP--GDIDVIYAHNDDMALGAIQALKEAGLkpgKDVLVVGID 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274735229 260 ALPEALAQIKAGNMAGTVLNDAeNQAKATLLMAKNLAAGKaatdgtdfKIEnKIVRIPYVPVDKDN 325
Cdd:cd06309 223 GQKDALEAIKAGELNATVECNP-LFGPTAFDTIAKLLAGE--------KVP-KLIIVEERLFDKDN 278
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
27-303 |
4.87e-31 |
|
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: 117.78 E-value: 4.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDAREtGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKE-LGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKepnakALASYDKAYYVGTDSKESGVIQGQLIEKhwKASPQWdlnkdgviQYVLLKGEPGHPDAEARTKYVI 186
Cdd:cd06323 80 GIPVITVDR-----SVTGGKVVSHIASDNVAGGEMAAEYIAK--KLGGKG--------KVVELQGIPGTSAARERGKGFH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLNKDGiKTKQLALDTAMWDTAQAKDKTDAWL-SGPNADKievVISNNDAMAMGAIEALKAHNKKSIPVFGVDALPEAL 265
Cdd:cd06323 145 NAIAKYP-KINVVASQTADFDRTKGLNVMENLLqAHPDIDA---VFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAV 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 1274735229 266 AQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAATD 303
Cdd:cd06323 221 KAVKDGKLAATVAQQPEEMGAKAVETADKYLKGEKVPK 258
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
27-309 |
9.61e-31 |
|
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: 117.10 E-value: 9.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLG-VKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKEPNAKALASydkayYVGTDSKESGVIQGQLIEKHWKaspqwdlNKDGVIqyvLLKGEPGHPDAEARTKYVI 186
Cdd:cd19968 80 GIPVVTVDRRAEGAAPVP-----HVGADNVAGGREVAKFVVDKLP-------NGAKVI---ELTGTPGSSPAIDRTKGFH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLNKdGIKTKQLALDTAMWDTAQAKDKTDAWLSGpNADKIEVVISNNDAMAMGAIEALKAH--NKKSIPVFGVDALPEA 264
Cdd:cd19968 145 EELAA-GPKIKVVFEQTGNFERDEGLTVMENILTS-LPGPPDAIICANDDMALGAIEAMRAAglDLKKVKVIGFDAVPDA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1274735229 265 LAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAATDGTDFKI 309
Cdd:cd19968 223 LQAIKDGELYATVEQPPGGQARTALRILVDYLKDKKAPKKVNLKP 267
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
27-327 |
3.11e-30 |
|
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: 115.82 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETG-GVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKA 105
Cdd:cd06320 1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGvKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 106 ADIPVVFFNKEPNAKAL--ASYDKAYYVGTDSKESGVIQGQ-LIEKhwkaspqwdLNKDGviQYVLLKGEPGHPDAEART 182
Cdd:cd06320 81 KGIPVINLDDAVDADALkkAGGKVTSFIGTDNVAAGALAAEyIAEK---------LPGGG--KVAIIEGLPGNAAAEART 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 183 KYVIETLNKDGiKTKQLALDTAMWDTAQAKDKTDAWLSGpNADkIEVVISNNDAMAMGAIEALKAHNKKS-IPVFGVDAL 261
Cdd:cd06320 150 KGFKETFKKAP-GLKLVASQPADWDRTKALDAATAILQA-HPD-LKGIYAANDTMALGAVEAVKAAGKTGkVLVVGTDGI 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274735229 262 PEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKaatdgtdfKIENKIVrIPYVPVDKDNLS 327
Cdd:cd06320 227 PEAKKSIKAGELTATVAQYPYLEGAMAVEAALRLLQGQ--------KVPAVVA-TPQALITKDNVD 283
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
45-317 |
5.40e-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: 113.11 E-value: 5.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 45 KDIEKDARETGGVALLMNdSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVffnkepnakalaS 124
Cdd:cd19994 19 ENLKSELEEAGYTVDLQY-ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVI------------A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 125 YDK--------AYYVGTDSKESGVIQGQLIEKHWKaspqwDLNKDGVIQYVLLKGEPGHPDAEARTKYVIETLN---KDG 193
Cdd:cd19994 86 YDRlimntdavDYYVTFDNEKVGELQGQYLVDKLG-----LKDGKGPFNIELFAGSPDDNNAQLFFKGAMEVLQpyiDDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 194 ---IKTKQLALD---TAMWDTAQAKDKTDAWLSGPNAD--KIEVVISNNDAMAMGAIEALKAHNKKSIP---VFGVDALP 262
Cdd:cd19994 161 tlvVRSGQTTFEqvaTPDWDTETAQARMETLLSAYYTGgkKLDAVLSPNDGIARGVIEALKAAGYDTGPwpvVTGQDAED 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1274735229 263 EALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAATDGTDFKIENKIVRIP 317
Cdd:cd19994 241 ASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVEVNDTKTYDNGVKVVP 295
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
27-325 |
1.45e-27 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 108.65 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLG-VELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNK--EPNAKAlasydkAYYVGTDSKESGVIQGqliekHWKAspqwDLNKDGVIQYVLLKGEPGHPDAEARTKY 184
Cdd:cd06318 80 GIPVITVDSalDPSANV------ATQVGRDNKQNGVLVG-----KEAA----KALGGDPGKIIELSGDKGNEVSRDRRDG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 185 VIETLN--------KDGIKTKQLALD--------TAMWDTAQAkdktdawlsgpNADkIEVVISNNDAMAMGAIEALKAH 248
Cdd:cd06318 145 FLAGVNeyqlrkygKSNIKVVAQPYGnwirsgavAAMEDLLQA-----------HPD-INVVYAENDDMALGAMKALKAA 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274735229 249 NK-KSIPVFGVDALPEALAQIKAGNMAGTVLNDAENQAKATLLMAKnlaagKAATDGTDFKienKIVRIPYVPVDKDN 325
Cdd:cd06318 213 GMlDKVKVAGADGQKEALKLIKDGKYVATGLNDPDLLGKTAVDTAA-----KVVKGEESFP---EFTYTPTALITKDN 282
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
27-295 |
4.62e-26 |
|
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: 104.71 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGGVALLMnDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVF-DHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKEPNAKALAsydKAYYVgTDSKESGVIQGQLIEKhwkaspqwDLNKDGviQYVLLKGEPGHPDAEARTKYVI 186
Cdd:cd19967 80 GIPVFLIDREINAEGVA---VAQIV-SDNYQGAVLLAQYFVK--------LMGEKG--LYVELLGKESDTNAQLRSQGFH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLnKDGIKTKQLALDTAMWDTAQAKDKTDAWL-SGPnadKIEVVISNNDAMAMGAIEALKAHNK-KSIPVFGVDALPEA 264
Cdd:cd19967 146 SVI-DQYPELKMVAQQSADWDRTEAFEKMESILqANP---DIKGVICGNDEMALGAIAALKAAGRaGDVIIVGFDGSNDV 221
|
250 260 270
....*....|....*....|....*....|.
gi 1274735229 265 LAQIKAGNMAGTVLNDAENQAKATLLMAKNL 295
Cdd:cd19967 222 RDAIKEGKISATVLQPAKLIARLAVEQADQY 252
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
59-299 |
1.05e-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: 103.91 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 59 LLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFnkepnAKALASYDKAYYVGTDSKES 138
Cdd:cd19995 35 VIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAY-----DRLILGGPADYYVSFDNVAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 139 GVIQGQLIEKHWKAspqwdlNKDGVIQYVLLKGEPGHPDAEARTK---YVIETLNKDGIKTKQLALDTAMWDTAQAKDKT 215
Cdd:cd19995 110 GEAQAQSLVDHLKA------IGKKGVNIVMINGSPTDNNAGLFKKgahEVLDPLGDSGELKLVCEYDTPDWDPANAQTAM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 216 DAWLSgPNADKIEVVISNNDAMAMGAIEALKAHNKKSIPVF-GVDALPEALAQIKAGNMAGTVLNDAENQAKATLLMAKN 294
Cdd:cd19995 184 EQALT-KLGNNIDGVLSANDGLAGGAIAALKAQGLAGKVPVtGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVA 262
|
....*
gi 1274735229 295 LAAGK 299
Cdd:cd19995 263 LLKGE 267
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
27-321 |
1.65e-24 |
|
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: 100.35 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDArETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAV-EANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKEPNAKALAsydkAYYVGTDSKESGVIQGQ-LIEKHWKASpqwdlnkdgviQYVLLKgepgHPDAEA---RT 182
Cdd:cd19971 80 GIPVINVDTPVKDTDLV----DSTIASDNYNAGKLCGEdMVKKLPEGA-----------KIAVLD----HPTAEScvdRI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 183 KYVIETLnKDGIKTKQLALDTAMWDTAQAKDKTDAWLSgpNADKIEVVISNNDAMAMGAIEALKAHNK-KSIPVFGVDAL 261
Cdd:cd19971 141 DGFLDAI-KKNPKFEVVAQQDGKGQLEVAMPIMEDILQ--AHPDLDAVFALNDPSALGALAALKAAGKlGDILVYGVDGS 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 262 PEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKaatdgtdfKIENKIvripYVPV 321
Cdd:cd19971 218 PDAKAAIKDGKMTATAAQSPIEIGKKAVETAYKILNGE--------KVEKEI----VVPT 265
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
45-322 |
8.45e-23 |
|
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: 95.77 E-value: 8.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 45 KDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVffnkepnakalaS 124
Cdd:cd19991 18 RDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVL------------A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 125 YDKA-------YYVGTDSKESGVIQGQLIekhwkaspqwdLNKDGVIQYVLLKGEPGHPDAEARTKYVIETLNKDGIKTK 197
Cdd:cd19991 86 YDRLilnadvdLYVSFDNEKVGELQAEAL-----------VKAKPKGNYVLLGGSPTDNNAKLFREGQMKVLQPLIDSGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 198 -QLALDTAM--WDTAQAKDKTDAWLSGpNADKIEVVISNNDAMAMGAIEALKAHN-KKSIPVFGVDALPEALAQIKAGNM 273
Cdd:cd19991 155 iKVVGDQWVddWDPEEALKIMENALTA-NNNKIDAVIASNDGTAGGAIQALAEQGlAGKVAVSGQDADLAACQRIVEGTQ 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1274735229 274 AGTVLNDAENQAKATLLMAKNLAAGKA-ATDGTDFkieNKIVRIPYVPVD 322
Cdd:cd19991 234 TMTIYKPIKELAEKAAELAVALAKGEKnEANRTIN---NGKKEVPSILLD 280
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
49-300 |
1.48e-22 |
|
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: 95.24 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 49 KDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKepnakaLASYDKA 128
Cdd:cd19993 22 KKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDR------LIENPIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 129 YYVGTDSKESGVIQGQLIekhWKASPQWDlnkdgviqYVLLKGEPGHPDAEARTKYVIETLNK--DGIKTKQLA-LDTAM 205
Cdd:cd19993 96 FYISFDNVEVGRMQARGV---LKAKPEGN--------YVFIKGSPTDPNADFLRAGQMEVLQPaiDSGKIKIVGeQYTDG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 206 WDTAQAKDKTDAWLSGpNADKIEVVISNNDAMAMGAIEALKAHN-KKSIPVFGVDALPEALAQIKAGNMAGTVLNDAENQ 284
Cdd:cd19993 165 WKPANAQKNMEQILTA-NNNKVDAVVASNDGTAGGAVAALAAQGlAGKVPVSGQDADKAALNRIALGTQTVTVWKDAREL 243
|
250
....*....|....*.
gi 1274735229 285 AKATLLMAKNLAAGKA 300
Cdd:cd19993 244 GKEAAEIAVELAKGTK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
27-326 |
1.96e-21 |
|
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: 92.04 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELG-YEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKEPNakalaSYDKAYYVGTDSKESGVIQGQLIEKHWKASPqWDLNKdgviqYVLLKGEPGHPDAEARTKYVI 186
Cdd:cd06319 80 KIPVVIADIGTG-----GGDYVSYIISDNYDGGYQAGEYLAEALKENG-WGGGS-----VGIIAIPQSRVNGQARTAGFE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLNKDGIKTKQLALdTAMWDTAQAKDKT-DAWLSGPnadKIEVVISNNDAMAMGAIEALKAHNKKS-IPVFGVDALPEA 264
Cdd:cd06319 149 DALEEAGVEEVALRQ-TPNSTVEETYSAAqDLLAANP---DIKGIFAQNDQMAQGALQAIEEAGRTGdILVVGFDGDPEA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274735229 265 LAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAATDgtdfkienKIVRIPYVPVDKDNL 326
Cdd:cd06319 225 LDLIKDGKLDGTVAQQPFGMGARAVELAIQALNGDNTVE--------KEIYLPVLLVTSENV 278
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
28-273 |
2.63e-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: 91.57 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 28 IGVTIYKYDDNFMSMVRKDIEKDArETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAAD 107
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEA-AELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 108 IPVVFFNKEPNAKALASydkayYVGTDSKESGVIQGQLIEKHWkaspqwdLNKDGVIQYVllkgepGHPDAEArtkyVIE 187
Cdd:cd06322 81 IPVFTVDVKADGAKVVT-----HVGTDNYAGGKLAGEYALKAL-------LGGGGKIAII------DYPEVES----VVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 188 TLN--KDGIKT----KQLALDTAMWDTAQAKDKTDAWLSGpnADKIEVVISNNDAMAMGAIEALK-AHNKKSIPVFGVDA 260
Cdd:cd06322 139 RVNgfKEAIKKypniEIVAEQPGDGRREEALAATEDMLQA--NPDLDGIFAIGDPAALGALTAIEsAGKEDKIKVIGFDG 216
|
250
....*....|...
gi 1274735229 261 LPEALAQIKAGNM 273
Cdd:cd06322 217 NPEAIKAIAKGGK 229
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
45-317 |
1.43e-20 |
|
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: 89.79 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 45 KDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNkepnaKALAS 124
Cdd:cd01538 18 RDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYD-----RLILN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 125 YDKAYYVGTDSKESGVIQGqliekhwkaspQWDLNKDGVIQYVLLKGEPGHPDAEARTKYVIETLNKDGIKTKQLALD-- 202
Cdd:cd01538 93 ADVDYYISFDNEKVGELQA-----------QALLDAKPEGNYVLIGGSPTDNNAKLFRDGQMKVLQPAIDSGKIKVVGdq 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 203 -TAMWDTAQAKDKTDAWLSGpNADKIEVVISNNDAMAMGAIEALKAHN-KKSIPVFGVDALPEALAQIKAGNMAGTVLND 280
Cdd:cd01538 162 wVDDWLPANAQQIMENALTA-NGNNVDAVVASNDGTAGGAIAALKAQGlSGGVPVSGQDADLAAIKRILAGTQTMTVYKD 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1274735229 281 AENQAKATLLMAKNLAAGKAATDGTdfKIENKIVRIP 317
Cdd:cd01538 241 IRLLADAAAEVAVALMRGEKPPING--TTNNGLKDVP 275
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
64-257 |
4.93e-19 |
|
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: 85.82 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 64 SQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEpnakalASYDKAYYVGTDSKESGVIQG 143
Cdd:cd19999 42 ADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQP------VSSPDAINVVIDQYKWAAIQA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 144 Q-LIEKhwkaspqwdLNKDGVIqyVLLKGEPGHPDAEARTKYVIETLNKD-GIKTkqLALDTAMWDTAQAKDKTDAWLSg 221
Cdd:cd19999 116 QwLAEQ---------LGGKGNI--VAINGVAGNPANEARVKAADDVFAKYpGIKV--LASVPGGWDQATAQQVMATLLA- 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 1274735229 222 pNADKIEVVIsNNDAMAMGAIEALKAHNKKSIPVFG 257
Cdd:cd19999 182 -TYPDIDGVL-TQDGMAEGVLRAFQAAGKDPPVMTG 215
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-277 |
1.42e-18 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 84.37 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 1 MNKKVFTL-TALVASMMLGAAAHAADTkIGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLI 79
Cdd:PRK10653 2 NMKKLATLvSAVALSATVSANAMAKDT-IALVVSTLNNPFFVSLKDGAQKEADKLG-YNLVVLDSQNNPAKELANVQDLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 80 AKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAKALASYdkayyVGTDSKESGVIQGQLIEKhwKASpqwdlN 159
Cdd:PRK10653 80 VRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSH-----IASDNVAGGKMAGDFIAK--KLG-----E 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 160 KDGVIQyvlLKGEPGHPDAEARTKYVIETLNKDgiKTKQLALDTAMWDTAQAKDKTDAWLSGpNADkIEVVISNNDAMAM 239
Cdd:PRK10653 148 GAKVIQ---LEGIAGTSAARERGEGFKQAVAAH--KFNVLASQPADFDRTKGLNVMQNLLTA-HPD-VQAVFAQNDEMAL 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 1274735229 240 GAIEALKAHNKKSIPVFGVDALPEALAQIKAGNMAGTV 277
Cdd:PRK10653 221 GALRALQTAGKSDVMVVGFDGTPDGIKAVNRGKLAATI 258
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
59-259 |
3.01e-18 |
|
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: 83.44 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 59 LLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAKALASydkayYVGTDSKES 138
Cdd:cd19996 35 LIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSGVGSDKYTA-----FVGVDDAAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 139 GVIQGQ-LIEKhwkaspqwdLNKDGVIqyVLLKGEPGHPDAEARTKYVIETLNKD-GIKTkqLALDTAMWDTAQAKDKTD 216
Cdd:cd19996 110 GRVGAEwLVKQ---------LGGKGNI--IALRGIAGVSVSEDRWAGAKEVFKEYpGIKI--VGEVYADWDYAKAKQAVE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1274735229 217 AWLS-GPnadKIEVVISNNDAMAMGAIEALKAHNKKSIPVFGVD 259
Cdd:cd19996 177 SLLAaYP---DIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTGED 217
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
35-277 |
5.46e-18 |
|
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: 82.24 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 35 YDDNFMSMVRKDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFN 114
Cdd:cd06314 9 LNNPFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 115 KE-PNAKALAsydkayYVGTDSKESGVIQGQLIekhWKASPqwdlnkdGVIQYVLLKGEPGHPDAEARTKYVIETLnKDG 193
Cdd:cd06314 89 SDaPDSKRLA------YIGTDNYEAGREAGELM---KKALP-------GGGKVAIITGGLGADNLNERIQGFKDAL-KGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 194 IKTKQLALDTAMWDTAQAKDKTDAWLSG-PNADKIEVVISNNdamAMGAIEALKAHNK-KSIPVFGVDALPEALAQIKAG 271
Cdd:cd06314 152 PGIEIVDPLSDNDDIAKAVQNVEDILKAnPDLDAIFGVGAYN---GPAIAAALKDAGKvGKVKIVGFDTLPETLQGIKDG 228
|
....*.
gi 1274735229 272 NMAGTV 277
Cdd:cd06314 229 VIAATV 234
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
1-310 |
4.83e-16 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 77.22 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 1 MNK--KVFTLTAlVASMMLGAAAHAADtkIGVTIYKYDDNFMSMVRKDIEKDARETG-GVALLMNDSQNDQSKQNDQVDV 77
Cdd:PRK09701 1 MNKylKYFSGTL-VGLMLSTSAFAAAE--YAVVLKTLSNPFWVDMKKGIEDEAKTLGvSVDIFASPSEGDFQSQLQLFED 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 78 LIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAKALASYDKAY--YVGTDSKESGVIQGQLIEKHWKASPQ 155
Cdd:PRK09701 78 LSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKKAGGNVeaFVTTDNVAVGAKGASFIIDKLGAEGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 156 wdlnkdgviQYVLLKGEPGHPDAEARTKYVIETLNKDGiKTKQLALDTAMWDTAQAKD-KTDAWLSGPNadkIEVVISNN 234
Cdd:PRK09701 158 ---------EVAIIEGKAGNASGEARRNGATEAFKKAS-QIKLVASQPADWDRIKALDvATNVLQRNPN---IKAIYCAN 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274735229 235 DAMAMGAIEALKAHNKKS-IPVFGVDALPEALAQIKAGNMAGTVLND-AENQAKATLLMAKNLAAGKAATDGTDFKIE 310
Cdd:PRK09701 225 DTMAMGVAQAVANAGKTGkVLVVGTDGIPEARKMVEAGQMTATVAQNpADIGATGLKLMVDAEKSGKVIPLDKAPEFK 302
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
27-302 |
5.74e-16 |
|
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: 76.71 E-value: 5.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKG-YKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKEPnakalASYDKAYYVGTDSKESGVIQGQLIEKHwkaspqwdlnKDGVIQYVLLKGEPGHPDAEARTKYVI 186
Cdd:cd19972 80 GIPVIAVDRNP-----EDAPGDTFIATDSVAAAKELGEWVIKQ----------TGGKGEIAILHGQLGTTPEVDRTKGFQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLNKDGIKtKQLALDTAMWDTAQA-KDKTDAWLSGPNadkIEVVISNNDAMAMGAIEALKAHNK-KSIPVFGVDALPEA 264
Cdd:cd19972 145 EALAEAPGI-KVVAEQTADWDQDEGfKVAQDMLQANPN---ITVFFGQSDAMALGAAQAVKVAGLdHKIWVVGFDGDVAG 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 1274735229 265 LAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAAT 302
Cdd:cd19972 221 LKAVKDGVLDATMTQQTQKMGRLAVDSAIDLLNGKAVP 258
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
39-285 |
1.98e-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: 74.98 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 39 FMSMvRKDIEKDARETGGVALLMNDSQNDQS--KQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKE 116
Cdd:cd19970 14 FIEM-EKGARKHAKEANGYELLVKGIKQETDieQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 117 PNAKALASYDKAY-YVGTDSKESGVIQGQLIEKHwkaspqwdLNKDGviQYVLLKGEPGHPDAEARTKYVIETLNKDGIK 195
Cdd:cd19970 93 LDADALKEGGINVpFVGPDNRQGAYLAGDYLAKK--------LGKGG--KVAIIEGIPGADNAQQRKAGFLKAFEEAGMK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 196 TkqLALDTAMWDTAQAKDKTDAWLSG-PNadkIEVVISNNDAMAMGAIEALKAHNKKS-IPVFGVDALPEALAQIKAGNM 273
Cdd:cd19970 163 I--VASQSANWEIDEANTVAANLLTAhPD---IRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKM 237
|
250
....*....|..
gi 1274735229 274 AGTVLNDAENQA 285
Cdd:cd19970 238 LATIDQHPAKQA 249
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
36-277 |
2.17e-15 |
|
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: 74.96 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 36 DDNFMSMVRKDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNK 115
Cdd:cd06312 11 SDPFWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAINS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 116 EPnakalaSYDKAY-----YVGTDSKESGVIQGQliekhwkaspqwDLNKDGVIQYVLLKGEPGHPDAEARTKYVIETLN 190
Cdd:cd06312 91 GD------DRSKERlgaltYVGQDEYLAGQAAGE------------RALEAGPKNALCVNHEPGNPGLEARCKGFADAFK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 191 KDGIKTKQLALDTamwDTAQAKDKTDAWLsgpNADK-IEVVISNNDAMAMGAIEALKAHNKKS-IPVFGVDALPEALAQI 268
Cdd:cd06312 153 GAGILVELLDVGG---DPTEAQEAIKAYL---QADPdTDAVLTLGPVGADPALKAVKEAGLKGkVKIGTFDLSPETLEAI 226
|
....*....
gi 1274735229 269 KAGNMAGTV 277
Cdd:cd06312 227 KDGKILFAI 235
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
27-277 |
8.92e-15 |
|
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: 73.08 E-value: 8.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIeKDARETGGVALLMNDSQN-DQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKA 105
Cdd:cd19965 1 KFVFVTHVTTNPFFQPVKKGM-DDACELLGAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 106 ADIPVVFFN---KEPNAKALAsydkayYVGTDSKESGVIQGQLIEKhwkaspqwdLNKDGVIQYVLLKGEPGHPDAEART 182
Cdd:cd19965 80 AGIPVVAFNvdaPGGENARLA------FVGQDLYPAGYVLGKRIAE---------KFKPGGGHVLLGISTPGQSALEQRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 183 KYVIETL--NKDGIKTKQLALDTamwDTAQAKDKTDAWLSG-PNadkIEVVISNNDAMAMGAIEALKAHN-KKSIPVFGV 258
Cdd:cd19965 145 DGIKQALkeYGRGITYDVIDTGT---DLAEALSRIEAYYTAhPD---IKAIFATGAFDTAGAGQAIKDLGlKGKVLVGGF 218
|
250
....*....|....*....
gi 1274735229 259 DALPEALAQIKAGNMAGTV 277
Cdd:cd19965 219 DLVPEVLQGIKAGYIDFTI 237
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
27-310 |
1.31e-14 |
|
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: 72.76 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGG-VALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKA 105
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVkIIFVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 106 ADIPVVFFNKEPNAKALASydkayYVGTDSKESGVIQGQ-LIEKhwkaspqwdLNKDGVIqyVLLKGEPGHPDAEARTKY 184
Cdd:cd06310 81 KGIPVIVIDSGIKGDAYLS-----YIATDNYAAGRLAAQkLAEA---------LGGKGKV--AVLSLTAGNSTTDQREEG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 185 VIETLNKDGIKTKQLALDTAMWDTAQAKDKTDAWLSG-PNADkieVVISNNDAMAMGAIEALK-AHNKKSIPVFGVDALP 262
Cdd:cd06310 145 FKEYLKKHPGGIKVLASQYAGSDYAKAANETEDLLGKyPDID---GIFATNEITALGAAVAIKsRKLSGQIKIVGFDSQE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1274735229 263 EALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKAATDGTDFKIE 310
Cdd:cd06310 222 ELLDALKNGKIDALVVQNPYEIGYEGIKLALKLLKGEEVPKNIDTGAE 269
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
49-271 |
1.76e-14 |
|
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: 72.36 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 49 KDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAA-GVVISKAKAADIPVVFFNKePNAKALASYDK 127
Cdd:cd19966 23 KDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAyTPLIEAAKKAGIIVTSFNT-DLPKLEYGDCG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 128 AYYVGTDSKESGVIQGQ-LIEKHwkaspqwDLNK-DGVIQYVLLkgePGHPDAEARTKYVIETLNKDGIKTKQLALDTAM 205
Cdd:cd19966 102 LGYVGADLYAAGYTLAKeLVKRG-------GLKTgDRVFVPGLL---PGQPYRVLRTKGVIDALKEAGIKVDYLEISLEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274735229 206 WDTAQAKDKTDAWLSGPNADKieVVISNNDAMAMGAIEALKAHNKK--SIPVFGVDALPEALAQIKAG 271
Cdd:cd19966 172 NKPAEGIPVMTGYLAANPDVK--AIVGDGGGLTANVAKYLKAAGKKpgEIPVAGFDLSPATVQAIKSG 237
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
63-328 |
4.86e-14 |
|
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: 71.59 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 63 DSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAKAlasydkAYYVGTDSKESGVIQ 142
Cdd:cd06300 41 NSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGAVTSPD------AYNVSNDQVEWGRLG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 143 GQLIEKHwkaspqwdLNKDGVIqyVLLKGEPGHPDAEARTKYVIETLNKDGiKTKQLALDTAMWDTAQAKDKTDAWL-SG 221
Cdd:cd06300 115 AKWLFEA--------LGGKGNV--LVVRGIAGAPASADRHAGVKEALAEYP-GIKVVGEVFGGWDEATAQTAMLDFLaTH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 222 PNADKievvISNNDAMAMGAIEALKAHNKKSIPVFGVD---ALPEALAQIKAGNMAGTVLNDAENQAKAtllmaknLAAG 298
Cdd:cd06300 184 PQVDG----VWTQGGEDTGVLQAFQQAGRPPVPIVGGDengFAKQWWKHPKKGLTGAAVWPPPAIGAAG-------LEVA 252
|
250 260 270
....*....|....*....|....*....|
gi 1274735229 299 KAATDGTDFKIenKIVRIPYVPVDKDNLSQ 328
Cdd:cd06300 253 LRLLEGQGPKP--QSVLLPPPLITNDDAKA 280
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
26-329 |
6.47e-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: 380540 [Multi-domain] Cd Length: 281 Bit Score: 70.87 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 26 TKIGVTIYKYDDNFMSMVRKdiEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKA 105
Cdd:cd06317 1 TIALVQINQQAQFFNQINQG--AQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 106 ADIPVVFFNKEPNAKALASydkayYVGTDSKESGVIQGQLIEKHWKASPQwDLNKDGVI----QYVLLKGEPGHPDAEAR 181
Cdd:cd06317 79 AGIPVIAYDAVIPSDFQAA-----QVGVDNLEGGKEIGKYAADYIKAELG-GQAKIGVVgalsSLIQNQRQKGFEEALKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 182 TKYVIETLNKDGiktkQLALDTAMwdtAQAKDKTDAwlsgpNADkIEVVISNNDAMAMGAIEALKAHNK-KSIPVFGVDA 260
Cdd:cd06317 153 NPGVEIVATVDG----QNVQEKAL---SAAENLLTA-----NPD-LDAIYATGEPALLGAVAAVRSQGRqGKIKVFGWDL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 261 LPEALAQ-IKAGNMAGTVLNDAENQAKATLLMAKNLAAGKaatdgtdfKIEnKIVRIPYVPVDKDNLSQF 329
Cdd:cd06317 220 TKQAIFLgIDEGVLQAVVQQDPEKMGYEAVKAAVKAIKGE--------DVE-KTIDVPPTIVTKENVDQF 280
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
27-301 |
2.58e-13 |
|
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: 68.85 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETG-GVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKA 105
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINpGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 106 ADIPVVFFNKepNAKALASydkayYVGTDSKESGVIQGQ-LIEKhwkaspqwdLNKDGVIqyVLLKGEP---------GH 175
Cdd:cd06321 81 AGIIVVAVDV--AAEGADA-----TVTTDNVQAGYLACEyLVEQ---------LGGKGKV--AIIDGPPvsavidrvnGC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 176 PDAEARTKYVIETLNKDGIKTKQLALdTAMWDTAQAKDKTDAwlsgpnadkievVISNNDAMAMGAIEALKAHNKKSIPV 255
Cdd:cd06321 143 KEALAEYPGIKLVDDQNGKGSRAGGL-SVMTRMLTAHPDVDG------------VFAINDPGAIGALLAAQQAGRDDIVI 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1274735229 256 FGVDALPEALAQIKAGN--MAGTVLNDAENQAKATLLMAKNLAAGKAA 301
Cdd:cd06321 210 TSVDGSPEAVAALKREGspFIATAAQDPYDMARKAVELALKILNGQEP 257
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
36-331 |
5.66e-13 |
|
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: 68.40 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 36 DDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVD-PAAAGVVISKAKAADIPVVFFN 114
Cdd:cd06324 11 DEPFWQNVTRFMQAAAKDLG-IELEVLYANRNRFKMLELAEELLARPPKPDYLILVNeKGVAPELLELAEQAKIPVFLIN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 115 KEPNAKALASYDK-----AYYVGT---DSKESG-VIQGQLIEKHWKaspqwdLNKDGVIQYVLLKGEPGHPDAEARTKYV 185
Cdd:cd06324 90 NDLTDEERALLGKprekfKYWLGSivpDNEQAGyLLAKALIKAARK------KSDDGKIRVLAISGDKSTPASILREQGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 186 IETLNK-DGIKTKQLALdtAMWDTAQAKDKTDAWLSG-PNADkieVVISNNDAMAMGAIEALKAHNK---KSIPVFGVDA 260
Cdd:cd06324 164 RDALAEhPDVTLLQIVY--ANWSEDEAYQKTEKLLQRyPDID---IVWAANDAMALGAIDALEEAGLkpgKDVLVGGIDW 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274735229 261 LPEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLaagkaatDGTDFKIENKIVRIPYVPVDKDNLSQFTK 331
Cdd:cd06324 239 SPEALQAVKDGELTASVGGHFLEGAWALVLLYDYH-------HGIDFAAGTSVQLKPMLAITRDNVAQYLK 302
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
28-264 |
1.56e-12 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 67.15 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 28 IGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLIAKGVKALaInLVDPAAAGVVISKAKAAD 107
Cdd:COG1609 64 IGVVVPDLSNPFFAELLRGIEEAARERG-YQLLLANSDEDPEREREALRLLLSRRVDGL-I-LAGSRLDDARLERLAEAG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 108 IPVVFFNKEPNAKALASydkayyVGTDSKESGVIQGQ-LIEKHWKaspqwdlnkdgviQYVLLKGEPGHPDAEARTKYVI 186
Cdd:COG1609 141 IPVVLIDRPLPDPGVPS------VGVDNRAGARLATEhLIELGHR-------------RIAFIGGPADSSSARERLAGYR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLNKDGIKTKQLALDTAMWDTAQAKDKTDAWLSGPnaDKIEVVISNNDAMAMGAIEALKAHNKKsIP----VFGVDALP 262
Cdd:COG1609 202 EALAEAGLPPDPELVVEGDFSAESGYEAARRLLARG--PRPTAIFCANDLMALGALRALREAGLR-VPedvsVVGFDDIP 278
|
..
gi 1274735229 263 EA 264
Cdd:COG1609 279 LA 280
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
28-264 |
3.18e-12 |
|
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: 65.62 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 28 IGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAgvVISKAKAAD 107
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAARERG-YSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDE--LLEELLAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 108 IPVVFFNKEPNakalasYDKAYYVGTDSKESGVIQGQ-LIEK-HWKaspqwdlnkdgvIqyVLLKGEPGHPDAEARTKYV 185
Cdd:cd06267 79 IPVVLIDRRLD------GLGVDSVVVDNYAGAYLATEhLIELgHRR------------I--AFIGGPLDLSTSRERLEGY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 186 IETLNKDGIKTKQLALDTAMWDTAQAKDKTDAWLSGPnaDKIEVVISNNDAMAMGAIEALKAHNKKsIP----VFGVDAL 261
Cdd:cd06267 139 RDALAEAGLPVDPELVVEGDFSEESGYEAARELLALP--PRPTAIFAANDLMAIGALRALRELGLR-VPedisVVGFDDI 215
|
...
gi 1274735229 262 PEA 264
Cdd:cd06267 216 PLA 218
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
1-328 |
8.87e-12 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 65.15 E-value: 8.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 1 MNKKVFTLTALVASMMLGAAAHAADTKIGVTIykyDDNFMSMVRKD--IEKDARETGGVALLMNDSQNDQSKQNDQVDVL 78
Cdd:PRK10355 1 MKIKNILLTLCASLLLTSVAAHAKEVKIGMAI---DDLRLERWQKDrdIFVKKAESLGAKVFVQSANGNEETQMSQIENM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 79 IAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNakalaSYDKAYYVGTDSKESGVIQGQ-LIEKhwkaSPQWD 157
Cdd:PRK10355 78 INRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMIN-----NADIDFYISFDNEKVGELQAKaLVDK----VPQGN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 158 lnkdgviqYVLLKGEPGHPDAEARTKYVIETLnKDGIKTKQLALDTAMWdtaqakdkTDAWLS-----------GPNADK 226
Cdd:PRK10355 149 --------YFLMGGSPVDNNAKLFRAGQMKVL-KPYIDSGKIKVVGDQW--------VDGWLPenalkimenalTANNNK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 227 IEVVISNNDAMAMGAIEALKAHN-KKSIPVFGVDALPEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKaaTDGT 305
Cdd:PRK10355 212 IDAVVASNDATAGGAIQALSAQGlSGKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGE--EPKA 289
|
330 340
....*....|....*....|....*...
gi 1274735229 306 DFKIENKIVRIPY-----VPVDKDNLSQ 328
Cdd:PRK10355 290 NTTLNNGLKDVPSrlltpIDVNKNNIDS 317
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
27-299 |
6.20e-11 |
|
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 61.97 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd19969 1 YYVMVTFKSGHPYWDDVKEGFEDAGAELGVKTEYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKE-PNAKALAsydkayYVGTDSKESGVIQGQ-LIEKhwkaspqwdLNKDGVIQYVLLKGEPGHpdaEARTKY 184
Cdd:cd19969 81 GIPVVTFDSDaPESKRIS------YVGTDNYEAGYAAAEkLAEL---------LGGKGKVAVLTGPGQPNH---EERVEG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 185 VIETL-NKDGIKTKQLALDTAmwDTAQAKDKTDAWLSG-PNADKIEVVISNNdamAMGAIEALKAHNKKS-IPVFGVDAL 261
Cdd:cd19969 143 FKEAFaEYPGIEVVAVGDDND--DPEKAAQNTSALLQAhPDLVGIFGVDASG---GVGAAQAVREAGKTGkVKIVAFDDD 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 1274735229 262 PEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGK 299
Cdd:cd19969 218 PETLDLIKDGVIDASIAQRPWMMGYWSLQFLYDLANGL 255
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
27-280 |
7.72e-11 |
|
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: 61.54 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGGvALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGG-TVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKEPNAKAL---ASYDKAyyVGTDSkesgviQGQLIEkhwkaspqwDLNKDGVIQYVLLKGEPghPDAEARTK 183
Cdd:cd06305 80 GIPVVTFDTDSQVPGVnniTQDDYA--LGTLS------LGQLVK---------DLNGEGNIAVFNVFGVP--PLDKRYDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 184 YVIETLNKDGIKTKQLALDTAMWDTAQ-AKDKTDAWLSGPNADKIEVVISNNDAMAMGAIEALKAHNKKSIPVFGVDALP 262
Cdd:cd06305 141 YKAVLKANPGIKKIVAELGDVTPNTAAdAQTQVEALLKKYPEGGIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISN 220
|
250 260
....*....|....*....|
gi 1274735229 263 EALAQIKA--GNMAGTVLND 280
Cdd:cd06305 221 QDLELMADegSPWVATAAQD 240
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
27-272 |
1.01e-10 |
|
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: 61.23 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGGVALLMNDSQNDQsKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAA 106
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNAN-EQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 107 DIPVVFFNKEPNAkalASYDkaYYVGTDSKESGVIQGQLIEKHwkaspqwdLNKDGVIqyVLLKGEPGHPDAEARTKYVI 186
Cdd:cd06311 80 GIPVVNFDRGLNV---LIYD--LYVAGDNPGMGVVSAEYIGKK--------LGGKGNV--VVLEVPSSGSVNEERVAGFK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLnKDGIKTKQLALDTAMWDTAQA-KDKTDAWLSGPnadKIEVVISNNDAMAMGAIEALKAHNKKSIPVF-GVDALPEA 264
Cdd:cd06311 145 EVI-KGNPGIKILAMQAGDWTREDGlKVAQDILTKNK---KIDAVWAADDDMAIGVLQAIKEAGRTDIKVMtGGGGSQEY 220
|
....*...
gi 1274735229 265 LAQIKAGN 272
Cdd:cd06311 221 FKRIMDGD 228
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
27-281 |
3.70e-10 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 59.55 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGgVALLMN--DSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAK 104
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELG-VEIYWRgpSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 105 AADIPVVFFNkepnaKALASYDKAYYVGTDSKESGVIQGQLIEKhwkaspqwDLNKDGVIqyVLLKGEPGHPDAEARTKY 184
Cdd:cd20004 80 AQGIPVVIID-----SDLGGDAVISFVATDNYAAGRLAAKRMAK--------LLNGKGKV--ALLRLAKGSASTTDRERG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 185 VIETLNKDGIKTKQLALDTAMWDTAQAKDKTDAWLSgpNADKIEVVISNNDAMAMGAIEALKAHNK-KSIPVFGVDALPE 263
Cdd:cd20004 145 FLEALKKLAPGLKVVDDQYAGGTVGEARSSAENLLN--QYPDVDGIFTPNESTTIGALRALRRLGLaGKVKFIGFDASDL 222
|
250
....*....|....*...
gi 1274735229 264 ALAQIKAGNMAGTVLNDA 281
Cdd:cd20004 223 LLDALRAGEISALVVQDP 240
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
64-328 |
4.86e-10 |
|
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: 59.61 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 64 SQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEpnakalASYDKAYYVGTDSKESGVIQG 143
Cdd:cd19998 41 SGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNV------VDEPCAYNVNTDQAKAGEQTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 144 QLIEKHwkaspqwdLNKDGVIqyVLLKGEPGHPDAEARTKYVIETLNK-DGIKTkqLALDTAMWDTAQAKDKTDAWLsgP 222
Cdd:cd19998 115 QWLVDK--------LGGKGNI--LMVRGVPGTSVDRDRYEGAKEVFKKyPDIKV--VAEYYGNWDDGTAQKAVADAL--A 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 223 NADKIEVVISnNDAMAmGAIEALKAHNKKSIPV--FGVDALPEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAGKA 300
Cdd:cd19998 181 AHPDVDGVWT-QGGET-GVIKALQAAGHPLVPVggEAENGFRKAMLEPLANGLPGISAGSPPALSAVALKLAVAVLEGEK 258
|
250 260
....*....|....*....|....*...
gi 1274735229 301 ATDgtdfkieNKIVRIPYVPVDKDNLSQ 328
Cdd:cd19998 259 EPK-------TIELPLPWVTTDDVKLCQ 279
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
66-271 |
1.96e-09 |
|
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: 57.59 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 66 NDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAKALASydkayYVGTDSKESGVIQGQL 145
Cdd:cd06306 41 TNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNGIDSPKVAA-----RVLVDFYDMGYLAGEY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 146 IEKHwkaspqwdlNKDGVIQYVLLKGEPGHPDAEARTKYVIETLNKDGIKTkqlaLDTAMWDT---AQAKDKTDAWLSGP 222
Cdd:cd06306 116 LVEH---------HPGKPVKVAWFPGPAGAGWAEDREKGFKEALAGSNVEI----VATKYGDTgkaVQLNLVEDALQAHP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1274735229 223 NADkievVISNNDAMAMGAIEALK-AHNKKSIPVFGVDALPEALAQIKAG 271
Cdd:cd06306 183 DID----YIVGNAVAAEAAVGALReAGLTGKVKVVSTYLTPGVYRGIKRG 228
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
37-300 |
5.04e-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: 380662 [Multi-domain] Cd Length: 271 Bit Score: 56.09 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 37 DNFMSMVRKDIEKDAREtGGVALLMN-DSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNK 115
Cdd:cd20007 11 DPFYITMQCGAEAAAKE-LGVELDVQgPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 116 EPNAKALAsydkAYYVGTDSKESGVIQG-QLIEKhwkaspqwdLNKDGVIqyVLLKGEPGHPDAEARTKYVIETLNKDGi 194
Cdd:cd20007 90 TLGDPSFV----LSQIASDNVAGGALAAeALAEL---------IGGKGKV--LVINSTPGVSTTDARVKGFAEEMKKYP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 195 KTKQLALDTAMWDTAQAKDKTDAWLSGPnaDKIEVVISNNDAMAMGAIEALKAHNKK-SIPVFGVDALPEALAQIKAGNM 273
Cdd:cd20007 154 GIKVLGVQYSENDPAKAASIVAAALQAN--PDLAGIFGTNTFSAEGAAAALRNAGKTgKVKVVGFDASPAQVEQLKAGTI 231
|
250 260
....*....|....*....|....*..
gi 1274735229 274 AGTVLNDAENQAKATLLMAKNLAAGKA 300
Cdd:cd20007 232 DALIAQKPAEIGYLAVEQAVAALTGKP 258
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
63-324 |
7.10e-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: 55.71 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 63 DSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAKALASydkayYVGTDSKESGVIQ 142
Cdd:cd20005 38 DTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGVPSDLPLA-----TVATDNYAAGALA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 143 G----QLIekhwkaspqwdlnkDGVIQYVLLKGEPGHPDAEARTKYVIETLNKDGIKTKQLALDTAMWDTAQAKDKTDAW 218
Cdd:cd20005 113 AdhlaELI--------------GGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDIKVVNVQYGVGDHAKAADIAKAI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 219 LSGpNADkIEVVISNNDAMAMGAIEALKAHNK-KSIPVFGVDALPEALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAA 297
Cdd:cd20005 179 LQA-NPD-LKGIYATNEGAAIGVANALKEMGKlGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAAVKALK 256
|
250 260
....*....|....*....|....*..
gi 1274735229 298 GKAATdgtdfkienKIVRIPYVPVDKD 324
Cdd:cd20005 257 GEEVE---------KLIDTGAKWYDKD 274
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
49-325 |
1.06e-08 |
|
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: 55.71 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 49 KDARETGGVALLMN-DSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAKAlasydK 127
Cdd:cd06302 22 KKAAKELGVEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSDAPPSA-----R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 128 AYYV-GTDSKESGVIQGQLIEKhwkaspqwdlNKDGVIQYVLLKGEPGHPDAEARTKYVIETLNKDGIKTKqlALDTAMW 206
Cdd:cd06302 97 DYFVnQADDEGLGEALVDSLAK----------EIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKYPDIE--LVDTYYT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 207 DTAQAKDKT---DAWLSGPNADKIEVVISNNDAMAMGAIEALKAHNKksIPVFGVdALPEALAQ-IKAGNMAGTVLNDAE 282
Cdd:cd06302 165 DDDQQKAYTqaqNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGK--VAVTGI-GLPNTARPyLKDGSVKEGVLWDPA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1274735229 283 NQAKATLLMAKNLAAGKAATDGTD---------FKIENKIVRI-PYVPVDKDN 325
Cdd:cd06302 242 KLGYLTVYAAYQLLKGKGFTEDSDdvgtggkvkVDVAGGEILLgPPLVFTKDN 294
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
39-254 |
3.36e-08 |
|
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: 53.68 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 39 FMSMVRKDIEKDARETGGVALLMNdSQNDQSKQNDQVDVLIAKGVKALAInlvdpAAAGVVISKAKAADIPVVFFNKEPN 118
Cdd:cd06291 13 FFAELAKYIEKELFKKGYKMILCN-SNEDEEKEKEYLEMLKRNKVDGIIL-----GSHSLDIEEYKKLNIPIVSIDRYLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 119 akalasyDKAYYVGTDSKESGVIQGQ-LIEKhwkaspqwdlnkdGVIQYVLLKGEPGHPDAEARTKYVIETLNKDGIKTK 197
Cdd:cd06291 87 -------EGIPSVSSDNYQGGRLAAEhLIEK-------------GCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1274735229 198 QLALDTAMWDTAQAKDKTDAWLS-GPNADKIevvISNNDAMAMGAIEALKAHNKKsIP 254
Cdd:cd06291 147 IIEIDENDFSEEDAYELAKELLEkYPDIDGI---FASNDLLAIGVLKALQKLGIR-VP 200
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
63-278 |
1.38e-07 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 51.83 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 63 DSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAKALASydkayYVGTDSKESGVIQ 142
Cdd:cd20006 40 ESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSPVNSKKADS-----FVATDNYEAGKKA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 143 GQLIEKHWKASPqwdlnKDGVIQYVllkgePGHPDAEARTKYVIETLNKDG---IKTKQLALDtamwDTAQAKDKTDAWL 219
Cdd:cd20006 115 GEKLASLLGEKG-----KVAIVSFV-----KGSSTAIEREEGFKQALAEYPnikIVETEYCDS----DEEKAYEITKELL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 220 SgpNADKIEVVISNNDAMAMGAIEALKA-HNKKSIPVFGVDALPEALAQIKAGNMAGTVL 278
Cdd:cd20006 181 S--KYPDINGIVALNEQSTLGAARALKElGLGGKVKVVGFDSSVEEIQLLEEGIIDALVV 238
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
27-276 |
2.84e-07 |
|
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).
Pssm-ID: 395423 [Multi-domain] Cd Length: 281 Bit Score: 50.97 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVtIYKYDDN--FMSMVrKDIEKDARETGGVALLMNDSQNDQSKQNdQVDVLIAKGVKALAINLVDPAAAGVViSKAK 104
Cdd:pfam00532 3 KLGA-LVPQLDEpfFQDLV-KGITKAAKDHGFDVFLLAVGDGEDTLTN-AIDLLLASGADGIIITTPAPSGDDIT-AKAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 105 AADIPVVFFNKEP-NAKALASYdkayyvGTDSKESGVIQGQliekhwkaspqwDLNKDGVIQYVLLKGEP-GHPDAEART 182
Cdd:pfam00532 79 GYGIPVIAADDAFdNPDGVPCV------MPDDTQAGYESTQ------------YLIAEGHKRPIAVMAGPaSALTARERV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 183 KYVIETLNKDGIKTKQLALDTAMWDTAQAKDKTDAWL-SGPNadkIEVVISNNDAMAMGAIEALKAHNKKSIP------- 254
Cdd:pfam00532 141 QGFMAALAAAGREVKIYHVATGDNDIPDAALAANAMLvSHPT---IDAIVAMNDEAAMGAVRALLKQGRVKIPdivgigi 217
|
250 260
....*....|....*....|....
gi 1274735229 255 --VFGVDALPEALAQIKAGNMAGT 276
Cdd:pfam00532 218 nsVVGFDGLSKAQDTGLYLSPLTV 241
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
63-328 |
6.51e-07 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380539 [Multi-domain] Cd Length: 294 Bit Score: 49.93 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 63 DSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAkALASYDKAYYVGTDSKESGVIQ 142
Cdd:cd06316 37 DANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKLVFMDNVPDG-LEAGKDYVSVVSSDNRGNGQIA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 143 GQLIEKHWKASpqwdlNKDGVIQYvllkGEPGHPDAEaRTKYVIETL--NKDGIKTKQLALDTamwDTAQAKDKTDAWLS 220
Cdd:cd06316 116 AELLAEAIGGK-----GKVGIIYH----DADFYATNQ-RDKAFKDTLkeKYPDIKIVAEQGFA---DPNDAEEVASAMLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 221 G-PNADKIEVVIsnnDAMAMGAIEALKAHNKKSIPVFGVDALPE-ALAQIKAGNMAGTVLNDAENQAKATLLMAKNLAAG 298
Cdd:cd06316 183 AnPDIDGIYVSW---DTPALGVISALRAAGRSDIKITTVDLGTEiALDMAKGGNVKGIGAQRPYDQGVAEALAAALALLG 259
|
250 260 270
....*....|....*....|....*....|
gi 1274735229 299 KAATdgtdfkienKIVRIPYVPVDKDNLSQ 328
Cdd:cd06316 260 KEVP---------PFIGVPPLAVTKDNLLE 280
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
45-259 |
1.33e-06 |
|
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: 49.08 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 45 KDIEKDARETGgVALLMNDSQNDQSKQNDQVDVLIAKGVKALAinLVDPAAAGVVISkAKAADIPVVFFNkepnakALAS 124
Cdd:cd06288 20 RGAQDAAEEHG-YLLLLANTGGDPELEAEAIRELLSRRVDGII--YASMHHREVTLP-PELTDIPLVLLN------CFDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 125 YDKAYYVGTDSKESGVIQGQ-LIEKHWKaspqwdlnKDGVIQyvllkGEPGHPDAEARTKYVIETLNKDGIKTKQLALDT 203
Cdd:cd06288 90 DPSLPSVVPDDEQGGYLATRhLIEAGHR--------RIAFIG-----GPEDSLATRLRLAGYRAALAEAGIPYDPSLVVH 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 204 AMWDTAQAKDKTDAWLSGPnaDKIEVVISNNDAMAMGAIEALKAHNKKsIP----VFGVD 259
Cdd:cd06288 157 GDWGRESGYEAAKRLLSAP--DRPTAIFCGNDRMAMGVYQAAAELGLR-VPedlsVVGFD 213
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
49-311 |
2.43e-06 |
|
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380482 [Multi-domain] Cd Length: 294 Bit Score: 48.44 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 49 KDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVV-----FFNKEPNakala 123
Cdd:cd01540 22 KKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAGIPVIavddqLVDADPM----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 124 syDKAYYVGTDSKESGVIQGQLIEKHWKASPQWDLNKDGVI----QYVllkgepghPDAEARTKYVIETLNKDGIKTKQl 199
Cdd:cd01540 97 --KIVPFVGIDAYKIGEAVGEWLAKEMKKRGWDDVKEVGVLaitmDTL--------SVCVDRTDGAKDALKAAGFPEDQ- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 200 aldtaMWDTAQAKDKTDAWLSGPNAD-------KIEVVISNNDAMAMGAIEALKAHNKKSIPVFGV-----DALPEALAQ 267
Cdd:cd01540 166 -----IFQAPYKGTDTEGAFNAANAVitahpevKHWLVVGCNDEGVLGAVRALEQAGFDAEDIIGVgiggyLAADEEFKK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1274735229 268 IKAGNMAGTVLNDAENQAKATLLMAKNLAAGKA-----ATDGTDFKIEN 311
Cdd:cd01540 241 QPTGFKASLYISPDKHGYIAAEELYNWITDGKPppaetLTDGVIVTRDN 289
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
39-264 |
3.04e-06 |
|
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: 47.95 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 39 FMSMVRKDIEKDARETGGVALLMNdSQNDQSKQNDQVDVLIAKGVKALAINlvdPAAA--GVVISKAKAADIPVVFFNKE 116
Cdd:cd06289 13 FFAELLAGIEEALEEAGYLVFLAN-TGEDPERQRRFLRRMLEQGVDGLILS---PAAGttAELLRRLKAWGIPVVLALRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 117 PnakALASYDkayYVGTDSKESGviqgQLIEKHwkaspqwdLNKDGVIQYVLLKGEPGHPDAEARTKYVIETLNKDGIKt 196
Cdd:cd06289 89 V---PGSDLD---YVGIDNRLGA----QLATEH--------LIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLP- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274735229 197 kqlaLDTAMW-----DTAQAKDKTDAWLSgpNADKIEVVISNNDAMAMGAIEALKAHNKKS---IPVFGVDALPEA 264
Cdd:cd06289 150 ----LDESLIvpgpaTREAGAEAARELLD--AAPPPTAVVCFNDLVALGAMLALRRRGLEPgrdIAVVGFDDVPEA 219
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
27-280 |
6.37e-06 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 46.84 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSMVRKDIEKDARETGGVALLMN-DSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKa 105
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGpATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 106 ADIPVVFFNKEPNAKAlasYDKAYyvGTDSKESGVIQGQLIEKHWKASPqwdlNKDGVIqyVLLKGEPGHPDAEARTKYV 185
Cdd:cd20008 80 AGIPVVLVDSGANTDD---YDAFL--ATDNVAAGALAADELAELLKASG----GGKGKV--AIISFQAGSQTLVDREEGF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 186 IETL--NKDGIKTkqlaLDTAMW--DTAQAKDKT-DAWLSGPNADKIevvISNNDAMAMGAIEALKAHNK-KSIPVFGVD 259
Cdd:cd20008 149 RDYIkeKYPDIEI----VDVQYSdgDIAKALNQTtDLLTANPDLVGI---FGANNPSAVGVAQALAEAGKaGKIVLVGFD 221
|
250 260
....*....|....*....|.
gi 1274735229 260 ALPEALAQIKAGNMAGTVLND 280
Cdd:cd20008 222 SSPDEVALLKSGVIKALVVQD 242
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
28-264 |
5.01e-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: 380508 [Multi-domain] Cd Length: 269 Bit Score: 44.14 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 28 IGVTIYKYDDNFMSMVRKDIEKDARETGGVALLMNDSQNDqSKQNDQVDVLIAKGVKALAInlVDPAAAGVVISKAKAAD 107
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDP-ERELAALDSLLSRRVDGLII--TPARDDAPDLQELAARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 108 IPVVFFNKEPNAKALASydkayyVGTDSKESGVIQGQ-LIEKhwkaspqwdlnkdGVIQYVLLKGEPGHPDAEARTKYVI 186
Cdd:cd06285 79 VPVVLVDRRIGDTALPS------VTVDNELGGRLATRhLLEL-------------GHRRIAVVAGPLNASTGRDRLRGYR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 187 ETLNKDGIKTKQLALDTAMWDTAQAKDKTDAWLSGPnaDKIEVVISNNDAMAMGAIEALKAHN---KKSIPVFGVDALPE 263
Cdd:cd06285 140 RALAEAGLPVPDERIVPGGFTIEAGREAAYRLLSRP--ERPTAVFAANDLMAIGVLRAARDLGlrvPEDLSVVGFDDIPL 217
|
.
gi 1274735229 264 A 264
Cdd:cd06285 218 A 218
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
39-111 |
2.77e-04 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to 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: 380656 Cd Length: 296 Bit Score: 41.88 E-value: 2.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274735229 39 FMSMvRKDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVV 111
Cdd:cd20001 14 FDRM-ETGVEQFAKDTGVNVYQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDAGIVVI 85
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
52-264 |
4.93e-04 |
|
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: 40.98 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 52 RETGGVALLMNDSQNDQskQNDQVDVLIAKGVKALAINLVDPAAAgvVISKAKAADIPVVFFNKEPNAKALASydkayyV 131
Cdd:cd06278 26 QARGLRPLLFNVDDEDD--VDDALRQLLQYRVDGVIVTSATLSSE--LAEECARRGIPVVLFNRVVEDPGVDS------V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 132 GTDSKESGVIQGQLIEKHwkaspqwdlnkdGVIQYVLLKGEPGHPDAEARTKYVIETLNKDGIKTkqLALDTAMWDTAQA 211
Cdd:cd06278 96 SCDNRAGGRLAADLLLAA------------GHRRIAFLGGPEGTSTSRERERGFRAALAELGLPP--PAVEAGDYSYEGG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1274735229 212 KDKTDAWLSGPnaDKIEVVISNNDAMAMGAIEALKAHNKKSIP----VFGVDALPEA 264
Cdd:cd06278 162 YEAARRLLAAP--DRPDAIFCANDLMALGALDAARQEGGLVVPedisVVGFDDIPMA 216
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
32-121 |
5.02e-04 |
|
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. 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: 380655 Cd Length: 298 Bit Score: 41.09 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 32 IYKYDDN-FMSMVRKDIEKDARETGGVALLMNDSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPV 110
Cdd:cd20000 5 LPKSLGNpYFDAARDGAKEAAKELGGELIFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAAGIKV 84
|
90
....*....|.
gi 1274735229 111 VFFNKEPNAKA 121
Cdd:cd20000 85 VTFDSDVAPEA 95
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
66-329 |
1.13e-03 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380652 [Multi-domain] Cd Length: 305 Bit Score: 40.35 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 66 NDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAADIPVVFFNKEPNAkalasyDKAYYVGTDSKESGviqgql 145
Cdd:cd19997 44 GSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGVTE------PCAYILNNDFEDYG------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 146 iekhwKASPQWDLNKDG----VIQYVLLKGEPghPDAEARTKYVIETLNKDGIKTkqLALDTAMWDTAQAKDKTDAWLsg 221
Cdd:cd19997 112 -----AASVEYVADRLGgkgnVLEVRGVAGTS--PDEEIYAGQVEALKKYPDLKV--VAEVYGNWTQSVAQKAVTGIL-- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 222 PNADKIEVVISNNDAmAMGAIEALKAHNKKsIPVFGVDALPEALAQIKAGNMA---GTV-LNDAENQAKATLLMAKNLAA 297
Cdd:cd19997 181 PSLPEVDAVITQGGD-GYGAAQAFEAAGRP-LPIIIGGNRGEFLKWWQEEYAKngyETVsVSTDPGQGSAAFWVALDILN 258
|
250 260 270
....*....|....*....|....*....|..
gi 1274735229 298 GKAATdgtdfkienKIVRIPYVPVDKDNLSQF 329
Cdd:cd19997 259 GKDVP---------KEMILPVVTITEDDLDAW 281
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
174-264 |
1.20e-03 |
|
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: 39.81 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 174 GHPDAEARTKYVIETLNKDGIKTKQLALDTAmWDTAQAKDKTDAWLSgpNADKIEVVISNNDAMAMGAIEALKAHNKKsI 253
Cdd:cd01544 129 GEEIEDPRLRAFREYMKEKGLYNEEYIYIGE-FSVESGYEAMKELLK--EGDLPTAFFVASDPMAIGALRALQEAGIK-V 204
|
90
....*....|....*
gi 1274735229 254 P----VFGVDALPEA 264
Cdd:cd01544 205 PedisIISFNDIEVA 219
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
27-303 |
1.32e-03 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 39.89 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 27 KIGVTIYKYDDNFMSmVRKDIEKDARETGGVALLMNDSQNDQSKQNDqvDVLIAKGVKALAINLV----DPAAAGVVisk 102
Cdd:COG2984 4 KIGILQISEHPALDA-AREGFKDGLAEAGYGKNLKLDYQNAQGDQAT--AAQIAAKLVADKPDLIvaigTPAAQAAA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 103 AKAADIPVVFFnkepnakALASYDKAYYVGTDSKE----SGVIQGQLIEKHW----KASPqwDLNKDGVIqyvllkGEPG 174
Cdd:COG2984 78 NATKDIPVVFT-------AVTDPVGAGLVKSLEKPggnvTGVSDLLPIEKQLelikKLLP--DAKRIGVL------YNPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 175 HPDAEARTKYVIETLNKDGIKTKQLALDTamwdTAQAKDKTDAWlsgpnADKIEVVISNNDAMAMGAIEAL-KAHNKKSI 253
Cdd:COG2984 143 EANSVAQVEELKKAAKKLGLELVEATVTS----SNEIQQALQSL-----AGKVDAIYVPTDNTVVSALEAIaKVAARAKI 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1274735229 254 PVFGVDAlpealAQIKAGnMAGTVLNDAENQAKATLLMAKNLAAGKAATD 303
Cdd:COG2984 214 PVFGGDD-----SSVKAG-ALAGYGIDYYELGRQAAEMALRILKGEKPAD 257
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
32-276 |
1.60e-03 |
|
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: 39.76 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 32 IYKYDDN-FMSMVRKDIEKDARETGgvALLMN---DSQNDQSKQNDQVDVLIAKGVKALAINLVDPAAAGVVISKAKAAD 107
Cdd:cd19973 5 ITKTDTNpFFVKMKEGAQKAAKALG--IKLMTaagKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 108 IPVVFFNK--EPNAKALASYdkayyvGTDSKESGVIQGQLIEKHWKAspqwdlnKDGVIqyVLLKGEPGHPDAEAR---- 181
Cdd:cd19973 83 VLVIALDTptDPIDAADATF------ATDNFKAGVLIGEWAKAALGA-------KDAKI--ATLDLTPGHTVGVLRhqgf 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 182 -TKYVIETL----NKDGIKTKQLALDTAMWDTAQAKDKTDAWLSgpNADKIEVVISNNDAMAMGAIEALKAHNK-KSIPV 255
Cdd:cd19973 148 lKGFGIDEKdpesNEDEDDSQVVGSADTNGDQAKGQTAMENLLQ--KDPDINLVYTINEPAAAGAYQALKAAGKeKGVLI 225
|
250 260
....*....|....*....|.
gi 1274735229 256 FGVDALPEALAQIKAGNMAGT 276
Cdd:cd19973 226 VSVDGGCPGVKDVKDGIIGAT 246
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
171-264 |
4.06e-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: 38.39 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 171 GEPGHPDAEARTKYVIETLNKDGIKtkqlaldtamWDTAQAKDKTDAWLSGPNA--------DKIEVVISNNDAMAMGAI 242
Cdd:cd06295 131 GDPPHPEVADRLQGYRDALAEAGLE----------ADPSLLLSCDFTEESGYAAmralldsgTAFDAIFAASDLIAMGAI 200
|
90 100
....*....|....*....|....*.
gi 1274735229 243 EALKAHNkKSIP----VFGVDALPEA 264
Cdd:cd06295 201 RALRERG-ISVPgdvaVVGYDDIPLA 225
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
28-254 |
5.65e-03 |
|
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: 38.01 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 28 IGVTIYKYDDNFMSMVRKDIEKDARETGGVALLMNdSQNDQSKQNDQVDVLIAKGVKALAinLVDPAAAGVVISKAKAAD 107
Cdd:cd06280 2 IGLIVPDITNPFFTTIARGIEDAAEKHGYQVILAN-TDEDPEKEKRYLDSLLSKQVDGII--LAPSAGPSRELKRLLKHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274735229 108 IPVVFFNKEPNAKALasydkaYYVGTDSKESGVIQGQ-LIEkhwkaspqwdlnkDGVIQYVLLKGEPGHPDAEARTKYVI 186
Cdd:cd06280 79 IPIVLIDREVEGLEL------DLVAGDNREGAYKAVKhLIE-------------LGHRRIGLITGPLEISTTRERLAGYR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274735229 187 ETLNKDGIKTKQ---LALDTAMWDTAQAkdkTDAWLSGPnaDKIEVVISNNDAMAMGAIEALKaHNKKSIP 254
Cdd:cd06280 140 EALAEAGIPVDEsliFEGDSTIEGGYEA---VKALLDLP--PRPTAIFATNNLMAVGALRALR-ERGLEIP 204
|
|
| |
