|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15395 |
PRK15395 |
galactose/glucose ABC transporter substrate-binding protein MglB; |
242-551 |
0e+00 |
|
galactose/glucose ABC transporter substrate-binding protein MglB;
Pssm-ID: 185293 [Multi-domain] Cd Length: 330 Bit Score: 646.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 242 AAGITLGMdELYGSRDNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIE 321
Cdd:PRK15395 22 AADTRIGV-TIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAPTVIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 322 KARGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGWDLNKDGQIQFVLLKGEPGHPDAEAR 401
Cdd:PRK15395 101 KARGQDVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANPAWDLNKDGKIQYVLLKGEPGHPDAEAR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 402 TTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDAL 481
Cdd:PRK15395 181 TTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDAL 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 482 PEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKVVRVPYVGVDKDNLAEFSK 551
Cdd:PRK15395 261 PEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAEGTNWKIENKVVRVPYVGVDKDNLAEFTK 330
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
252-541 |
7.95e-152 |
|
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: 445.49 E-value: 7.95e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 252 LYGSRDNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVV 331
Cdd:cd01539 7 IYNYDDTFISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 332 FFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGWDLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELND 411
Cdd:cd01539 87 FFNREPSREDLKSYDKAYYVGTDAEESGIMQGEIIADYWKANPEIDKNGDGKIQYVMLKGEPGHQDAIARTKYSVKTLND 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 412 KGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNaNKIEVVIANNDAMAMGAVEALKAHN------KSSIPVFGVDALPEAL 485
Cdd:cd01539 167 AGIKTEQLAEDTANWDRAQAKDKMDAWLSKYG-DKIELVIANNDDMALGAIEALKAAGyntgdgDKYIPVFGVDATPEAL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 83699618 486 ALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGTN-WKIDNKVVRVPYVGV 541
Cdd:cd01539 246 EAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLETGYkFLVEGKYVRIPYKKV 302
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
253-540 |
7.99e-119 |
|
Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.
Pssm-ID: 380479 [Multi-domain] Cd Length: 265 Bit Score: 359.25 E-value: 7.99e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 253 YGSRDNFMSVVRKAIEQDAKAaPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGtVIEKARGQNVPVVF 332
Cdd:cd01537 7 YSYDDNFMSVIRKAIEQDAKQ-PGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAG-VAEKARGQNVPVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 333 FNKEPSRkaldsYDKAYYVGTDSKESGIIQGDLIAKHWaanqgwdlnkdgQIQFVLLKGEPGHPDAEARTTYVIKELNDK 412
Cdd:cd01537 85 FDKEPSR-----YDKAYYVITDSKEGGIIQGDLLAKHG------------HIQIVLLKGPLGHPDAEARLAGVIKELNDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 413 GIKTEQLQLDTAMWDTAQAKDKMDAWLSGPnaNKIEVVIANNDAMAMGAVEALKAHNK---SSIPVFGVDALPEALalvK 489
Cdd:cd01537 148 GIKTEQLQLDTGDWDTASGKDKMDQWLSGP--NKPTAVIANNDAMAMGAVEALKEHGLrvpSDISVFGYDALPEAL---K 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 83699618 490 SGALAGTVLNDANNQAKATFDLAKNLADgkgaadgtNWKIDNKVVRVPYVG 540
Cdd:cd01537 223 SGPLLTTILQDANNLGKTTFDLLLNLAD--------NWKIDNKVVRVPYVL 265
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
242-546 |
1.27e-62 |
|
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: 212.86 E-value: 1.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 242 AAGITLGMDeLYGSRDNFMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIE 321
Cdd:COG1879 31 AKGKTIGFV-VKTLGNPFFVAVRKGAEAAAKEL-GVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 322 KARGQNVPVVFFNKEPsrkalDSYDKAYYVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEAR 401
Cdd:COG1879 109 KAKAAGIPVVTVDSDV-----DGSDRVAYVGSDNYAAGRLAAEYLAKA--------LGGKGKV--AILTGSPGAPAANER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 402 TTYVIKELNDKGiKTEQLQLDTAMWDTAQAKDKMDAWLSgpnAN-KIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVD 479
Cdd:COG1879 174 TDGFKEALKEYP-GIKVVAEQYADWDREKALEVMEDLLQ---AHpDIDGIFAANDGMALGAAQALKAAGRKGdVKVVGFD 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83699618 480 ALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKgaadgtnwKIDnKVVRVPYVGVDKDNL 546
Cdd:COG1879 250 GSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGK--------EVP-KEILTPPVLVTKENV 307
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
257-519 |
1.99e-61 |
|
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: 207.93 E-value: 1.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 257 DNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKE 336
Cdd:pfam13407 10 NPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAGIPVVTFDSD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 337 psrkaLDSYDKAYYVGTDSKESGIIQGDLIAKHWaanqgwdlnkDGQIQFVLLKGEPGHPDAEARTTYVIKELNDK--GI 414
Cdd:pfam13407 90 -----APSSPRLAYVGFDNEAAGEAAGELLAEAL----------GGKGKVAILSGSPGDPNANERIDGFKKVLKEKypGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 415 KTEQLQlDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIP-VFGVDALPEALALVKSGAL 493
Cdd:pfam13407 155 KVVAEV-EGTNWDPEKAQQQMEALLTA-YPNPLDGIISPNDGMAGGAAQALEAAGLAGKVvVTGFDATPEALEAIKDGTI 232
|
250 260
....*....|....*....|....*.
gi 83699618 494 AGTVLNDANNQAKATFDLAKNLADGK 519
Cdd:pfam13407 233 DATVLQDPYGQGYAAVELAAALLKGK 258
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
252-519 |
7.81e-61 |
|
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: 206.26 E-value: 7.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 252 LYGSRDNFMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVV 331
Cdd:cd01536 6 VKDLTNPFWVAVKKGAEAAAKEL-GVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAGIPVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 332 FFNkepsRKALDSYDKAYYVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELND 411
Cdd:cd01536 85 AVD----TDIDGGGDVVAFVGTDNYEAGKLAGEYLAEA--------LGGKGKV--AILEGPPGSSTAIDRTKGFKEALKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 412 KGiKTEQLQLDTAMWDTAQAKDKMDAWLsgpNAN-KIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVK 489
Cdd:cd01536 151 YP-DIEIVAEQPANWDRAKALTVTENLL---QANpDIDAVFAANDDMALGAAEALKAAGRTGdIKIVGVDGTPEALKAIK 226
|
250 260 270
....*....|....*....|....*....|
gi 83699618 490 SGALAGTVLNDANNQAKATFDLAKNLADGK 519
Cdd:cd01536 227 DGELDATVAQDPYLQGYLAVEAAVKLLNGE 256
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
252-518 |
1.30e-57 |
|
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: 197.84 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 252 LYGSRDNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVV 331
Cdd:cd06301 7 MQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPLV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 332 FFNKEPSrkalDSYDKAYYVGTDSKESGIIQGDLIAKhwaanqgwdlNKDGQIQFVLLKGEPGHPDAEARTTYVIKELND 411
Cdd:cd06301 87 YVNREPD----SKPKGVAFVGSDDIESGELQMEYLAK----------LLGGKGNIAILDGVLGHEAQILRTEGNKDVLAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 412 -KGIKTEQLQldTAMWDTAQAKDKMDAWL-SGPnanKIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEALALV 488
Cdd:cd06301 153 yPGMKIVAEQ--TANWSREKAMDIVENWLqSGD---KIDAIVANNDEMAIGAILALEAAGKKdDILVAGIDATPDALKAM 227
|
250 260 270
....*....|....*....|....*....|
gi 83699618 489 KSGALAGTVLNDANNQAKATFDLAKNLADG 518
Cdd:cd06301 228 KAGRLDATVFQDAAGQGETAVDVAVKAAKG 257
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
253-549 |
1.37e-47 |
|
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380536 [Multi-domain] Cd Length: 277 Bit Score: 170.14 E-value: 1.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 253 YGSRDNFMSVVRKAIEQDAKAaPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVF 332
Cdd:cd06313 7 YGLSSEFITNLVEAMKAVAKE-LNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAGIPLVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 333 FNKepsrkALDSYDKAYYVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELNDK 412
Cdd:cd06313 86 VNA-----LIENEDLTAYVGSDDVVAGELEGQAVADR--------LGGKGNV--VILEGPIGQSAQIDRGKGIENVLKKY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 413 -GIKTeqLQLDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSG 491
Cdd:cd06313 151 pDIKV--LAEQTANWSRDEAMSLMENWLQA-YGDEIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDALQAVKSG 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 83699618 492 ALAGTVLNDANNQAKATFDLAKNLADGKGAadgtnwkidNKVVRVPYVGVDKDNLAEF 549
Cdd:cd06313 228 ELIATVLQDAEAQGKGAVEVAVDAVKGEGV---------EKKYYIPFVLVTKDNVDDY 276
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
264-539 |
6.76e-43 |
|
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: 157.36 E-value: 6.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 264 RKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALD 343
Cdd:cd19992 18 KEYMEEEAKEL-GVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDRLILNADVD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 344 sydkaYYVGTDSKESGIIQGDLIAKhwAANQGwdlnkdgqiQFVLLKGEPGHPDAEA-RTTY--VIKELNDKG-IK--TE 417
Cdd:cd19992 97 -----LYVGRDNYKVGQLQAEYALE--AVPKG---------NYVILSGDPGDNNAQLiTAGAmdVLQPAIDSGdIKivLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 418 QLqldTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAGT 496
Cdd:cd19992 161 QY---VKGWSPDEAMKLVENALTA-NNNNIDAVLAPNDGMAGGAIQALKAQGlAGKVFVTGQDAELAALKRIVEGTQTMT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 83699618 497 VLNDANNQAKATFDLAKNLADGKgAADGTNWKIDNKVVRVPYV 539
Cdd:cd19992 237 VWKDLKELARAAADAAVKLAKGE-KPQTTDETINNGGKDVPAI 278
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
264-548 |
7.03e-39 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 146.82 E-value: 7.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 264 RKAIEQDAKAA---PDVQllmnDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVffnkepsrk 340
Cdd:COG4213 21 GDNFKAALKELgyeVDVQ----NANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVI--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 341 aldSYDK-------AYYVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIQFVLLKGEPGhpDAEARTTY-----VIKE 408
Cdd:COG4213 88 ---AYDRlilnsdvDYYVSFDNVKVGELQGQYLVDG--------LPLKGKGNIELFGGSPT--DNNATLFFegamsVLQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 409 LNDKG---IKTEQlqlDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVF-GVDALPEA 484
Cdd:COG4213 155 YIDSGklvVVSGQ---WTLGWDPETAQKRMENLLTA-NGNKVDAVLAPNDGLAGGIIQALKAQGLAGKVVVtGQDAELAA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83699618 485 LALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAAdgTNWKIDNKVVRVPY-----VGVDKDNLAE 548
Cdd:COG4213 231 VQRILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPE--VNGTYDNGKKDVPSyllepVAVTKDNVKE 297
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
263-519 |
6.04e-34 |
|
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: 131.13 E-value: 6.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 263 VRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFnkepSRKaL 342
Cdd:cd06308 17 MNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVL----DRK-V 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 343 DSYDKAYYVGTDSKESGIIQGDLIAKhwaanqgwDLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELND-KGIKteQLQL 421
Cdd:cd06308 92 SGDDYTAFIGADNVEIGRQAGEYIAE--------LLNGKGNV--VEIQGLPGSSPAIDRHKGFLEAIAKyPGIK--IVAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 422 DTAMWDTAQAKDKMDAWLS-GPnanKIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDALPEAL-ALVKSGALAGTVL 498
Cdd:cd06308 160 QDGDWLRDKAIKVMEDLLQaHP---DIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGLPEAGeKAVKDGILAATFL 236
|
250 260
....*....|....*....|.
gi 83699618 499 NDANnqAKATFDLAKNLADGK 519
Cdd:cd06308 237 YPTG--GKEAIEAALKILNGE 255
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
269-537 |
4.52e-32 |
|
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: 126.98 E-value: 4.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 269 QDAKAAPDVQLlmndSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVffnkepsrkaldSYDK- 347
Cdd:cd19994 26 EEAGYTVDLQY----ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVI------------AYDRl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 348 -------AYYVGTDSKESGIIQGDLIAKHWAANqgwdlNKDGQIQFVLLKGEPGhpDAEARTTY-----VIKELNDKGI- 414
Cdd:cd19994 90 imntdavDYYVTFDNEKVGELQGQYLVDKLGLK-----DGKGPFNIELFAGSPD--DNNAQLFFkgameVLQPYIDDGTl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 415 -----KTEQLQLDTAMWDTAQAKDKMDAWLSGPNA--NKIEVVIANNDAMAMGAVEALKAHNKSSIP---VFGVDALPEA 484
Cdd:cd19994 163 vvrsgQTTFEQVATPDWDTETAQARMETLLSAYYTggKKLDAVLSPNDGIARGVIEALKAAGYDTGPwpvVTGQDAEDAS 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 83699618 485 LALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKVVRVP 537
Cdd:cd19994 243 VKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVEVNDTKTYDNGVKVVP 295
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
254-548 |
2.24e-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: 124.25 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 254 GSRDNFMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFF 333
Cdd:cd06309 8 GSESPWRVANTKSIKEAAKKR-GYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 334 NkepsrKALDSYDKAYY---VGTDSKESGIIQGDLIAKHWAanqgwdlNKDGQIqfVLLKGEPGHPDAEARTT---YVIK 407
Cdd:cd06309 87 D-----RTIDGEDGSLYvtfIGSDFVEEGRRAAEWLVKNYK-------GGKGNV--VELQGTAGSSVAIDRSKgfrEVIK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 408 ELNDKGIKTEQlqldTAMWDTAQAKDKMDAWL-SGPnaNKIEVVIANNDAMAMGAVEALKAHNKS---SIPVFGVDALPE 483
Cdd:cd06309 153 KHPNIKIVASQ----SGNFTREKGQKVMENLLqAGP--GDIDVIYAHNDDMALGAIQALKEAGLKpgkDVLVVGIDGQKD 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83699618 484 ALALVKSGALAGTVLNDAnNQAKATFDLAKNLADGKgaadgtnwKIDnKVVRVPYVGVDKDNLAE 548
Cdd:cd06309 227 ALEAIKAGELNATVECNP-LFGPTAFDTIAKLLAGE--------KVP-KLIIVEERLFDKDNAAE 281
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
266-518 |
3.89e-31 |
|
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: 123.67 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 266 AIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNkepsRKALDSY 345
Cdd:cd06318 20 AAKAEAKKL-GVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGIPVITVD----SALDPSA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 346 DKAYYVGTDSKESGIIQGdliakHWAAnqgwDLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKT------EQL 419
Cdd:cd06318 95 NVATQVGRDNKQNGVLVG-----KEAA----KALGGDPGKIIELSGDKGNEVSRDRRDGFLAGVNEYQLRKygksniKVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 420 QLDTAMWDTAQAKDKMDAWLSgpnANK-IEVVIANNDAMAMGAVEALKAHNKSSI-PVFGVDALPEALALVKSGALAGTV 497
Cdd:cd06318 166 AQPYGNWIRSGAVAAMEDLLQ---AHPdINVVYAENDDMALGAMKALKAAGMLDKvKVAGADGQKEALKLIKDGKYVATG 242
|
250 260
....*....|....*....|.
gi 83699618 498 LNDANNQAKATFDLAKNLADG 518
Cdd:cd06318 243 LNDPDLLGKTAVDTAAKVVKG 263
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
259-497 |
4.40e-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: 122.79 E-value: 4.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNkeps 338
Cdd:cd06323 13 FFVSLKDGAQAEAKEL-GVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVD---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 339 RKALDSyDKAYYVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEARTTYvIKELNDKGIKTEQ 418
Cdd:cd06323 88 RSVTGG-KVVSHIASDNVAGGEMAAEYIAKK--------LGGKGKV--VELQGIPGTSAARERGKG-FHNAIAKYPKINV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 419 LQLDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTV 497
Cdd:cd06323 156 VASQTADFDRTKGLNVMENLLqAHPD---IDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVKAVKDGKLAATV 232
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
259-530 |
9.11e-30 |
|
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: 119.03 E-value: 9.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNkeps 338
Cdd:cd19968 13 FFVYMHEQAVDEAAKL-GVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAGIPVVTVD---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 339 RKAlDSYDKAYYVGTDSKESGIIQGDLIAKhwaanqgwDLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELnDKGIKTEQ 418
Cdd:cd19968 88 RRA-EGAAPVPHVGADNVAGGREVAKFVVD--------KLPNGAKV--IELTGTPGSSPAIDRTKGFHEEL-AAGPKIKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 419 LQLDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAH--NKSSIPVFGVDALPEALALVKSGALAGT 496
Cdd:cd19968 156 VFEQTGNFERDEGLTVMENILTS-LPGPPDAIICANDDMALGAIEAMRAAglDLKKVKVIGFDAVPDALQAIKDGELYAT 234
|
250 260 270
....*....|....*....|....*....|....
gi 83699618 497 VLNDANNQAKATFDLAKNLADGKGAADGTNWKID 530
Cdd:cd19968 235 VEQPPGGQARTALRILVDYLKDKKAPKKVNLKPK 268
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
272-539 |
2.49e-29 |
|
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: 118.54 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 272 KAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNkepsrKALDSYDKAYYV 351
Cdd:cd19995 28 KLCPDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYD-----RLILGGPADYYV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 352 GTDSKESGIIQGDLIAKHWAAnqgwDLNKDGQIqfVLLKGEPGHPDA---EARTTYVIKELNDKGIKTEQLQLDTAMWDT 428
Cdd:cd19995 103 SFDNVAVGEAQAQSLVDHLKA----IGKKGVNI--VMINGSPTDNNAglfKKGAHEVLDPLGDSGELKLVCEYDTPDWDP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 429 AQAKDKMDAWLSgPNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKA 507
Cdd:cd19995 177 ANAQTAMEQALT-KLGNNIDGVLSANDGLAGGAIAALKAQGlAGKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAAA 255
|
250 260 270
....*....|....*....|....*....|...
gi 83699618 508 TFDLAKNLADGKG-AADGTNWKIDNKVVRVPYV 539
Cdd:cd19995 256 AAKVAVALLKGETpPSDLVTGTVTNGGDKVPAV 288
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
264-537 |
5.49e-29 |
|
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: 117.58 E-value: 5.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 264 RKAIEQDA-KAAPD---VQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVffnkepsr 339
Cdd:cd19993 13 RWKTDEAAmKKALEkagAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVI-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 340 kaldSYDK------AYYVGTDSKESGIIQGDLIAKhwAANQGwdlnkdgqiQFVLLKGEPGHPDAE---ARTTYVIKELN 410
Cdd:cd19993 85 ----AYDRlienpiAFYISFDNVEVGRMQARGVLK--AKPEG---------NYVFIKGSPTDPNADflrAGQMEVLQPAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 411 DKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVK 489
Cdd:cd19993 150 DSGKIKIVGEQYTDGWKPANAQKNMEQILTA-NNNKVDAVVASNDGTAGGAVAALAAQGlAGKVPVSGQDADKAALNRIA 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 83699618 490 SGALAGTVLNDANNQAKATFDLAKNLADGK---GAADGTNWKIDNKVVRVP 537
Cdd:cd19993 229 LGTQTVTVWKDARELGKEAAEIAVELAKGTkieAIKGAALTNDGPKKVAVP 279
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
259-547 |
1.65e-28 |
|
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: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAAP-DVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEP 337
Cdd:cd06320 13 FWVAMKDGIEAEAKKLGvKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKKGIPVINLDDAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 338 SRKALDSY--DKAYYVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEART---TYVIKElnDK 412
Cdd:cd06320 93 DADALKKAggKVTSFIGTDNVAAGALAAEYIAEK--------LPGGGKV--AIIEGLPGNAAAEARTkgfKETFKK--AP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 413 GIKTEQLQldTAMWDTAQAKDKMDAWLSG-PNANKIevvIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKS 490
Cdd:cd06320 161 GLKLVASQ--PADWDRTKALDAATAILQAhPDLKGI---YAANDTMALGAVEAVKAAGKTGkVLVVGTDGIPEAKKSIKA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 83699618 491 GALAGTVLNDANNQAKATFDLAKNLADGKgaadgtnwKIDNKVVrVPYVGVDKDNLA 547
Cdd:cd06320 236 GELTATVAQYPYLEGAMAVEAALRLLQGQ--------KVPAVVA-TPQALITKDNVD 283
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
253-546 |
6.03e-27 |
|
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: 111.30 E-value: 6.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 253 YGSRDNFMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVF 332
Cdd:cd06319 7 YDLDNPFWQIMERGVQAAAEEL-GYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIPVVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 333 fnkepSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANqGWdlnKDGQIqfVLLKGEPGHPDAEARTTYVIKELNDK 412
Cdd:cd06319 86 -----ADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKEN-GW---GGGSV--GIIAIPQSRVNGQARTAGFEDALEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 413 GIKTEQLQLdTAMWDTAQAKDKM-DAWLSGPnanKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKS 490
Cdd:cd06319 155 GVEEVALRQ-TPNSTVEETYSAAqDLLAANP---DIKGIFAQNDQMAQGALQAIEEAGRTGdILVVGFDGDPEALDLIKD 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 83699618 491 GALAGTVLNDANNQAKATFDLAKNLADGKGAADgtnwkidnKVVRVPYVGVDKDNL 546
Cdd:cd06319 231 GKLDGTVAQQPFGMGARAVELAIQALNGDNTVE--------KEIYLPVLLVTSENV 278
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
259-519 |
2.65e-26 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380626 [Multi-domain] Cd Length: 267 Bit Score: 108.83 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAAPDvQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPS 338
Cdd:cd19971 13 FFIAINDGIKKAVEANGD-ELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPVK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 339 -RKALDSydkayYVGTDSKESGIIQGDLIAKhwaanqgwDLNKDGQIqfVLLKgepgHPDAEA---RTT---YVIKelND 411
Cdd:cd19971 92 dTDLVDS-----TIASDNYNAGKLCGEDMVK--------KLPEGAKI--AVLD----HPTAEScvdRIDgflDAIK--KN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 412 KGIKTEQlQLDTAMwDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDALPEALALVK 489
Cdd:cd19971 151 PKFEVVA-QQDGKG-QLEVAMPIMEDILqAHPD---LDAVFALNDPSALGALAALKAAGKlGDILVYGVDGSPDAKAAIK 225
|
250 260 270
....*....|....*....|....*....|
gi 83699618 490 SGALAGTVLNDANNQAKATFDLAKNLADGK 519
Cdd:cd19971 226 DGKMTATAAQSPIEIGKKAVETAYKILNGE 255
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
262-537 |
1.09e-25 |
|
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: 107.51 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 262 VVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNkepsRKA 341
Cdd:cd01538 15 QTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYD----RLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 342 LDSyDKAYYVGTDSKESGIIQGDLIAKhwaanqgwdlnKDGQIQFVLLKGEPGHPDA---EARTTYVIKELNDKGIKTEQ 418
Cdd:cd01538 91 LNA-DVDYYISFDNEKVGELQAQALLD-----------AKPEGNYVLIGGSPTDNNAklfRDGQMKVLQPAIDSGKIKVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 419 LQLDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTV 497
Cdd:cd01538 159 GDQWVDDWLPANAQQIMENALTA-NGNNVDAVVASNDGTAGGAIAALKAQGLSGgVPVSGQDADLAAIKRILAGTQTMTV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 83699618 498 LNDANNQAKATFDLAKNLADGKGAadGTNWKIDNKVVRVP 537
Cdd:cd01538 238 YKDIRLLADAAAEVAVALMRGEKP--PINGTTNNGLKDVP 275
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
259-479 |
1.47e-24 |
|
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: 105.02 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAAPDV--QLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKE 336
Cdd:cd19996 13 WRVQMIAEFEAEAAKLKKLikELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 337 PsrkalDSYDKAYYVGTDSKESGIIQGDLIAKhwaanqgwDLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELND-KGIK 415
Cdd:cd19996 93 V-----GSDKYTAFVGVDDAAFGRVGAEWLVK--------QLGGKGNI--IALRGIAGVSVSEDRWAGAKEVFKEyPGIK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83699618 416 TeqLQLDTAMWDTAQAKDKMDAWLS-GPnanKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVD 479
Cdd:cd19996 158 I--VGEVYADWDYAKAKQAVESLLAaYP---DIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTGED 217
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
286-542 |
2.16e-24 |
|
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: 103.86 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 286 NDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNkepsRKALDSyDKAYYVGTDSKESGIIQGDL 365
Cdd:cd19991 39 GDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYD----RLILNA-DVDLYVSFDNEKVGELQAEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 366 IAKHwaanqgwdlnkDGQIQFVLLKGEPGHPDAE---ARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGp 442
Cdd:cd19991 114 LVKA-----------KPKGNYVLLGGSPTDNNAKlfrEGQMKVLQPLIDSGDIKVVGDQWVDDWDPEEALKIMENALTA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 443 NANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGA 521
Cdd:cd19991 182 NNNKIDAVIASNDGTAGGAIQALAEQGlAGKVAVSGQDADLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKN 261
|
250 260
....*....|....*....|.
gi 83699618 522 AdgTNWKIDNKVVRVPYVGVD 542
Cdd:cd19991 262 E--ANRTINNGKKEVPSILLD 280
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
259-519 |
1.72e-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: 95.04 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPS 338
Cdd:cd06322 13 FFVDIKDAMKKEAAEL-GVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFTVDVKAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 339 RKALDSydkayYVGTDSKESGIIQGDLIAKHWaanqgwdLNKDGQIQFVllkgepGHPDAEA---RT--------TY--- 404
Cdd:cd06322 92 GAKVVT-----HVGTDNYAGGKLAGEYALKAL-------LGGGGKIAII------DYPEVESvvlRVngfkeaikKYpni 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 405 -VIKELNDKGIKTEQLQldtAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALP 482
Cdd:cd06322 154 eIVAEQPGDGRREEALA---ATEDMLQANPDLDG------------IFAIGDPAALGALTAIESAGKEDkIKVIGFDGNP 218
|
250 260 270
....*....|....*....|....*....|....*...
gi 83699618 483 EAL-ALVKSGALAGTVLNDANNQAKATFDLAKNLADGK 519
Cdd:cd06322 219 EAIkAIAKGGKIKADIAQQPDKIGQETVEAIVKYLAGE 256
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
255-522 |
5.01e-20 |
|
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: 90.84 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 255 SRDN-FMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFF 333
Cdd:cd19967 8 TPNNpFFVVEAEGAKEKAKEL-GYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 334 NKEpsrkaLDSYDKAYYVGTDSKESGiiqGDLIAKHWAAnqgwDLNKDGqiQFVLLKGEPGHPDAEART---TYVIKELN 410
Cdd:cd19967 87 DRE-----INAEGVAVAQIVSDNYQG---AVLLAQYFVK----LMGEKG--LYVELLGKESDTNAQLRSqgfHSVIDQYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 411 DKGIKTEQlqldTAMWDTAQAKDKMDAWL-SGPnanKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALV 488
Cdd:cd19967 153 ELKMVAQQ----SADWDRTEAFEKMESILqANP---DIKGVICGNDEMALGAIAALKAAGRAGdVIIVGFDGSNDVRDAI 225
|
250 260 270
....*....|....*....|....*....|....*
gi 83699618 489 KSGALAGTVLNDANNQA-KATFDLAKNLADGKGAA 522
Cdd:cd19967 226 KEGKISATVLQPAKLIArLAVEQADQYLKGGSTGK 260
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
254-519 |
1.15e-17 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 83.93 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 254 GSRDNFMSVVRKAIEQDAKAApDVQL--LMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVV 331
Cdd:cd06310 8 GTTSAFWRTVREGAEAAAKDL-GVKIifVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 332 FFNkepSRKALDSYDKayYVGTDSKESGIIQGDLIAkhwAAnqgwdLNKDGQIqfVLLKGEPGHPDAEARTTYVIKEL-- 409
Cdd:cd06310 87 VID---SGIKGDAYLS--YIATDNYAAGRLAAQKLA---EA-----LGGKGKV--AVLSLTAGNSTTDQREEGFKEYLkk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 410 NDKGIKTEQLQLdtAMWDTAQAKDKMDAWLSG-PNankIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEALAL 487
Cdd:cd06310 152 HPGGIKVLASQY--AGSDYAKAANETEDLLGKyPD---IDGIFATNEITALGAAVAIKSRKLSgQIKIVGFDSQEELLDA 226
|
250 260 270
....*....|....*....|....*....|..
gi 83699618 488 VKSGALAGTVLNDANNQAKATFDLAKNLADGK 519
Cdd:cd06310 227 LKNGKIDALVVQNPYEIGYEGIKLALKLLKGE 258
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
258-519 |
1.23e-17 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 83.64 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 258 NFMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEP 337
Cdd:cd19972 12 DFFNQIKQSVEAEAKKK-GYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 338 SRKALDSydkayYVGTDSKESGIIQGDLIAKHwaanqgwdlnKDGQIQFVLLKGEPGHPDAEART---TYVIKELNDKGI 414
Cdd:cd19972 91 EDAPGDT-----FIATDSVAAAKELGEWVIKQ----------TGGKGEIAILHGQLGTTPEVDRTkgfQEALAEAPGIKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 415 KTEQlqldTAMWDTAQA-KDKMDAWLSGPNankIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGA 492
Cdd:cd19972 156 VAEQ----TADWDQDEGfKVAQDMLQANPN---ITVFFGQSDAMALGAAQAVKVAGLDHkIWVVGFDGDVAGLKAVKDGV 228
|
250 260
....*....|....*....|....*..
gi 83699618 493 LAGTVLNDANNQAKATFDLAKNLADGK 519
Cdd:cd19972 229 LDATMTQQTQKMGRLAVDSAIDLLNGK 255
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
259-523 |
2.35e-17 |
|
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: 82.72 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVffnkeps 338
Cdd:cd06321 14 FVAMVRGAEEAAAEINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVV------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 339 rkALDSYDKAY--YVGTDSKESGIIQGDLIAKhwaanqgwDLNKDGQIqfVLLKGEPGHP--D---------AEARTTYV 405
Cdd:cd06321 87 --AVDVAAEGAdaTVTTDNVQAGYLACEYLVE--------QLGGKGKV--AIIDGPPVSAviDrvngckealAEYPGIKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 406 IKELNDKGIKTEQLqldTAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEAL 485
Cdd:cd06321 155 VDDQNGKGSRAGGL---SVMTRMLTAHPDVDG------------VFAINDPGAIGALLAAQQAGRDDIVITSVDGSPEAV 219
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 83699618 486 ALVK--SGALAGTVLNDANNQAKATFDLAKNLADGKGAAD 523
Cdd:cd06321 220 AALKreGSPFIATAAQDPYDMARKAVELALKILNGQEPAP 259
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
279-497 |
7.60e-17 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 82.06 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 279 LLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYdkayyVGTDSKES 358
Cdd:PRK10653 59 LVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSH-----IASDNVAG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 359 GIIQGDLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELndKGIKTEQLQLDTAMWDTAQAKDKMDAW 438
Cdd:PRK10653 134 GKMAGDFIAKK--------LGEGAKV--IQLEGIAGTSAARERGEGFKQAV--AAHKFNVLASQPADFDRTKGLNVMQNL 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 439 LSgpnAN-KIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTV 497
Cdd:PRK10653 202 LT---AHpDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGIKAVNRGKLAATI 258
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
257-497 |
1.63e-16 |
|
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: 80.35 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 257 DNFMSVVRKAIEQDAKAAP-DVQLLmNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNK 335
Cdd:cd06312 12 DPFWSVVKKGAKDAAKDLGvTVQYL-GPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAINS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 336 EPSRKALDSydkAY--YVGTDSKESGIIQGDLIAKHWAANqgwdlnkdgqiqFVLLKGEPGHPDAEARTTYVIKELNDKG 413
Cdd:cd06312 91 GDDRSKERL---GAltYVGQDEYLAGQAAGERALEAGPKN------------ALCVNHEPGNPGLEARCKGFADAFKGAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 414 IKTEQLQLDTamwDTAQAKDKMDAWLsgpNANK-IEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSG 491
Cdd:cd06312 156 ILVELLDVGG---DPTEAQEAIKAYL---QADPdTDAVLTLGPVGADPALKAVKEAGLKGkVKIGTFDLSPETLEAIKDG 229
|
....*.
gi 83699618 492 ALAGTV 497
Cdd:cd06312 230 KILFAI 235
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
259-497 |
1.76e-16 |
|
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: 80.32 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAaPDVQLLMNDSQN-DQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEp 337
Cdd:cd06314 13 FWDLAEAGAEKAAKE-LGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFDSD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 338 srkALDSYDKAyYVGTDSKESGIIQGDLIAKhwaanqgwDLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELNDKGiKTE 417
Cdd:cd06314 91 ---APDSKRLA-YIGTDNYEAGREAGELMKK--------ALPGGGKV--AIITGGLGADNLNERIQGFKDALKGSP-GIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 418 QLQLDTAMWDTAQAKDKMDAWLSG-PNANKIEVVIANNdamAMGAVEALKAHNK-SSIPVFGVDALPEALALVKSGALAG 495
Cdd:cd06314 156 IVDPLSDNDDIAKAVQNVEDILKAnPDLDAIFGVGAYN---GPAIAAALKDAGKvGKVKIVGFDTLPETLQGIKDGVIAA 232
|
..
gi 83699618 496 TV 497
Cdd:cd06314 233 TV 234
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
284-477 |
1.92e-16 |
|
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: 81.20 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 284 SQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPsrkaldSYDKAYYVGTDSKESGIIQG 363
Cdd:cd19999 42 ADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPV------SSPDAINVVIDQYKWAAIQA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 364 dliakHWAANQgwdLNKDGQIqfVLLKGEPGHPDAEAR---TTYVIKElnDKGIKTeqLQLDTAMWDTAQAKDKMDAWLS 440
Cdd:cd19999 116 -----QWLAEQ---LGGKGNI--VAINGVAGNPANEARvkaADDVFAK--YPGIKV--LASVPGGWDQATAQQVMATLLA 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 83699618 441 gpNANKIEVVIaNNDAMAMGAVEALKAHNKSSIPVFG 477
Cdd:cd19999 182 --TYPDIDGVL-TQDGMAEGVLRAFQAAGKDPPVMTG 215
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
257-549 |
2.24e-16 |
|
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: 80.11 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 257 DNFMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNke 336
Cdd:cd06317 11 AQFFNQINQGAQAAAKDL-GVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYD-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 337 psrKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGwdlnkdGQIQFVLLkGEPGHPDAEARTTYVIKELNDK---- 412
Cdd:cd06317 88 ---AVIPSDFQAAQVGVDNLEGGKEIGKYAADYIKAELG------GQAKIGVV-GALSSLIQNQRQKGFEEALKANpgve 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 413 --GIKTEQLQLDTAMwdtAQAKDKMDAwlsgpNANkIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPE-ALALV 488
Cdd:cd06317 158 ivATVDGQNVQEKAL---SAAENLLTA-----NPD-LDAIYATGEPALLGAVAAVRSQGRQgKIKVFGWDLTKQaIFLGI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83699618 489 KSGALAGTVLNDANNQAKATFDLAKNLADGKGAAdgtnwkidnKVVRVPYVGVDKDNLAEF 549
Cdd:cd06317 229 DEGVLQAVVQQDPEKMGYEAVKAAVKAIKGEDVE---------KTIDVPPTIVTKENVDQF 280
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
259-497 |
4.40e-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: 380625 [Multi-domain] Cd Length: 275 Bit Score: 79.22 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAAPDVQLLMNDSQNDQS--KQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKE 336
Cdd:cd19970 13 FFIEMEKGARKHAKEANGYELLVKGIKQETDieQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 337 PSRKALDSYDKAY-YVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELNDKGIK 415
Cdd:cd19970 93 LDADALKEGGINVpFVGPDNRQGAYLAGDYLAKK--------LGKGGKV--AIIEGIPGADNAQQRKAGFLKAFEEAGMK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 416 TEQLQldTAMWDTAQAKDKMDAWLSG-PNankIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGAL 493
Cdd:cd19970 163 IVASQ--SANWEIDEANTVAANLLTAhPD---IRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKM 237
|
....
gi 83699618 494 AGTV 497
Cdd:cd19970 238 LATI 241
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
265-546 |
4.54e-16 |
|
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: 79.68 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 265 KAIEQDAKAAPDVQLLMN----DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNkepsrK 340
Cdd:cd06300 19 ASLKADAAQSGQKGLVKElivaNSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFD-----G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 341 ALDSYDkAYYVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELnDKGIKTEQLQ 420
Cdd:cd06300 94 AVTSPD-AYNVSNDQVEWGRLGAKWLFEA--------LGGKGNV--LVVRGIAGAPASADRHAGVKEAL-AEYPGIKVVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 421 LDTAMWDTAQAKDKMDAWL-SGPNANKievvIANNDAMAMGAVEALKAHNKSSIPVFGVD---ALPEALALVKSGALAGT 496
Cdd:cd06300 162 EVFGGWDEATAQTAMLDFLaTHPQVDG----VWTQGGEDTGVLQAFQQAGRPPVPIVGGDengFAKQWWKHPKKGLTGAA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 83699618 497 VLNDANNQAKAtFDLAKNLADGKGAAdgtnwkidNKVVRVPYVGVDKDNL 546
Cdd:cd06300 238 VWPPPAIGAAG-LEVALRLLEGQGPK--------PQSVLLPPPLITNDDA 278
|
|
| GFP |
pfam01353 |
Green fluorescent protein; |
577-772 |
3.26e-15 |
|
Green fluorescent protein;
Pssm-ID: 426217 Cd Length: 211 Bit Score: 75.30 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 577 LDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFGYGLmcFARYPDHMkqhDFFKSAMPEG-YVQER 655
Cdd:pfam01353 7 MEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKGALPFSPYLLAPHL*YYQ--YLPFPDGT---SPFQAAVENGgYQVHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 656 TIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLeyNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGS- 734
Cdd:pfam01353 82 TFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSL--TGWDPSVEKMIPRNDKTLVGDINWSLKLTDGKr 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 83699618 735 --VQLADHYQQNTPIGDGpVLLPDNHYLSYQSALSKDPNE 772
Cdd:pfam01353 160 yrAQVVTNYTFAKPVPAG-LKLPPPHFVFRKIERTGSKTE 198
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
257-493 |
5.35e-15 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380621 [Multi-domain] Cd Length: 278 Bit Score: 76.21 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 257 DNFMSVVRKAieqdAKAAPD---VQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGT-VIEKARGQNVPVVF 332
Cdd:cd19966 12 DPFWTVVYNG----AKDAAAdlgVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTpLIEAAKKAGIIVTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 333 FNKePSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGwdlnkdgqiQFVLLKGEPGH-PDAEARTTYVIKELND 411
Cdd:cd19966 88 FNT-DLPKLEYGDCGLGYVGADLYAAGYTLAKELVKRGGLKTG---------DRVFVPGLLPGqPYRVLRTKGVIDALKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 412 KGIKTEQLQLDTAMWDTAQAKDKMDAWLSgpnANK-IEVVIANNDAMAMGAVEALKAHNK--SSIPVFGVDALPEALALV 488
Cdd:cd19966 158 AGIKVDYLEISLEPNKPAEGIPVMTGYLA---ANPdVKAIVGDGGGLTANVAKYLKAAGKkpGEIPVAGFDLSPATVQAI 234
|
....*
gi 83699618 489 KSGAL 493
Cdd:cd19966 235 KSGYV 239
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
259-484 |
1.69e-14 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 75.62 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRkAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALaInLVDPAAAGTVIEKARGQNVPVVFFNKEPS 338
Cdd:COG1609 76 FAELLR-GIEEAARER-GYQLLLANSDEDPEREREALRLLLSRRVDGL-I-LAGSRLDDARLERLAEAGIPVVLIDRPLP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 339 RKALDSydkayyVGTDSKESGiiqgDLIAKHwAANQGWDlnkdgqiQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQ 418
Cdd:COG1609 152 DPGVPS------VGVDNRAGA----RLATEH-LIELGHR-------RIAFIGGPADSSSARERLAGYREALAEAGLPPDP 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 419 LQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNKsSIP----VFGVDALPEA 484
Cdd:COG1609 214 ELVVEGDFSAESGYEAARRLLARGP--RPTAIFCANDLMALGALRALREAGL-RVPedvsVVGFDDIPLA 280
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
269-489 |
3.01e-14 |
|
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: 73.87 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 269 QDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKAL---DSY 345
Cdd:cd06305 22 VAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAGIPVVTFDTDSQVPGVnniTQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 346 DKAyyVGTDSkesgiiqGDLIAKhwaanqgwDLNKDGQIQFVLLKGEPghPDAEARTTYVIKELNDKGIKTEQLQLDTAM 425
Cdd:cd06305 102 DYA--LGTLS-------LGQLVK--------DLNGEGNIAVFNVFGVP--PLDKRYDIYKAVLKANPGIKKIVAELGDVT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83699618 426 WDTAQ-AKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVK 489
Cdd:cd06305 163 PNTAAdAQTQVEALLKKYPEGGIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISNQDLELMA 227
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
259-497 |
3.99e-14 |
|
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: 73.46 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIeQDAKAAPDVQLLMNDSQN-DQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEp 337
Cdd:cd19965 13 FFQPVKKGM-DDACELLGAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAFNVD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 338 srkALDSYDKAY-YVGTDSKESGIIQGDLIAKhwaanqgwdLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKT 416
Cdd:cd19965 91 ---APGGENARLaFVGQDLYPAGYVLGKRIAE---------KFKPGGGHVLLGISTPGQSALEQRLDGIKQALKEYGRGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 417 EQLQLDTAMwDTAQAKDKMDAWLSG-PNANkieVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALA 494
Cdd:cd19965 159 TYDVIDTGT-DLAEALSRIEAYYTAhPDIK---AIFATGAFDTAGAGQAIKDLGlKGKVLVGGFDLVPEVLQGIKAGYID 234
|
...
gi 83699618 495 GTV 497
Cdd:cd19965 235 FTI 237
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
276-497 |
7.82e-14 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 73.41 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 276 DVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVD-PAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYDK-----AY 349
Cdd:cd06324 30 GIELEVLYANRNRFKMLELAEELLARPPKPDYLILVNeKGVAPELLELAEQAKIPVFLINNDLTDEERALLGKprekfKY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 350 YVGT---DSKESGIiqgdLIAKHwAANQGWDLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIkTEQLQLDTAMW 426
Cdd:cd06324 110 WLGSivpDNEQAGY----LLAKA-LIKAARKKSDDGKIRVLAISGDKSTPASILREQGLRDALAEHPD-VTLLQIVYANW 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83699618 427 DTAQAKDKMDAWLSG-PNANkieVVIANNDAMAMGAVEALKAHNK---SSIPVFGVDALPEALALVKSGALAGTV 497
Cdd:cd06324 184 SEDEAYQKTEKLLQRyPDID---IVWAANDAMALGAIDALEEAGLkpgKDVLVGGIDWSPEALQAVKDGELTASV 255
|
|
| GFP |
pfam01353 |
Green fluorescent protein; |
34-217 |
1.38e-13 |
|
Green fluorescent protein;
Pssm-ID: 426217 Cd Length: 211 Bit Score: 70.68 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 34 LDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTWGVqcFSRYPDHMkqhDFFKSAMPEG-YVQER 112
Cdd:pfam01353 7 MEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKGALPFSPYLLAPHL*YYQ--YLPFPDGT---SPFQAAVENGgYQVHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 113 TIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLeyNYISHNVYITADKQKNGIKANFKIRHNIEDGS- 191
Cdd:pfam01353 82 TFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSL--TGWDPSVEKMIPRNDKTLVGDINWSLKLTDGKr 159
|
170 180
....*....|....*....|....*...
gi 83699618 192 --VQLADHYQQNTPIGDGpVLLPDNHYL 217
Cdd:pfam01353 160 yrAQVVTNYTFAKPVPAG-LKLPPPHFV 186
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
254-544 |
9.17e-13 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 69.19 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 254 GSRDNFMSVVRKAIEQdakAAPDVQLLMN----DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVP 329
Cdd:cd20005 8 GFQHQFWKAVKKGAEQ---AAKELGVKITfegpDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 330 VVFFNkepsrKALDSYDKAYYVGTDSKESGIIQGDLIAKhwaanqgwdlNKDGQIQFVLLKGEPGHPDAEARTTYVIKEL 409
Cdd:cd20005 85 VVTFD-----SGVPSDLPLATVATDNYAAGALAADHLAE----------LIGGKGKVAIVAHDATSETGIDRRDGFKDEI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 410 NDK--GIKTEQLQLDTAmwDTAQAKDKMDAWLSG-PNankIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDALPEAL 485
Cdd:cd20005 150 KEKypDIKVVNVQYGVG--DHAKAADIAKAILQAnPD---LKGIYATNEGAAIGVANALKEMGKlGKIKVVGFDSGEAQI 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 83699618 486 ALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAAdgtnwkidnKVVRVPYVGVDKD 544
Cdd:cd20005 225 DAIKNGVIAGSVTQNPYGMGYKTVKAAVKALKGEEVE---------KLIDTGAKWYDKD 274
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
259-500 |
1.45e-12 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 69.52 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKA-APDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAI------NLVDPAAagtvieKARGQNVPVV 331
Cdd:PRK09701 38 FWVDMKKGIEDEAKTlGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFaplssvNLVMPVA------RAWKKGIYLV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 332 FFNKEPSrkaLDSYDKA-----YYVGTDSKESGIIQGDLIAKHWAANQGwdlnkdgqiQFVLLKGEPGHPDAEAR---TT 403
Cdd:PRK09701 112 NLDEKID---MDNLKKAggnveAFVTTDNVAVGAKGASFIIDKLGAEGG---------EVAIIEGKAGNASGEARrngAT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 404 YVIKElnDKGIKTEQLQldTAMWDTAQAKDKMDAWLS-GPNankIEVVIANNDAMAMGAVEALK-AHNKSSIPVFGVDAL 481
Cdd:PRK09701 180 EAFKK--ASQIKLVASQ--PADWDRIKALDVATNVLQrNPN---IKAIYCANDTMAMGVAQAVAnAGKTGKVLVVGTDGI 252
|
250
....*....|....*....
gi 83699618 482 PEALALVKSGALAGTVLND 500
Cdd:PRK09701 253 PEARKMVEAGQMTATVAQN 271
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
283-497 |
1.70e-12 |
|
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: 68.52 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 283 DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEpsrkALDSyDKAYYVGTDSKESGIIQ 362
Cdd:cd19969 37 PATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSD----APES-KRISYVGTDNYEAGYAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 363 GDLIAKHwaanqgwdLNKDGQIQFVLLKGEPGHpdaEARTT------------YVIKELNDKGIKTEQLQLDTAMwdtAQ 430
Cdd:cd19969 112 AEKLAEL--------LGGKGKVAVLTGPGQPNH---EERVEgfkeafaeypgiEVVAVGDDNDDPEKAAQNTSAL---LQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83699618 431 AKDKMDAWLsGPNANKievvianndamAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTV 497
Cdd:cd19969 178 AHPDLVGIF-GVDASG-----------GVGAAQAVREAGKTGkVKIVAFDDDPETLDLIKDGVIDASI 233
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
257-484 |
9.87e-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: 66.00 E-value: 9.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 257 DNFMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALaInLVDPAAAGTVIEKARGQNVPVVFFNKE 336
Cdd:cd06267 11 NPFFAELLRGIEDAARER-GYSLLLCNTDEDPEREREYLRLLLSRRVDGI-I-LAPSSLDDELLEELLAAGIPVVLIDRR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 337 PSRKALDSydkayyVGTDSKESGIiqgdLIAKHwaanqgwdLNKDG--QIqfVLLKGEPGHPDAEARTTYVIKELNDKGI 414
Cdd:cd06267 88 LDGLGVDS------VVVDNYAGAY----LATEH--------LIELGhrRI--AFIGGPLDLSTSRERLEGYRDALAEAGL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83699618 415 KTEQLQLDTAMWDTAQAKDKMDAWLSGPnaNKIEVVIANNDAMAMGAVEALKAHNKsSIP----VFGVDALPEA 484
Cdd:cd06267 148 PVDPELVVEGDFSEESGYEAARELLALP--PRPTAIFAANDLMAIGALRALRELGL-RVPedisVVGFDDIPLA 218
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
286-529 |
2.03e-11 |
|
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: 65.30 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 286 NDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDL 365
Cdd:cd06306 41 TNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNGIDSPKVAA-----RVLVDFYDMGYLAGEY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 366 IAKHwaanqgwdlNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTeqlqLDTAMWDT--AQAKDKMDAWL-SGP 442
Cdd:cd06306 116 LVEH---------HPGKPVKVAWFPGPAGAGWAEDREKGFKEALAGSNVEI----VATKYGDTgkAVQLNLVEDALqAHP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 443 NANkievVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGA 521
Cdd:cd06306 183 DID----YIVGNAVAAEAAVGALREAGLTGkVKVVSTYLTPGVYRGIKRGKILAAPSDQPVLQGRIAVDQAVRALEGKPV 258
|
....*...
gi 83699618 522 ADGTNWKI 529
Cdd:cd06306 259 PKHVGPPI 266
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
285-501 |
4.64e-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: 61.09 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 285 QNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNkepsrKALDSYDKAYYVGTDSKESGIIQGD 364
Cdd:cd20004 40 EDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIID-----SDLGGDAVISFVATDNYAAGRLAAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 365 LIAKhwaanqgwDLNKDGQIqfVLLKGEPGHPDAEART---TYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSG 441
Cdd:cd20004 115 RMAK--------LLNGKGKV--ALLRLAKGSASTTDRErgfLEALKKLAPGLKVVDDQYAGGTVGEARSSAENLLNQYPD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83699618 442 PNAnkievVIANNDAMAMGAVEALKAHNKSSIPVF-GVDALPEALALVKSGALAGTVLNDA 501
Cdd:cd20004 185 VDG-----IFTPNESTTIGALRALRRLGLAGKVKFiGFDASDLLLDALRAGEISALVVQDP 240
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
284-500 |
1.31e-09 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 59.94 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 284 SQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARgQNVPVVFFNkepSRKALDSYDKAYyvGTDSKESGIIQG 363
Cdd:cd20008 39 TEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD-AGIPVVLVD---SGANTDDYDAFL--ATDNVAAGALAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 364 DLIAKHWAANQGwdlnKDGQIqfVLLKGEPGHPDAEART---TYVIKElNDKGIKTEQLQLDTAmwDTAQAKDKM-DAWL 439
Cdd:cd20008 113 DELAELLKASGG----GKGKV--AIISFQAGSQTLVDREegfRDYIKE-KYPDIEIVDVQYSDG--DIAKALNQTtDLLT 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83699618 440 SGPNANKIevvIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEALALVKSGALAGTVLND 500
Cdd:cd20008 184 ANPDLVGI---FGANNPSAVGVAQALAEAGKAgKIVLVGFDSSPDEVALLKSGVIKALVVQD 242
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
269-545 |
2.77e-09 |
|
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: 59.18 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 269 QDAKAAPDVQLLMN-DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDsydk 347
Cdd:cd06302 22 KKAAKELGVEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSDAPPSARD---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 348 aYYV-GTDSKESGIIQGDLIAKhwaanqgwDLNKDGQIqfVLLKGEPGHPDAEARTTYvIKELNDKgiKTEQLQL----- 421
Cdd:cd06302 98 -YFVnQADDEGLGEALVDSLAK--------EIGGKGKV--AILSGSLTATNLNAWIKA-MKEYLKS--KYPDIELvdtyy 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 422 --DTAMWDTAQAKDKMDAWlsgPNankIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVdALP-EALALVKSGALAGTV 497
Cdd:cd06302 164 tdDDQQKAYTQAQNLIQAY---PD---LKGIIGVSTTAPPAAAQAVEEAGKTgKVAVTGI-GLPnTARPYLKDGSVKEGV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 83699618 498 LNDANNQAKATFDLAKNLADGKGAADGTNW---------KIDNKVVRV-PYVGVDKDN 545
Cdd:cd06302 237 LWDPAKLGYLTVYAAYQLLKGKGFTEDSDDvgtggkvkvDVAGGEILLgPPLVFTKDN 294
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
242-546 |
1.64e-08 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 57.06 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 242 AAGITLGM--DEL-----YGSRDNFmsvVRKAIEQDAKaapdvqLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPA 314
Cdd:PRK10355 23 AKEVKIGMaiDDLrlerwQKDRDIF---VKKAESLGAK------VFVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 315 AAGTVIEKARGQNVPVVFFNKEPSRKALDsydkaYYVGTDSKESGIIQGDLIakhwaanqgwdLNKDGQIQFVLLKGEPG 394
Cdd:PRK10355 94 VLSNVIKEAKQEGIKVLAYDRMINNADID-----FYISFDNEKVGELQAKAL-----------VDKVPQGNYFLMGGSPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 395 HPDAE---ARTTYVIKELNDKG-IKTEQLQLDTAmWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNK 470
Cdd:PRK10355 158 DNNAKlfrAGQMKVLKPYIDSGkIKVVGDQWVDG-WLPENALKIMENALTA-NNNKIDAVVASNDATAGGAIQALSAQGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 471 S-SIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLadGKGAADGTNWKIDNKVVRVPY-----VGVDKD 544
Cdd:PRK10355 236 SgKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVEL--GNGEEPKANTTLNNGLKDVPSrlltpIDVNKN 313
|
..
gi 83699618 545 NL 546
Cdd:PRK10355 314 NI 315
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
268-475 |
1.81e-08 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 56.22 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 268 EQDAKAAPDVQLLMNDSQNDQsKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEpsrkaLDSYDK 347
Cdd:cd06311 22 EKQAKELADLEYKLVTSSNAN-EQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRG-----LNVLIY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 348 AYYVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELNDK-GIKTEQLQLDTAMW 426
Cdd:cd06311 96 DLYVAGDNPGMGVVSAEYIGKK--------LGGKGNV--VVLEVPSSGSVNEERVAGFKEVIKGNpGIKILAMQAGDWTR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 83699618 427 DTAqAKDKMDAWLSGPnanKIEVVIANNDAMAMGAVEALKAHNKSSIPV 475
Cdd:cd06311 166 EDG-LKVAQDILTKNK---KIDAVWAADDDMAIGVLQAIKEAGRTDIKV 210
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
284-477 |
4.63e-08 |
|
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: 55.37 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 284 SQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPsrkaldSYDKAYYVGTDSKESGIIQG 363
Cdd:cd19998 41 SGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVV------DEPCAYNVNTDQAKAGEQTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 364 DLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEART---TYVIKELNDKGIKTEQlqldTAMWDTAQAKDKMDAWLs 440
Cdd:cd19998 115 QWLVDK--------LGGKGNI--LMVRGVPGTSVDRDRYegaKEVFKKYPDIKVVAEY----YGNWDDGTAQKAVADAL- 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 83699618 441 gPNANKIEVVIAnNDAMAmGAVEALKAHNKSSIPVFG 477
Cdd:cd19998 180 -AAHPDVDGVWT-QGGET-GVIKALQAAGHPLVPVGG 213
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
279-484 |
4.71e-08 |
|
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380512 [Multi-domain] Cd Length: 268 Bit Score: 54.88 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 279 LLMNDSQNDQSKQNDQIDVLLAKGVKALAINlvdpAAAGT---VIEKARGQNVPVVFFNKEPSRKALDsydkayYVGTDS 355
Cdd:cd06289 32 VFLANTGEDPERQRRFLRRMLEQGVDGLILS----PAAGTtaeLLRRLKAWGIPVVLALRDVPGSDLD------YVGIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 356 KESGiiqgDLIAKHwaanqgwdLNKDGQIQFVLLKGEPGHPDAEARttyviKELNDKGIKTEQLQLDTAMW-----DTAQ 430
Cdd:cd06289 102 RLGA----QLATEH--------LIALGHRRIAFLGGLSDSSTRRER-----LAGFRAALAEAGLPLDESLIvpgpaTREA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 83699618 431 AKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKSS---IPVFGVDALPEA 484
Cdd:cd06289 165 GAEAARELLD--AAPPPTAVVCFNDLVALGAMLALRRRGLEPgrdIAVVGFDDVPEA 219
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
279-484 |
2.65e-07 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 52.92 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 279 LLMNDSQNDQskQNDQIDVLLAKGVKALAINLVDPAAAgtVIEKARGQNVPVVFFNKEPSRKALDSydkayyVGTDSKES 358
Cdd:cd06278 33 LLFNVDDEDD--VDDALRQLLQYRVDGVIVTSATLSSE--LAEECARRGIPVVLFNRVVEDPGVDS------VSCDNRAG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 359 GiiqgDLIAKHWAANqgwdlnkdGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIktEQLQLDTAMWDTAQAKDKMDAW 438
Cdd:cd06278 103 G----RLAADLLLAA--------GHRRIAFLGGPEGTSTSRERERGFRAALAELGL--PPPAVEAGDYSYEGGYEAARRL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 83699618 439 LSGPNAnkIEVVIANNDAMAMGAVEALKAHNKSSIP----VFGVDALPEA 484
Cdd:cd06278 169 LAAPDR--PDAIFCANDLMALGALDAARQEGGLVVPedisVVGFDDIPMA 216
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
257-542 |
2.82e-07 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380662 [Multi-domain] Cd Length: 271 Bit Score: 52.63 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 257 DNFMSVVRKAIEQDAKAApDVQLLMN-DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFfnk 335
Cdd:cd20007 11 DPFYITMQCGAEAAAKEL-GVELDVQgPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVT--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 336 epsrkaLDSY--DKAY---YVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIqfVLLKGEPGHPDAEARTTYVIKELn 410
Cdd:cd20007 87 ------VDTTlgDPSFvlsQIASDNVAGGALAAEALAEL--------IGGKGKV--LVINSTPGVSTTDARVKGFAEEM- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 411 DKGIKTEQLQLDTAMWDTAQAKDKMDAWLSgpnANK-IEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEALALV 488
Cdd:cd20007 150 KKYPGIKVLGVQYSENDPAKAASIVAAALQ---ANPdLAGIFGTNTFSAEGAAAALRNAGKTgKVKVVGFDASPAQVEQL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 83699618 489 KSGALAGTVLNDANNQAKATFDLAKNLADGKgaadgtnwKIDNKVVrVPYVGVD 542
Cdd:cd20007 227 KAGTIDALIAQKPAEIGYLAVEQAVAALTGK--------PVPKDIL-TPFVVIT 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
283-556 |
3.66e-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: 52.63 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 283 DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPS-RKALDSYdkAYYVGTDSKESGII 361
Cdd:cd06316 37 DANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKLVFMDNVPDgLEAGKDY--VSVVSSDNRGNGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 362 QGDLIAKHwaanqgwdLNKDGQIQFVllkgepGHP---------DAEARTTyvIKELNDkGIKTEQLQLDTAMWDTAQ-A 431
Cdd:cd06316 115 AAELLAEA--------IGGKGKVGII------YHDadfyatnqrDKAFKDT--LKEKYP-DIKIVAEQGFADPNDAEEvA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 432 KDKMDAWlsgPNANKIEVVIannDAMAMGAVEALKAHNKSSIPVFGVDALPE-ALALVKSGALAGTVLNDANNQAKATFD 510
Cdd:cd06316 178 SAMLTAN---PDIDGIYVSW---DTPALGVISALRAAGRSDIKITTVDLGTEiALDMAKGGNVKGIGAQRPYDQGVAEAL 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 83699618 511 LAKNLADGKGAAdgtnwkidnKVVRVPYVGVDKDNLAEFSKKGAGT 556
Cdd:cd06316 252 AAALALLGKEVP---------PFIGVPPLAVTKDNLLEAWKQIFKT 288
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
256-484 |
6.87e-07 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 51.46 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 256 RDNFMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAInlVDPAAAGTVIEKARGQNVPVVFFNK 335
Cdd:cd06285 10 SNPFYAELVEGIEDAARER-GYTVLLADTGDDPERELAALDSLLSRRVDGLII--TPARDDAPDLQELAARGVPVVLVDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 336 EPSRKALDSydkayyVGTDSkESGiiqGDLIAKHWAANqgwdlnkdGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIK 415
Cdd:cd06285 87 RIGDTALPS------VTVDN-ELG---GRLATRHLLEL--------GHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83699618 416 TEQLQLDTAMWDTAQAKDKMDAWLSGPN---AnkievVIANNDAMAMGAVEALKAHNKsSIP----VFGVDALPEA 484
Cdd:cd06285 149 VPDERIVPGGFTIEAGREAAYRLLSRPErptA-----VFAANDLMAIGVLRAARDLGL-RVPedlsVVGFDDIPLA 218
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
259-484 |
9.69e-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: 51.36 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVrKAIEQDAKA-APDVQLLMNDSQNDQSKQndQIDVLLAKGVKALAINLVDPAAAgTVIEKARGQNVPVVFFNkep 337
Cdd:pfam00532 16 FQDLV-KGITKAAKDhGFDVFLLAVGDGEDTLTN--AIDLLLASGADGIIITTPAPSGD-DITAKAEGYGIPVIAAD--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 338 srkalDSYDKAYYVGTDSKEsgiiqgdliAKHWAANQGWDLNKDGQIQFVLLKGEP-GHPDAEARTTYVIKELNDKGIKT 416
Cdd:pfam00532 89 -----DAFDNPDGVPCVMPD---------DTQAGYESTQYLIAEGHKRPIAVMAGPaSALTARERVQGFMAALAAAGREV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83699618 417 EQLQLDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNKSSIP---------VFGVDALPEA 484
Cdd:pfam00532 155 KIYHVATGDNDIPDAALAANAMLvSHPT---IDAIVAMNDEAAMGAVRALLKQGRVKIPdivgiginsVVGFDGLSKA 229
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
265-498 |
1.31e-06 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 50.67 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 265 KAIEQDAKAAP-----DVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEpsr 339
Cdd:cd20006 17 QTVKSGAEAAAkeygvDLEFLGPESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSP--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 340 kaLDSYDKAYYVGTDSKESGIIQGDLIAKHwaanqgwdLNKDGQIQFVllkgepGHpdAEARTTYVIKElndKGIKtEQL 419
Cdd:cd20006 94 --VNSKKADSFVATDNYEAGKKAGEKLASL--------LGEKGKVAIV------SF--VKGSSTAIERE---EGFK-QAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 420 QLDTAMW---------DTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKA-HNKSSIPVFGVDALPEALALVK 489
Cdd:cd20006 152 AEYPNIKiveteycdsDEEKAYEITKELLS--KYPDINGIVALNEQSTLGAARALKElGLGGKVKVVGFDSSVEEIQLLE 229
|
....*....
gi 83699618 490 SGALAGTVL 498
Cdd:cd20006 230 EGIIDALVV 238
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
259-467 |
2.04e-06 |
|
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380503 [Multi-domain] Cd Length: 266 Bit Score: 49.95 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEqDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALainLVDPAAAGT-VIEKARGQNVPVVFFNKEP 337
Cdd:cd06280 13 FFTTIARGIE-DAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGI---ILAPSAGPSrELKRLLKHGIPIVLIDREV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 338 SRKALDSydkayyVGTDSKESGIIqgdlIAKHwaanqgwdLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTE 417
Cdd:cd06280 89 EGLELDL------VAGDNREGAYK----AVKH--------LIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 83699618 418 Q---LQLDTAMWDTAQAkdkMDAWLSGPNAnkIEVVIANNDAMAMGAVEALKA 467
Cdd:cd06280 151 EsliFEGDSTIEGGYEA---VKALLDLPPR--PTAIFATNNLMAVGALRALRE 198
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
246-468 |
2.50e-06 |
|
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380499 [Multi-domain] Cd Length: 269 Bit Score: 49.95 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 246 TLGMdeLYGSRDN--FMSVVRkAIEqDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALainLVDPAAAGTVIEK- 322
Cdd:cd06275 1 TIGL--LVTSSENpfFAEVVR-GVE-DACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGL---LLMCSEMTDDDAEl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 323 -ARGQNVPVVFFNKEPSRKALDSydkayyVGTDSkESGiiqGDLIAKHwaanqgwdLNKDGQIQFVLLKGEPGHPDAEAR 401
Cdd:cd06275 74 lAALRSIPVVVLDREIAGDNADA------VLDDS-FQG---GYLATRH--------LIELGHRRIGCITGPLEHSVSRER 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83699618 402 TTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAH 468
Cdd:cd06275 136 LAGFRRALAEAGIEVPPSWIVEGDFEPEGGYEAMQRLLSQPP--RPTAVFACNDMMALGALRAAQEQ 200
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
259-496 |
3.91e-06 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380628 [Multi-domain] Cd Length: 285 Bit Score: 49.39 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKA-APDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNK-- 335
Cdd:cd19973 13 FFVKMKEGAQKAAKAlGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVLVIALDTpt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 336 EPsrkaLDSYDKAYyvGTDSKESGIIQGDliakhWAANQGWDlnKDGQIqfVLLKGEPGHPDAEAR-----TTYVIKELN 410
Cdd:cd19973 93 DP----IDAADATF--ATDNFKAGVLIGE-----WAKAALGA--KDAKI--ATLDLTPGHTVGVLRhqgflKGFGIDEKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 411 DKGIKTEQ----LQLDTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEAL 485
Cdd:cd19973 158 PESNEDEDdsqvVGSADTNGDQAKGQTAMENLLQ--KDPDINLVYTINEPAAAGAYQALKAAGKEKgVLIVSVDGGCPGV 235
|
250
....*....|.
gi 83699618 486 ALVKSGALAGT 496
Cdd:cd19973 236 KDVKDGIIGAT 246
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
279-474 |
5.12e-06 |
|
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380514 [Multi-domain] Cd Length: 264 Bit Score: 48.67 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 279 LLMNdSQNDQSKQNDQIDVLLAKGVKALAInlvdpAAAGTVIEKARGQNVPVVFFNKEPSrkaldsyDKAYYVGTDSKES 358
Cdd:cd06291 33 ILCN-SNEDEEKEKEYLEMLKRNKVDGIIL-----GSHSLDIEEYKKLNIPIVSIDRYLS-------EGIPSVSSDNYQG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 359 GIiqgdLIAKHwaanqgwdLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAW 438
Cdd:cd06291 100 GR----LAAEH--------LIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFSEEDAYELAKEL 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 83699618 439 LSgpNANKIEVVIANNDAMAMGAVEALKAHNKsSIP 474
Cdd:cd06291 168 LE--KYPDIDGIFASNDLLAIGVLKALQKLGI-RVP 200
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
257-557 |
7.26e-06 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380652 [Multi-domain] Cd Length: 305 Bit Score: 48.83 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 257 DNFMSVVRKAIEQDAKAAPDVQllmnDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKE 336
Cdd:cd19997 19 DAFEEAAKKAKADGLIADYIVV----NADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 337 PSRkaldsyDKAYYVGTDSKESGIIQGDliakhWAANQgwdLNKDGQIqfVLLKGEPG-HPDAE--ARTTYVIKELNDKG 413
Cdd:cd19997 95 VTE------PCAYILNNDFEDYGAASVE-----YVADR---LGGKGNV--LEVRGVAGtSPDEEiyAGQVEALKKYPDLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 414 IKTEQlqldTAMWDTAQAKDKMDAWLsgPNANKIEVVIANNDAmAMGAVEALKAHNKsSIPVFGVDALPEALALVKSGAL 493
Cdd:cd19997 159 VVAEV----YGNWTQSVAQKAVTGIL--PSLPEVDAVITQGGD-GYGAAQAFEAAGR-PLPIIIGGNRGEFLKWWQEEYA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83699618 494 A---GTV-LNDANNQAKATFDLAKNLADGKGAAdgtnwkidnKVVRVPYVGVDKDNLAEFSKKGAGTG 557
Cdd:cd19997 231 KngyETVsVSTDPGQGSAAFWVALDILNGKDVP---------KEMILPVVTITEDDLDAWLAVTPDGI 289
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
259-467 |
2.93e-05 |
|
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380506 [Multi-domain] Cd Length: 266 Bit Score: 46.39 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAApDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVdpAAAGTVIEKARGQNVPVVFFNKEPS 338
Cdd:cd06283 13 FSSLLLKGIEDVCREA-GYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPT--GNNNDAYLELAQKGLPVVLVDRQIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 339 RKALDSydkayyVGTDSKESGIIQGDLIAKhwaanQGWDlnkdgqiQFVLLKGEPGHPDA-EARTTYVIKELNDKGIKTE 417
Cdd:cd06283 90 PLNWDT------VVTDNYDATYEATEHLKE-----QGYE-------RIVFVTEPIKGISTrRERLQGFLDALARYNIEGD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 83699618 418 QLQLDTAmwDTAQAKDKMDAWLSGPNANKIeVVIANNDAMAMGAVEALKA 467
Cdd:cd06283 152 VYVIEIE--DTEDLQQALAAFLSQHDGGKT-AIFAANGVVLLRVLRALKA 198
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
259-525 |
3.80e-05 |
|
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380658 Cd Length: 298 Bit Score: 46.50 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 259 FMSVVRKAIEQDAKAaPDVQLLMN-DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEP 337
Cdd:cd20003 13 YFTAAGQGAQEAAKE-LGVDVTYDgPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVTWDSDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 338 SRKALDsydkaYYVG-TDSKESGIIQGDLIAKHwaanqgwdLNKDGQIQFVllKGEPGHPD----AEARTTYVIKELNDK 412
Cdd:cd20003 92 NPDARD-----FFVNqATPEGIGKTLVDMVAEQ--------TGEKGKVAIV--TSSPTATNqnawIKAMKAYIAEKYPDM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 413 GIKTEQL---QLDTAMwdtAQAKDKMDAWlsgPNANKIEVVIANNDAMAMGAVEALKAHNKssIPVFGVdALPEAL-ALV 488
Cdd:cd20003 157 KIVTTQYgqeDPAKSL---QVAENILKAY---PDLKAIIAPDSVALPGAAEAVEQLGRTGK--VAVTGL-STPNVMrPYV 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 83699618 489 KSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGT 525
Cdd:cd20003 228 KDGTVKSVVLWDVVDLGYLAVYVARALADGTLLKVGD 264
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
394-484 |
2.29e-04 |
|
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380486 [Multi-domain] Cd Length: 269 Bit Score: 43.67 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 394 GHPDAEARTTYVIKELNDKGIKTEQLQLDTAmWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKsSI 473
Cdd:cd01544 129 GEEIEDPRLRAFREYMKEKGLYNEEYIYIGE-FSVESGYEAMKELLK--EGDLPTAFFVASDPMAIGALRALQEAGI-KV 204
|
90
....*....|....*
gi 83699618 474 P----VFGVDALPEA 484
Cdd:cd01544 205 PedisIISFNDIEVA 219
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
284-545 |
2.83e-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: 43.80 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 284 SQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVpVVFFNKEPSRKALDsYD-KAYyvgtDSKESGIIQ 362
Cdd:cd20001 38 ATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDAGI-VVITHEASNLKNVD-YDvEAF----DNAAYGAFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 363 GDLIAKHwaanqgwdLNKDGQ-IQFVLLKGEPGHPD------AEARTTYVIKELNDKGIKTEQLQldtamwDTAQAKDKm 435
Cdd:cd20001 112 MDKLAEA--------MGGKGKyVTFVGSLTSTSHMEwanaavAYQKANYPDMLLVTDRVETNDDS------ETAYEKAK- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 436 DAWLSGPNANKIEVVIANNDAMAMGAVEalKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNL 515
Cdd:cd20001 177 ELLKTYPDLKGIVGCSSSDVPGAARAVE--ELGLQGKIAVVGTGLPSVAGEYLEDGTIDYIQFWDPADAGYAMNALAVMV 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 83699618 516 ADGKGAADGTNWKID--NKV----VRVPY----VGVDKDN 545
Cdd:cd20001 255 LEGEKITDGTDLGVPgyEKVtvgkGKVLYgnawLIVTKDN 294
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
384-484 |
4.68e-04 |
|
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 41.55 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 384 IQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSG-PNAnkievVIANNDAMAMGAV 462
Cdd:pfam13377 10 IALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGAlPTA-----VFVANDEVALGVL 84
|
90 100
....*....|....*....|....*.
gi 83699618 463 EALKAHNKsSIP----VFGVDALPEA 484
Cdd:pfam13377 85 QALREAGL-RVPedlsVIGFDDSPLA 109
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
283-549 |
9.35e-04 |
|
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: 41.89 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 283 DSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVV-----FFNKEPSrkaldsyDKAYYVGTDSKE 357
Cdd:cd01540 36 DAKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAGIPVIavddqLVDADPM-------KIVPFVGIDAYK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 358 SGIIQGDLIAKHwAANQGWDLNKDG---QIQFVLLkgepghPDAEARTTYVIKELNDKGIKTEQ-LQLDTAMWDTAQAKD 433
Cdd:cd01540 109 IGEAVGEWLAKE-MKKRGWDDVKEVgvlAITMDTL------SVCVDRTDGAKDALKAAGFPEDQiFQAPYKGTDTEGAFN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 434 KMDAWLSG-PNANKIeVVIANNDAMAMGAVEAL-----KAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKA 507
Cdd:cd01540 182 AANAVITAhPEVKHW-LVVGCNDEGVLGAVRALeqagfDAEDIIGVGIGGYLAADEEFKKQPTGFKASLYISPDKHGYIA 260
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 83699618 508 TFDLAKNLADGKGAADGTnwkidnkvvRVPYVGVDKDNLAEF 549
Cdd:cd01540 261 AEELYNWITDGKPPPAET---------LTDGVIVTRDNYKEV 293
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
321-498 |
3.58e-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: 39.93 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 321 EKARGQNVPVVFFNKEPSRKALDSydkayyVGTDSKESGIiqgdLIAKHwaanqgwdLNKDGQIQFVLLkGEPGHPDAEA 400
Cdd:cd06295 80 RELAQQGLPMVVWGAPEDGQSYCS------VGSDNVKGGA----LATEH--------LIEIGRRRIAFL-GDPPHPEVAD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 401 RTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNKsSIP----V 475
Cdd:cd06295 141 RLQGYRDALAEAGLEADPSLLLSCDFTEESGYAAMRALLdSGTA---FDAIFAASDLIAMGAIRALRERGI-SVPgdvaV 216
|
170 180 190
....*....|....*....|....*....|
gi 83699618 476 FGVDALPEA------LALVK-SGALAGTVL 498
Cdd:cd06295 217 VGYDDIPLAayfrppLTTVRqDLALAGRLL 246
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
263-523 |
6.02e-03 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 39.51 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 263 VRKAIEQ---DAKAAPDVQLlmnDSQNDQSKQNdqIDVLLAKGVKALAINLV----DPAAAGTViekARGQNVPVVFFnk 335
Cdd:COG2984 19 AREGFKDglaEAGYGKNLKL---DYQNAQGDQA--TAAQIAAKLVADKPDLIvaigTPAAQAAA---NATKDIPVVFT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 336 epsrkALDSYDKAYYVGTDSKESGIIQG--DLIakhwaanqgwDLNKdgqiQFVLLK------------GEPGHPDAEAR 401
Cdd:COG2984 89 -----AVTDPVGAGLVKSLEKPGGNVTGvsDLL----------PIEK----QLELIKkllpdakrigvlYNPSEANSVAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 402 TTYVIKELNDKGIKTEQLQLDTamwdTAQAKDKMDAWlsgpnANKIEVVIANNDAMAMGAVEAL-KAHNKSSIPVFGVDA 480
Cdd:COG2984 150 VEELKKAAKKLGLELVEATVTS----SNEIQQALQSL-----AGKVDAIYVPTDNTVVSALEAIaKVAARAKIPVFGGDD 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 83699618 481 lpealALVKSGALAGtVLNDANNQAKATFDLAKNLADGKGAAD 523
Cdd:COG2984 221 -----SSVKAGALAG-YGIDYYELGRQAAEMALRILKGEKPAD 257
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
269-479 |
6.88e-03 |
|
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380511 [Multi-domain] Cd Length: 268 Bit Score: 39.07 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 269 QDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAInlvdpAAAGT--VIEKARGQNVPVVFFNkepsrkALDSYD 346
Cdd:cd06288 23 QDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIY-----ASMHHreVTLPPELTDIPLVLLN------CFDDDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83699618 347 KAYYVGTDSKESGIiqgdLIAKHWAANqgwdlnkdGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMW 426
Cdd:cd06288 92 SLPSVVPDDEQGGY----LATRHLIEA--------GHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHGDW 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 83699618 427 DTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNKsSIP----VFGVD 479
Cdd:cd06288 160 GRESGYEAAKRLLSAPD--RPTAIFCGNDRMAMGVYQAAAELGL-RVPedlsVVGFD 213
|
|
| |
