|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
43-311 |
6.66e-113 |
|
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: 327.70 E-value: 6.66e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYTKKYIdekLGGKSEIAIVTDLKSQIQMQRIDGFKDALKGSANVKILN 201
Cdd:cd06322 81 IPVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKAL---LGGGGKIAIIDYPEVESVVLRVNGFKEAIKKYPNIEIVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 202 SQPGY-DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGI-TDGTILAMIQQQ 278
Cdd:cd06322 158 EQPGDgRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAgKEDKIKVIGFDGNPEAIKAIaKGGKIKADIAQQ 237
|
250 260 270
....*....|....*....|....*....|...
gi 489531185 279 PKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYD 311
Cdd:cd06322 238 PDKIGQETVEAIVKYLAGETVEKEILIPPKLYT 270
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
4-315 |
4.97e-88 |
|
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: 266.02 E-value: 4.97e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 4 RKILSLGIAGILAIgMLTGCSmegpSKSDNKGGSDKKDLTIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDV 83
Cdd:COG1879 1 KRLALLAAVLALAL-ALAACG----SAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 84 AKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEytkkYIDEK 162
Cdd:COG1879 76 AKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAgIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAE----YLAKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 163 LGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSANVKILNSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGAK 240
Cdd:COG1879 152 LGGKGKVAILTgSPGAPAANERTDGFKEALKEYPGIKVVAEQYAdWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489531185 241 AALESA-KNKDVKIVGFDLTEEASSGITDGTILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYDKENI 315
Cdd:COG1879 232 QALKAAgRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
43-309 |
4.09e-81 |
|
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: 247.09 E-value: 4.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNT-ENITSYVGTVSYDAGKKLGEytkkYIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSANVKI 199
Cdd:cd01536 81 IPVVAVDTDIDGgGDVVAFVGTDNYEAGKLAGE----YLAEALGGKGKVAILEgPPGSSTAIDRTKGFKEALKKYPDIEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 200 LNSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGTILAMIQQ 277
Cdd:cd01536 157 VAEQPAnWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAgRTGDIKIVGVDGTPEALKAIKDGELDATVAQ 236
|
250 260 270
....*....|....*....|....*....|..
gi 489531185 278 QPKEMGRLAVEAVVKAIKGEKVEKNIPVPALL 309
Cdd:cd01536 237 DPYLQGYLAVEAAVKLLNGEKVPKEILTPVTL 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
43-319 |
7.45e-77 |
|
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: 236.50 E-value: 7.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYTKKYIDEKLGGKSEIAIVTDLKSQIQMQRIDGFKDALKGSANVKILN 201
Cdd:cd06317 81 IPVIAYDAVIPSDFQAAQVGVDNLEGGKEIGKYAADYIKAELGGQAKIGVVGALSSLIQNQRQKGFEEALKANPGVEIVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 202 SQPGYDREESLNTV-ENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEE-ASSGITDGTILAMIQQQ 278
Cdd:cd06317 161 TVDGQNVQEKALSAaENLLTANPDLDAIYATGEPALLGAVAAVRSQgRQGKIKVFGWDLTKQaIFLGIDEGVLQAVVQQD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489531185 279 PKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYDKENIKDFK 319
Cdd:cd06317 241 PEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTKENVDQFR 281
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
43-306 |
2.62e-67 |
|
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: 211.77 E-value: 2.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE-K 121
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYtkkyIDEKLGGKSEIAIVTDLK-SQIQMQRIDGFKDALKGSANVKIL 200
Cdd:cd06323 81 IPVITVDRSVTGGKVVSHIASDNVAGGEMAAEY----IAKKLGGKGKVVELQGIPgTSAARERGKGFHNAIAKYPKINVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNKDVKIVGFDLTEEASSGITDGTILAMIQQQP 279
Cdd:cd06323 157 ASQTAdFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQP 236
|
250 260
....*....|....*....|....*..
gi 489531185 280 KEMGRLAVEAVVKAIKGEKVEKNIPVP 306
Cdd:cd06323 237 EEMGAKAVETADKYLKGEKVPKKIPVP 263
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
43-306 |
6.06e-64 |
|
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: 202.81 E-value: 6.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVD-AVLNTENITSYVGTVSYDAGKKLGEYTKKyideKLGGKSEIAIVTDLKSQIQMQRIDGFKDALKGSANVKIL 200
Cdd:cd19971 81 IPVINVDtPVKDTDLVDSTIASDNYNAGKLCGEDMVK----KLPEGAKIAVLDHPTAESCVDRIDGFLDAIKKNPKFEVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQPGY-DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGTILAMIQQQ 278
Cdd:cd19971 157 AQQDGKgQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAgKLGDILVYGVDGSPDAKAAIKDGKMTATAAQS 236
|
250 260
....*....|....*....|....*...
gi 489531185 279 PKEMGRLAVEAVVKAIKGEKVEKNIPVP 306
Cdd:cd19971 237 PIEIGKKAVETAYKILNGEKVEKEIVVP 264
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
43-317 |
2.68e-55 |
|
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: 181.26 E-value: 2.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE-K 121
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTV---SYDAGKKLGEYTKKYIDEKlggKSEIAIVTDLK-SQIQMQRIDGFKDALKGSANV 197
Cdd:cd06309 81 IPVILVDRTIDGEDGSLYVTFIgsdFVEEGRRAAEWLVKNYKGG---KGNVVELQGTAgSSVAIDRSKGFREVIKKHPNI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 198 KILNSQPG-YDREESLNTVENLIQSNP-DVDIIYATAENSVLGAKAALESAK---NKDVKIVGFDLTEEASSGITDGTIL 272
Cdd:cd06309 158 KIVASQSGnFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGlkpGKDVLVVGIDGQKDALEAIKAGELN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489531185 273 AMIQQQPKeMGRLAVEAVVKAIKGEKVEKNIPVPALLYDKENIKD 317
Cdd:cd06309 238 ATVECNPL-FGPTAFDTIAKLLAGEKVPKLIIVEERLFDKDNAAE 281
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
43-318 |
6.04e-53 |
|
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380536 [Multi-domain] Cd Length: 277 Bit Score: 175.15 E-value: 6.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEytkkYIDEKLGGKSEIAIvtdLKSQI----QMQRIDGFKDALKGSANV 197
Cdd:cd06313 81 IPLVGVNALIENEDLTAYVGSDDVVAGELEGQ----AVADRLGGKGNVVI---LEGPIgqsaQIDRGKGIENVLKKYPDI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 198 KILNSQPG-YDREESLNTVENLIQSNPD-VDIIYATAENSVLGAKAALESAKNKDVKIVGFDLTEEASSGITDGTILAMI 275
Cdd:cd06313 154 KVLAEQTAnWSRDEAMSLMENWLQAYGDeIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDALQAVKSGELIATV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489531185 276 QQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYDKENIKDF 318
Cdd:cd06313 234 LQDAEAQGKGAVEVAVDAVKGEGVEKKYYIPFVLVTKDNVDDY 276
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
44-315 |
1.47e-52 |
|
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: 174.37 E-value: 1.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 44 IGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDP--DQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK 121
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAApsETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 -MPVVTVDAVLNTE-------NITSYVGTVSYDAGKKLGEYtkkyIDEKLGGKSEIAIVTDLKSQIQ-MQRIDGFKDALK 192
Cdd:cd06320 82 gIPVINLDDAVDADalkkaggKVTSFIGTDNVAAGALAAEY----IAEKLPGGGKVAIIEGLPGNAAaEARTKGFKETFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 193 GSANVKILNSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGT 270
Cdd:cd06320 158 KAPGLKLVASQPAdWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAgKTGKVLVVGTDGIPEAKKSIKAGE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489531185 271 ILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYDKENI 315
Cdd:cd06320 238 LTATVAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKDNV 282
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
43-303 |
2.31e-52 |
|
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: 173.15 E-value: 2.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQ-DVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK 121
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 -MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYTKKyideKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSANVKI 199
Cdd:cd06314 81 gIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKK----ALPGGGKVAIITgGLGADNLNERIQGFKDALKGSPGIEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 200 LNSQPGY-DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGTILAMIQQ 277
Cdd:cd06314 157 VDPLSDNdDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAgKVGKVKIVGFDTLPETLQGIKDGVIAATVGQ 236
|
250 260
....*....|....*....|....*.
gi 489531185 278 QPKEMGRLAVEAVVKAIKGEKVEKNI 303
Cdd:cd06314 237 RPYEMGYLSVKLLYKLLKGGKPVPDV 262
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
44-298 |
1.06e-51 |
|
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: 171.34 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 44 IGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQ-DVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEaDAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYtkkyIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSA-NVKI 199
Cdd:pfam13407 81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGEL----LAEALGGKGKVAILSgSPGDPNANERIDGFKKVLKEKYpGIKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 200 LNSQ--PGYDREESLNTVENLIQSNPD-VDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGTILAMI 275
Cdd:pfam13407 157 VAEVegTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAgLAGKVVVTGFDATPEALEAIKDGTIDATV 236
|
250 260
....*....|....*....|...
gi 489531185 276 QQQPKEMGRLAVEAVVKAIKGEK 298
Cdd:pfam13407 237 LQDPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
43-309 |
5.79e-51 |
|
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: 169.65 E-value: 5.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIK-EKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK 121
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKaEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 -MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEytkkYIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSANVKI 199
Cdd:cd06308 81 gIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGE----YIAELLNGKGNVVEIQgLPGSSPAIDRHKGFLEAIAKYPGIKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 200 LNSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFD-LTEEASSGITDGTILAMIq 276
Cdd:cd06308 157 VASQDGdWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAgREKEIKIIGVDgLPEAGEKAVKDGILAATF- 235
|
250 260 270
....*....|....*....|....*....|...
gi 489531185 277 qQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALL 309
Cdd:cd06308 236 -LYPTGGKEAIEAALKILNGEKVPKEIVLPTPL 267
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
43-303 |
6.59e-50 |
|
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: 167.02 E-value: 6.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDP--DQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE 120
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPatEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 KMPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYTKKYIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSA-NVK 198
Cdd:cd20008 81 GIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAELLKASGGGKGKVAIISfQAGSQTLVDREEGFRDYIKEKYpDIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 199 ILNSQPGY-DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKN-KDVKIVGFDLTEEASSGITDGTILAMIQ 276
Cdd:cd20008 161 IVDVQYSDgDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKaGKIVLVGFDSSPDEVALLKSGVIKALVV 240
|
250 260
....*....|....*....|....*...
gi 489531185 277 QQPKEMGRLAVEAVVKAIKGEK-VEKNI 303
Cdd:cd20008 241 QDPYQMGYEGVKTAVKALKGEEiVEKNV 268
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
42-306 |
2.95e-49 |
|
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: 165.48 E-value: 2.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 42 LTIGVSTITLQHQFFIDIDEGIKEKAKE-LGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE 120
Cdd:cd06301 1 IKIGVSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 -KMPVVTVDAVL-NTENITSYVGTVSYDAGKKLGEytkkYIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSANV 197
Cdd:cd06301 81 aGIPLVYVNREPdSKPKGVAFVGSDDIESGELQME----YLAKLLGGKGNIAILDgVLGHEAQILRTEGNKDVLAKYPGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 198 KILNSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNKD-VKIVGFDLTEEASSGITDGTILAMI 275
Cdd:cd06301 157 KIVAEQTAnWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDdILVAGIDATPDALKAMKAGRLDATV 236
|
250 260 270
....*....|....*....|....*....|.
gi 489531185 276 QQQPKEMGRLAVEAVVKAIKGEKVEKNIPVP 306
Cdd:cd06301 237 FQDAAGQGETAVDVAVKAAKGEEVESDIWIP 267
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
43-309 |
6.35e-49 |
|
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: 164.54 E-value: 6.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEytkkYIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSANVKIL 200
Cdd:cd19972 81 IPVIAVDRNPEDAPGDTFIATDSVAAAKELGE----WVIKQTGGKGEIAILHgQLGTTPEVDRTKGFQEALAEAPGIKVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGA-KAALESAKNKDVKIVGFDLTEEASSGITDGTILAMIQQQ 278
Cdd:cd19972 157 AEQTAdWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAaQAVKVAGLDHKIWVVGFDGDVAGLKAVKDGVLDATMTQQ 236
|
250 260 270
....*....|....*....|....*....|.
gi 489531185 279 PKEMGRLAVEAVVKAIKGEKVEKNIPVPALL 309
Cdd:cd19972 237 TQKMGRLAVDSAIDLLNGKAVPKEQLQDAVL 267
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
45-307 |
2.53e-48 |
|
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: 162.79 E-value: 2.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 45 GVSTITlqhqFFIDIDEGIKEKAKELGVKVIVNDPDQ-DVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-M 122
Cdd:cd20007 7 GVTGDP----FYITMQCGAEAAAKELGVELDVQGPPTfDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 PVVTVDAVLNTENI-TSYVGTVSYDAGKKLGEYTKKYIdeklGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSANVKIL 200
Cdd:cd20007 83 KVVTVDTTLGDPSFvLSQIASDNVAGGALAAEALAELI----GGKGKVLVINsTPGVSTTDARVKGFAEEMKKYPGIKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQ-PGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGTILAMIQQQ 278
Cdd:cd20007 159 GVQySENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAgKTGKVKVVGFDASPAQVEQLKAGTIDALIAQK 238
|
250 260
....*....|....*....|....*....
gi 489531185 279 PKEMGRLAVEAVVKAIKGEKVEKNIPVPA 307
Cdd:cd20007 239 PAEIGYLAVEQAVAALTGKPVPKDILTPF 267
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
43-309 |
5.97e-48 |
|
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: 161.69 E-value: 5.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKEL--GVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE 120
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEInpGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 K-MPVVTVDAvlNTENITSYVGTVSYDAGKKLGEytkkYIDEKLGGKSEIAIVTDLKSQIQMQRIDGFKDALKGSANVKI 199
Cdd:cd06321 81 AgIIVVAVDV--AAEGADATVTTDNVQAGYLACE----YLVEQLGGKGKVAIIDGPPVSAVIDRVNGCKEALAEYPGIKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 200 LNSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNKDVKIVGFDLTEEASSGITD--GTILAMIQ 276
Cdd:cd06321 155 VDDQNGkGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSVDGSPEAVAALKRegSPFIATAA 234
|
250 260 270
....*....|....*....|....*....|....
gi 489531185 277 QQPKEMGRLAVEAVVKAIKGEKV-EKNIPVPALL 309
Cdd:cd06321 235 QDPYDMARKAVELALKILNGQEPaPELVLIPSTL 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
43-315 |
7.80e-47 |
|
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: 159.06 E-value: 7.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE-K 121
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYTKKYIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSANVKIL 200
Cdd:cd06319 81 IPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKENGWGGGSVGIIAiPQSRVNGQARTAGFEDALEEAGVEEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQ-PGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGTILAMIQQQ 278
Cdd:cd06319 161 LRQtPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAgRTGDILVVGFDGDPEALDLIKDGKLDGTVAQQ 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 489531185 279 PKEMGRLAVEAVVKAIKGEK-VEKNIPVPALLYDKENI 315
Cdd:cd06319 241 PFGMGARAVELAIQALNGDNtVEKEIYLPVLLVTSENV 278
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
43-306 |
1.37e-46 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 159.10 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE-K 121
Cdd:PRK10653 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQaN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTVSYDAGKKLGeytkKYIDEKLGGKSEIaivtdlksqIQMQRI----------DGFKDAL 191
Cdd:PRK10653 108 IPVITLDRGATKGEVVSHIASDNVAGGKMAG----DFIAKKLGEGAKV---------IQLEGIagtsaarergEGFKQAV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 192 KGSaNVKILNSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNKDVKIVGFDLTEEASSGITDGT 270
Cdd:PRK10653 175 AAH-KFNVLASQPAdFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGIKAVNRGK 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 489531185 271 ILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVP 306
Cdd:PRK10653 254 LAATIAQQPDQIGAIGVETADKVLKGEKVEAKIPVD 289
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
43-312 |
2.31e-46 |
|
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: 157.78 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDP--DQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE 120
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPsrEDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 K-MPVVTVDAVLNTENITSYVGTVSYDAGKKLGeytkKYIDEKLGGKSEIAIVTDLK-SQIQMQRIDGFKDALKGSANVK 198
Cdd:cd20004 81 QgIPVVIIDSDLGGDAVISFVATDNYAAGRLAA----KRMAKLLNGKGKVALLRLAKgSASTTDRERGFLEALKKLAPGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 199 ILNSQP--GYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAK-NKDVKIVGFDLTEEASSGITDGTILAMI 275
Cdd:cd20004 157 KVVDDQyaGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGlAGKVKFIGFDASDLLLDALRAGEISALV 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 489531185 276 QQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYDK 312
Cdd:cd20004 237 VQDPYRMGYLGVKTAVAALRGKPVPKRIDTGVVLVTK 273
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
43-314 |
2.80e-46 |
|
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: 157.96 E-value: 2.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE-K 121
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTE-NITSYVGTVSYDAGKKLGEYTKKYIDEKlGGKSeIAIVTDLKSQIQMQRIDGFKDAL-------KG 193
Cdd:cd06318 81 IPVITVDSALDPSaNVATQVGRDNKQNGVLVGKEAAKALGGD-PGKI-IELSGDKGNEVSRDRRDGFLAGVneyqlrkYG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 194 SANVKILnSQP--GYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGT 270
Cdd:cd06318 159 KSNIKVV-AQPygNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAgMLDKVKVAGADGQKEALKLIKDGK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489531185 271 ILAMIQQQPKEMGRLAVEAVVKAIKGE-KVEKNIPVPALLYDKEN 314
Cdd:cd06318 238 YVATGLNDPDLLGKTAVDTAAKVVKGEeSFPEFTYTPTALITKDN 282
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
43-311 |
4.00e-46 |
|
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: 157.12 E-value: 4.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIV--NDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE 120
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFvgPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 K-MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYTKkyidEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSAN-V 197
Cdd:cd06310 81 KgIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLA----EALGGKGKVAVLSlTAGNSTTDQREEGFKEYLKKHPGgI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 198 KILNSQ-PGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAK-NKDVKIVGFDLTEEASSGITDGTILAMI 275
Cdd:cd06310 157 KVLASQyAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKlSGQIKIVGFDSQEELLDALKNGKIDALV 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 489531185 276 QQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYD 311
Cdd:cd06310 237 VQNPYEIGYEGIKLALKLLKGEEVPKNIDTGAELIT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
52-313 |
1.62e-45 |
|
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: 155.48 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 52 QHQFFIDIDEGIKEKAKELGVKVIVNDPD--QDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVD 128
Cdd:cd20005 10 QHQFWKAVKKGAEQAAKELGVKITFEGPDteSDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKgIPVVTFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 129 AVLNTENITSYVGTVSYDAGKKLGEYTKkyidEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSA-NVKILNSQPGY 206
Cdd:cd20005 90 SGVPSDLPLATVATDNYAAGALAADHLA----ELIGGKGKVAIVAhDATSETGIDRRDGFKDEIKEKYpDIKVVNVQYGV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 207 -DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKN-KDVKIVGFDLTEEASSGITDGTILAMIQQQPKEMGR 284
Cdd:cd20005 166 gDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKlGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGY 245
|
250 260
....*....|....*....|....*....
gi 489531185 285 LAVEAVVKAIKGEKVEKNIPVPALLYDKE 313
Cdd:cd20005 246 KTVKAAVKALKGEEVEKLIDTGAKWYDKD 274
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
43-306 |
1.40e-44 |
|
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: 153.31 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAF-EK 121
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIkAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTVSYDAGKKLGeytkKYIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSANVKIL 200
Cdd:cd19968 81 IPVVTVDRRAEGAAPVPHVGADNVAGGREVA----KFVVDKLPNGAKVIELTgTPGSSPAIDRTKGFHEELAAGPKIKVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQPG-YDREESLNTVENLIQSNP-DVDIIYATAENSVLGAKAALESA--KNKDVKIVGFDLTEEASSGITDGTILAMIQ 276
Cdd:cd19968 157 FEQTGnFERDEGLTVMENILTSLPgPPDAIICANDDMALGAIEAMRAAglDLKKVKVIGFDAVPDALQAIKDGELYATVE 236
|
250 260 270
....*....|....*....|....*....|
gi 489531185 277 QQPKEMGRLAVEAVVKAIKGEKVEKNIPVP 306
Cdd:cd19968 237 QPPGGQARTALRILVDYLKDKKAPKKVNLK 266
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-312 |
2.49e-44 |
|
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: 152.75 E-value: 2.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 61 EGIKEKAKELGVKVIVNDP--DQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLNTENIT 137
Cdd:cd20006 21 SGAEAAAKEYGVDLEFLGPesEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAgIPVITIDSPVNSKKAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 138 SYVGTVSYDAGKKLGEYTKKYIDEKlggkSEIAIVTDLK-SQIQMQRIDGFKDALKGSANVKILNSQPGY-DREESLNTV 215
Cdd:cd20006 101 SFVATDNYEAGKKAGEKLASLLGEK----GKVAIVSFVKgSSTAIEREEGFKQALAEYPNIKIVETEYCDsDEEKAYEIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 216 ENLIQSNPDVDIIYATAENSVLGAKAALESAKNKD-VKIVGFDLTEEASSGITDGTILAMIQQQPKEMGRLAVEAVVKAI 294
Cdd:cd20006 177 KELLSKYPDINGIVALNEQSTLGAARALKELGLGGkVKVVGFDSSVEEIQLLEEGIIDALVVQNPFNMGYLSVQAAVDLL 256
|
250
....*....|....*...
gi 489531185 295 KGEKVEKNIPVPALLYDK 312
Cdd:cd20006 257 NGKKIPKRIDTGSVVITK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
43-288 |
2.00e-41 |
|
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: 145.17 E-value: 2.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVN-DPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE- 120
Cdd:cd19969 1 YYVMVTFKSGHPYWDDVKEGFEDAGAELGVKTEYTgPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 KMPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYtkkyIDEKLGGKSEIAIVTDLKSQIQMQRIDGFKDALKGSANVKIL 200
Cdd:cd19969 81 GIPVVTFDSDAPESKRISYVGTDNYEAGYAAAEK----LAELLGGKGKVAVLTGPGQPNHEERVEGFKEAFAEYPGIEVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQPGY-DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAAL-ESAKNKDVKIVGFDLTEEASSGITDGTILAMIQQQ 278
Cdd:cd19969 157 AVGDDNdDPEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVrEAGKTGKVKIVAFDDDPETLDLIKDGVIDASIAQR 236
|
250
....*....|
gi 489531185 279 PKEMGRLAVE 288
Cdd:cd19969 237 PWMMGYWSLQ 246
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
43-309 |
2.28e-40 |
|
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: 142.39 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKE-LGVKVIVN--DPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAF 119
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEaNGYELLVKgiKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 120 E-KMPVVTVDA-----VLNTENIT-SYVGTVSYDAGKKLGeytkKYIDEKLGGKSEIAIVTDLKSQIQ-MQRIDGFKDAL 191
Cdd:cd19970 81 DaGIAVINIDNrldadALKEGGINvPFVGPDNRQGAYLAG----DYLAKKLGKGGKVAIIEGIPGADNaQQRKAGFLKAF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 192 KgSANVKILNSQPGY-DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDG 269
Cdd:cd19970 157 E-EAGMKIVASQSANwEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAgKAGKVLVVGFDNIPAVRPLLKDG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489531185 270 TILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALL 309
Cdd:cd19970 236 KMLATIDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPVEL 275
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
61-315 |
1.79e-35 |
|
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: 130.05 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 61 EGIKEKAKELGVKVI-VNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE---KMpVVTVDAVLNTENI 136
Cdd:cd06316 19 AGIKDTFEELGIEVVaVTDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADagiKL-VFMDNVPDGLEAG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 137 TSYVGTVSYDAgKKLGEYTKKYIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALK-GSANVKILNSQPGYDREESLNT 214
Cdd:cd06316 98 KDYVSVVSSDN-RGNGQIAAELLAEAIGGKGKVGIIYhDADFYATNQRDKAFKDTLKeKYPDIKIVAEQGFADPNDAEEV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 215 VENLIQSNPDVDIIYATAENSVLGAKAALESAKNKDVKIVGFDLTEEASSGITDGTILAMI-QQQPKEMGRLAVEAVVKA 293
Cdd:cd06316 177 ASAMLTANPDIDGIYVSWDTPALGVISALRAAGRSDIKITTVDLGTEIALDMAKGGNVKGIgAQRPYDQGVAEALAAALA 256
|
250 260
....*....|....*....|..
gi 489531185 294 IKGEKVEKNIPVPALLYDKENI 315
Cdd:cd06316 257 LLGKEVPPFIGVPPLAVTKDNL 278
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
65-319 |
2.59e-35 |
|
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: 129.67 E-value: 2.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 65 EKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLNTENITSYVGTV 143
Cdd:cd19996 26 AKLKKLIKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAgIPVVLFDSGVGSDKYTAFVGVD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 144 SYDAGKKLGEytkkYIDEKLGGKSEIAIVTDLK-SQIQMQRIDGFKDALKGSANVKILNSQ-PGYDREESLNTVENLIQS 221
Cdd:cd19996 106 DAAFGRVGAE----WLVKQLGGKGNIIALRGIAgVSVSEDRWAGAKEVFKEYPGIKIVGEVyADWDYAKAKQAVESLLAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 222 NPDVDIIYATAENSVLGAKAALESAKNKDVKIVGfdlteEASSG-------ITDGTILAMIqqQPKEMGRLAVEAVVKAI 294
Cdd:cd19996 182 YPDIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTG-----EDNNGflkawkeLPGFKSIAPS--YPPWLGATALDAALAAL 254
|
250 260
....*....|....*....|....*
gi 489531185 295 KGEKVEKNIPVPALLYDKENIKDFK 319
Cdd:cd19996 255 EGEPVPKYVYIPLPVITDENLDQYV 279
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
43-309 |
5.57e-35 |
|
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: 128.21 E-value: 5.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENI-TSYVGTVSYDAGKKLGEYTKKYIDEKLGGKSEIAIVTDLKSQIqmqRIDGFKDALKGSANVKIL 200
Cdd:cd19967 81 IPVFLIDREINAEGVaVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTNAQL---RSQGFHSVIDQYPELKMV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQ-PGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGTILAMIQQQ 278
Cdd:cd19967 158 AQQsADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAgRAGDVIIVGFDGSNDVRDAIKEGKISATVLQP 237
|
250 260 270
....*....|....*....|....*....|...
gi 489531185 279 PKEMGRLAVEAVVKAIKGEK--VEKNIPVPALL 309
Cdd:cd19967 238 AKLIARLAVEQADQYLKGGStgKEEKQLFDCVL 270
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
43-309 |
2.34e-34 |
|
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: 126.16 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDP--DQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE 120
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAggYTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 K-MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYTKKYIDeklGGKSEIAIVTDLK-SQIQMQRIDGFKDALKGSaNVK 198
Cdd:cd06306 81 AgIPVIDLVNGIDSPKVAARVLVDFYDMGYLAGEYLVEHHP---GKPVKVAWFPGPAgAGWAEDREKGFKEALAGS-NVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 199 ILNSQPG-YDREESLNTVENLIQSNPDVDIIYATAEnSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGTILAMIQ 276
Cdd:cd06306 157 IVATKYGdTGKAVQLNLVEDALQAHPDIDYIVGNAV-AAEAAVGALREAgLTGKVKVVSTYLTPGVYRGIKRGKILAAPS 235
|
250 260 270
....*....|....*....|....*....|...
gi 489531185 277 QQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALL 309
Cdd:cd06306 236 DQPVLQGRIAVDQAVRALEGKPVPKHVGPPILV 268
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
44-314 |
7.46e-33 |
|
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: 122.69 E-value: 7.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 44 IGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-M 122
Cdd:cd19992 2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAgV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 PVVTVDAVLNTENITSYVGTVSYDAGKKLGeytkKYIDEKlGGKSEIAIVTDLKSQIQMQRI-DGFKDALK---GSANVK 198
Cdd:cd19992 82 PVISYDRLILNADVDLYVGRDNYKVGQLQA----EYALEA-VPKGNYVILSGDPGDNNAQLItAGAMDVLQpaiDSGDIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 199 ILNSQ--PGYDREESLNTVEN-LIQSNPDVDIIYATAENSVLGAKAALESAK-NKDVKIVGFDLTEEASSGITDGTILAM 274
Cdd:cd19992 157 IVLDQyvKGWSPDEAMKLVENaLTANNNNIDAVLAPNDGMAGGAIQALKAQGlAGKVFVTGQDAELAALKRIVEGTQTMT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489531185 275 IQQQPKEMGRLAVEAVVKAIKGEKVEKN--------IPVPALLYDKEN 314
Cdd:cd19992 237 VWKDLKELARAAADAAVKLAKGEKPQTTdetinnggKDVPAILIPGVL 284
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
55-288 |
2.19e-32 |
|
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: 121.19 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 55 FFIDIDEGIKEKAKELGVKVIV-NDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDA--V 130
Cdd:cd06312 14 FWSVVKKGAKDAAKDLGVTVQYlGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAgIPVIAINSgdD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 131 LNTENI--TSYVGTVSYDAGKKLGEYTKKyidekLGGKSEIAIVTDLKSQIQMQRIDGFKDALKGsANVKILNSQPGYDR 208
Cdd:cd06312 94 RSKERLgaLTYVGQDEYLAGQAAGERALE-----AGPKNALCVNHEPGNPGLEARCKGFADAFKG-AGILVELLDVGGDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 209 EESLNTVENLIQSNPDVDIIYA-TAENSVLGAKAALESAKNKDVKIVGFDLTEEASSGITDGTILAMIQQQPKEMGRLAV 287
Cdd:cd06312 168 TEAQEAIKAYLQADPDTDAVLTlGPVGADPALKAVKEAGLKGKVKIGTFDLSPETLEAIKDGKILFAIDQQPYLQGYLAV 247
|
.
gi 489531185 288 E 288
Cdd:cd06312 248 V 248
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
43-295 |
9.90e-31 |
|
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: 117.18 E-value: 9.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIV--NDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE 120
Cdd:cd19973 1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTaaGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 K-MPVVTVDAVLNTENIT-SYVGTVSYDAGKKLGEYTKKyideKLGGKSEIAIVTDLKSQIQM--QRIDGFkdaLKG--- 193
Cdd:cd19973 81 AgVLVIALDTPTDPIDAAdATFATDNFKAGVLIGEWAKA----ALGAKDAKIATLDLTPGHTVgvLRHQGF---LKGfgi 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 194 ----------SANVKILNSQPGY-DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEE 261
Cdd:cd19973 154 dekdpesnedEDDSQVVGSADTNgDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAgKEKGVLIVSVDGGCP 233
|
250 260 270
....*....|....*....|....*....|....
gi 489531185 262 ASSGITDGTILAMIQQQPKEMGRLAVEAVVKAIK 295
Cdd:cd19973 234 GVKDVKDGIIGATSQQYPLRMAALGVEAIAAFAK 267
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
54-315 |
8.69e-30 |
|
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: 115.07 E-value: 8.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 54 QFFIDIDEGIKEKAKELGVKVIVNDP-DQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVL 131
Cdd:cd20003 12 PYFTAAGQGAQEAAKELGVDVTYDGPtEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKgIKVVTWDSDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 132 NTENITSYVGTVSYDAgkkLGEYTKKYIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGS-ANVKILNSQPGY-DR 208
Cdd:cd20003 92 NPDARDFFVNQATPEG---IGKTLVDMVAEQTGEKGKVAIVTsSPTATNQNAWIKAMKAYIAEKyPDMKIVTTQYGQeDP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 209 EESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNK-DVKIVGFDLTEEASSGITDGTILAMIQQQPKEMGRLAV 287
Cdd:cd20003 169 AKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTgKVAVTGLSTPNVMRPYVKDGTVKSVVLWDVVDLGYLAV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489531185 288 EAVVKAIKGE----------------KVEKN-----IPVPALLYDKENI 315
Cdd:cd20003 249 YVARALADGTllkvgdffvagrlgtfTVVPKgngiiLLGEPLIFTKENI 297
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
43-309 |
1.10e-28 |
|
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: 111.23 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSyvgTVSYDAGkkLGEYTKKYIDEKLGGKSEIAIVTDLKSQIQMQRIDGFKDALKgsANVKILN 201
Cdd:cd06305 81 IPVVTFDTDSQVPGVNN---ITQDDYA--LGTLSLGQLVKDLNGEGNIAVFNVFGVPPLDKRYDIYKAVLK--ANPGIKK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 202 SQPGYD------REESLNTVENLIQSNPD--VDIIYATAENSVLGAKAALESAKNKDVKIVGFDLTEEASSGITD--GTI 271
Cdd:cd06305 154 IVAELGdvtpntAADAQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISNQDLELMADegSPW 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 489531185 272 LAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALL 309
Cdd:cd06305 234 VATAAQDPALIGTVAVRNVARKLAGEDLPDKYSLVPVL 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
43-305 |
2.30e-28 |
|
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: 110.53 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYtkkyIDEKLGGKSEIAIVTDLKSQ-IQMQRIDGFKDALKGSANVKIL 200
Cdd:cd06311 81 IPVVNFDRGLNVLIYDLYVAGDNPGMGVVSAEY----IGKKLGGKGNVVVLEVPSSGsVNEERVAGFKEVIKGNPGIKIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNKDVK-IVGFDLTEEASSGITDG--TILAMIQ 276
Cdd:cd06311 157 AMQAGdWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIKvMTGGGGSQEYFKRIMDGdpIWPASAT 236
|
250 260 270
....*....|....*....|....*....|..
gi 489531185 277 QQPKeMGRLAVE---AVVKAIKGEKVEKNIPV 305
Cdd:cd06311 237 YSPA-MIADAIKlavLILKGGKTVEKEVIIPS 267
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
43-313 |
2.17e-27 |
|
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: 107.61 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVlGTDNSAIVPAVEgafEKM 122
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIIL-GSHSLDIEEYKK---LNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 PVVTVDAVLNtENItSYVGTVSYDAGKKLGEY-TKKyideklgGKSEIAIVT-DLKSQIQMQRIDGFKDALK--GSANVK 198
Cdd:cd06291 77 PIVSIDRYLS-EGI-PSVSSDNYQGGRLAAEHlIEK-------GCKKILHIGgPSNNSPANERYRGFEDALKeaGIEYEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 199 ILNSQPGYDREESLNTVENLIQSNPDVDIIYATAENSVLGA-KAALESAKN--KDVKIVGFD---LTEEASSGITdgtil 272
Cdd:cd06291 148 IEIDENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVlKALQKLGIRvpEDVQIIGFDgieISELLYPELT----- 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489531185 273 aMIQQQPKEMGRLAVEAVVKAIKGEKV-EKNIPVPALLYDKE 313
Cdd:cd06291 223 -TIRQPIEEMAKEAVELLLKLIEGEEIeESRIVLPVELIERE 263
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
61-315 |
2.31e-27 |
|
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: 108.48 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 61 EGIKEKAKELGVKVIVNDPDQ-DVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLNTENITS 138
Cdd:cd06302 19 EGAKKAAKELGVEVVYTGPTQaDAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAgIKVITWDSDAPPSARDY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 139 YVGTVSYdagKKLGEYTKKYIDEKLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSANV-KILNSQPGY-DREESLNTV 215
Cdd:cd06302 99 FVNQADD---EGLGEALVDSLAKEIGGKGKVAILSgSLTATNLNAWIKAMKEYLKSKYPDiELVDTYYTDdDQQKAYTQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 216 ENLIQSNPDVDIIYATAENSVLG-AKAALESAKNKDVKIVGFDLTEEASSGITDGTILAMIQQQPKEMGRLAVEAVVKAI 294
Cdd:cd06302 176 QNLIQAYPDLKGIIGVSTTAPPAaAQAVEEAGKTGKVAVTGIGLPNTARPYLKDGSVKEGVLWDPAKLGYLTVYAAYQLL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489531185 295 KGE---KVEKNIPV----------------PALLYDKENI 315
Cdd:cd06302 256 KGKgftEDSDDVGTggkvkvdvaggeillgPPLVFTKDNV 295
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
43-300 |
2.90e-27 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 108.75 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNS-AIVPAVEGAfeK 121
Cdd:COG1609 63 TIGVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDdARLERLAEA--G 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENItSYVGTVSYDAGKKLGEYtkkYIDeklGGKSEIAIVT-DLKSQIQMQRIDGFKDALKgSANVKIL 200
Cdd:COG1609 141 IPVVLIDRPLPDPGV-PSVGVDNRAGARLATEH---LIE---LGHRRIAFIGgPADSSSARERLAGYREALA-EAGLPPD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NS---QPGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAK---NKDVKIVGFD---LTEEASSGITdgti 271
Cdd:COG1609 213 PElvvEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGlrvPEDVSVVGFDdipLARYLTPPLT---- 288
|
250 260
....*....|....*....|....*....
gi 489531185 272 laMIQQQPKEMGRLAVEAVVKAIKGEKVE 300
Cdd:COG1609 289 --TVRQPIEEMGRRAAELLLDRIEGPDAP 315
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
50-299 |
3.73e-27 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 108.04 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 50 TLQHQFFIDIDEGIKEKAKELGVKV--IVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVT 126
Cdd:PRK09701 33 TLSNPFWVDMKKGIEDEAKTLGVSVdiFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKgIYLVN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 127 VDAVLNTENITSYVGTV----SYDaGKKLGEYTKKYIDEKLGGKS-EIAIVTDLKSQIQMQ-RIDGFKDALKGSANVKIL 200
Cdd:PRK09701 113 LDEKIDMDNLKKAGGNVeafvTTD-NVAVGAKGASFIIDKLGAEGgEVAIIEGKAGNASGEaRRNGATEAFKKASQIKLV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA-KNKDVKIVGFDLTEEASSGITDGTILAMIQQQ 278
Cdd:PRK09701 192 ASQPAdWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAgKTGKVLVVGTDGIPEARKMVEAGQMTATVAQN 271
|
250 260
....*....|....*....|.
gi 489531185 279 PKEMGRLAVEAVVKAIKGEKV 299
Cdd:PRK09701 272 PADIGATGLKLMVDAEKSGKV 292
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
43-309 |
1.17e-26 |
|
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: 105.68 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAfEKM 122
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLA-AGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 PVVTVDAVLNTENItSYVGTVSYDAGKKLGEY-TKKyideklgGKSEIAIVT-DLKSQIQMQRIDGFKDALKgSANVKIL 200
Cdd:cd06267 80 PVVLIDRRLDGLGV-DSVVVDNYAGAYLATEHlIEL-------GHRRIAFIGgPLDLSTSRERLEGYRDALA-EAGLPVD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NS---QPGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAK---NKDVKIVGFD---LTEEASSGITdgTi 271
Cdd:cd06267 151 PElvvEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGlrvPEDISVVGFDdipLAALLTPPLT--T- 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 489531185 272 lamIQQQPKEMGRLAVEAVVKAIKGEKVE-KNIPVPALL 309
Cdd:cd06267 228 ---VRQPAYEMGRAAAELLLERIEGEEEPpRRIVLPTEL 263
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
55-287 |
1.68e-25 |
|
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: 102.74 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 55 FFIDIDEGIKEKAKELGVKVIVNDP-DQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDA-VL 131
Cdd:cd19965 13 FFQPVKKGMDDACELLGAECQFTGPqTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAgIPVVAFNVdAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 132 NTENI-TSYVGTVSYDAGKKLGEYTKKYIDEKlGGKSEIAIVTDLKSQIQmQRIDGFKDALKGSA-NVKILNSQPGYDRE 209
Cdd:cd19965 93 GGENArLAFVGQDLYPAGYVLGKRIAEKFKPG-GGHVLLGISTPGQSALE-QRLDGIKQALKEYGrGITYDVIDTGTDLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489531185 210 ESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNKD-VKIVGFDLTEEASSGITDGTILAMIQQQPKEMGRLAV 287
Cdd:cd19965 171 EALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGkVLVGGFDLVPEVLQGIKAGYIDFTIDQQPYLQGFYPV 249
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
54-318 |
2.33e-24 |
|
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: 100.06 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 54 QFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTD---NSAIVPAVEGAfeKMPVVTVDAV 130
Cdd:cd01540 12 PWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDqklGPAIAAKAKAA--GIPVIAVDDQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 131 LNTE---NITSYVGTVSYDAGKKLGEYTKKYIDEK---LGGKSEIAIVTDLKSQIQMQRIDGFKDALK--GSANVKILNS 202
Cdd:cd01540 90 LVDAdpmKIVPFVGIDAYKIGEAVGEWLAKEMKKRgwdDVKEVGVLAITMDTLSVCVDRTDGAKDALKaaGFPEDQIFQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 203 -QPGYDREESLNTVENLIQSNPDVD--IIYATAENSVLGAKAALESA-KNKD----VKIVGFDLTEEASSGITDGTILAM 274
Cdd:cd01540 170 pYKGTDTEGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAgFDAEdiigVGIGGYLAADEEFKKQPTGFKASL 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489531185 275 IqQQPKEMGRLAVEAVVKAIK-GEKVEKNIPVPALLYDKENIKDF 318
Cdd:cd01540 250 Y-ISPDKHGYIAAEELYNWITdGKPPPAETLTDGVIVTRDNYKEV 293
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
43-301 |
3.22e-24 |
|
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: 99.26 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVL--GTDNSAIVPAVEgafE 120
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILApsAGPSRELKRLLK---H 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 KMPVVTVDAVLNTENITSyVGTVSYDAGKKLgeyTKKYIDekLGGKsEIAIVTDLKSQIQM-QRIDGFKDALKgSANVKI 199
Cdd:cd06280 78 GIPIVLIDREVEGLELDL-VAGDNREGAYKA---VKHLIE--LGHR-RIGLITGPLEISTTrERLAGYREALA-EAGIPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 200 ---LNSQPGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNK---DVKIVGFDLTEEASsgITDGTILA 273
Cdd:cd06280 150 desLIFEGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEipqDISVVGFDDSDWFE--IVDPPLTV 227
|
250 260
....*....|....*....|....*...
gi 489531185 274 mIQQQPKEMGRLAVEAVVKAIKGEKVEK 301
Cdd:cd06280 228 -VAQPAYEIGRIAAQLLLERIEGQGEEP 254
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
44-306 |
1.12e-23 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 98.11 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 44 IGVSTITLQH---QFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFE 120
Cdd:cd01391 2 IGVVTSSLHQireQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNLAQLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 KMPVVTVDAV---LNTENITSYVGTVSYD---AGKKLGEYTKKYideklgGKSEIAIVTDLKSQIQMQRIDGFKDALKgS 194
Cdd:cd01391 82 DIPQLALDATsqdLSDKTLYKYFLSVVFSdtlGARLGLDIVKRK------NWTYVAAIHGEGLNSGELRMAGFKELAK-Q 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 195 ANVKILNSQPGYDR--EESLNTVENLIQSNPDVDIIYATAENSVLGA-KAALESAKNKDVKIVGFDLTEEASSG--ITDG 269
Cdd:cd01391 155 EGICIVASDKADWNagEKGFDRALRKLREGLKARVIVCANDMTARGVlSAMRRLGLVGDVSVIGSDGWADRDEVgyEVEA 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 489531185 270 TILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVP 306
Cdd:cd01391 235 NGLTTIKQQKMGFGITAIKAMADGSQNMHEEVWFDEK 271
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
43-302 |
1.60e-23 |
|
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380632 [Multi-domain] Cd Length: 264 Bit Score: 97.22 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSA--IVPAVEgafE 120
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEdlIEKLVK---S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 KMPVVTVDAVLNtENITSYVGTVSYDAGKKLGEYtkkYIDEklgGKSEIAIVTDLKSQIQMQ-RIDGFKDALKgsaNVKI 199
Cdd:cd19977 78 GIPVVFVDRYIP-GLDVDTVVVDNFKGAYQATEH---LIEL---GHKRIAFITYPLELSTRQeRLEGYKAALA---DHGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 200 LNSQP----GYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNK---DVKIVGFDLTEEAS---SGITdg 269
Cdd:cd19977 148 PVDEElikhVDRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRipdDIALIGFDDIPWADlfnPPLT-- 225
|
250 260 270
....*....|....*....|....*....|...
gi 489531185 270 tilaMIQQQPKEMGRLAVEAVVKAIKGEKVEKN 302
Cdd:cd19977 226 ----VIAQPTYEIGRKAAELLLDRIENKPKGPP 254
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
51-319 |
2.32e-23 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 98.10 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 51 LQHQFFIDIDEGIKEKAKELGVKVIVNDPD--QDVAKQTSAIEDFIQQNVDGmIVLGT-DNSAIVPAVEGAFEKMPVVTV 127
Cdd:PRK10936 56 LKDSYWLSVNYGMVEEAKRLGVDLKVLEAGgyYNLAKQQQQLEQCVAWGADA-ILLGAvTPDGLNPDLELQAANIPVIAL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 128 DAVLNTENITSYVGTVSYDAGKKLGEYTKKYiDEKLGGKSEIAIV--------TDLKSQiqmqridGFKDALKGSAnVKI 199
Cdd:PRK10936 135 VNGIDSPQVTTRVGVSWYQMGYQAGRYLAQW-HPKGSKPLNVALLpgpegaggSKAVEQ-------GFRAAIAGSD-VRI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 200 LNSQPG-YDREESLNTVENLIQSNPDVDIIYATAensvLGAKAA---LESAKNKD-VKIVGFDLTEEASSGITDGTILAM 274
Cdd:PRK10936 206 VDIAYGdNDKELQRNLLQELLERHPDIDYIAGSA----VAAEAAigeLRGRNLTDkIKLVSFYLSHQVYRGLKRGKVLAA 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489531185 275 IQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYDKENIKDFK 319
Cdd:PRK10936 282 PSDQMVLQGRLAIDQAVRQLEGAPVPGDVGPKILVLTPKNLDSED 326
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
53-310 |
4.20e-23 |
|
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.
Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 96.48 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 53 HQFFIDIDEGIKEKAKEL---GVKVIVND-PDQDVAKQTSAIEDfIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTV 127
Cdd:cd06307 11 NPFYELLRRAIEAAAAALrdrRVRLRIHFvDSLDPEALAAALRR-LAAGCDGVALVAPDHPLVRAAIDELAARgIPVVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 128 DAVLNTENITSYVGTVSYDAGKKLGEYTKKYIdekLGGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSA-NVKILNSQPG 205
Cdd:cd06307 90 VSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFL---GRRPGKVLVILgSHRFRGHEEREAGFRSVLRERFpDLTVLEVLEG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 206 YD-REESLNTVENLIQSNPDVDIIY-ATAENSvlGAKAALESA-KNKDVKIVGFDLTEEASSGITDGTILAMIQQQPKEM 282
Cdd:cd06307 167 LDdDELAYELLRELLARHPDLVGIYnAGGGNE--GIARALREAgRARRVVFIGHELTPETRRLLRDGTIDAVIDQDPELQ 244
|
250 260
....*....|....*....|....*....
gi 489531185 283 GRLAVEAVVKAIKG-EKVEKNIPVPALLY 310
Cdd:cd06307 245 ARRAIEVLLAHLGGkGPAPPQPPIPIEII 273
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
43-305 |
4.74e-22 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 93.70 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAF-EK 121
Cdd:cd19993 1 VVGVSWSNFQEERWKTDEAAMKKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAaEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTEnITSYVGTVSYDAGKKLGEYTKKYIDE----KLGGKSEIAIvTDLKSQIQMQRIdgfKDALKgSANV 197
Cdd:cd19993 81 IPVIAYDRLIENP-IAFYISFDNVEVGRMQARGVLKAKPEgnyvFIKGSPTDPN-ADFLRAGQMEVL---QPAID-SGKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 198 KILNSQ--PGYDREESLNTVEN-LIQSNPDVDIIYATAENSVLGAKAALESAK-NKDVKIVGFDLTEEASSGITDGTILA 273
Cdd:cd19993 155 KIVGEQytDGWKPANAQKNMEQiLTANNNKVDAVVASNDGTAGGAVAALAAQGlAGKVPVSGQDADKAALNRIALGTQTV 234
|
250 260 270
....*....|....*....|....*....|..
gi 489531185 274 MIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPV 305
Cdd:cd19993 235 TVWKDARELGKEAAEIAVELAKGTKIEAIKGA 266
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
55-297 |
1.37e-21 |
|
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380655 Cd Length: 298 Bit Score: 92.70 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 55 FFIDIDEGIKEKAKELGVKVIVNDPDQ-DVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLN 132
Cdd:cd20000 13 YFDAARDGAKEAAKELGGELIFVGPTTaTAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAAgIKVVTFDSDVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 133 TENITSYVGTVSYDAgkkLGEYTKKYIDEKLGGKSEIAIVTDlKSQIQMQR--IDGFKDALKGSANVKILNSQPGY---D 207
Cdd:cd20000 93 PEARDLFVNQADADG---IGRAQVDMMAELIGGEGEFAILSA-TPTATNQNawIDAMKKELASPEYAGMKLVKVAYgddD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 208 REESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNKD-VKIVGFDLTEEASSGITDGTILAMIQQQPKEMGRLA 286
Cdd:cd20000 169 AQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGkVKVTGLGLPSEMAKYVKDGTVPAFALWNPIDLGYLA 248
|
250
....*....|.
gi 489531185 287 VEAVVKAIKGE 297
Cdd:cd20000 249 AYAAAALAQGE 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
53-273 |
2.41e-20 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 89.59 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 53 HQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQN--VDGMIVLGTDNSA--IVPAVEGAfeKMPVVTVD 128
Cdd:cd06324 12 EPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARPpkPDYLILVNEKGVApeLLELAEQA--KIPVFLIN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 129 AVL----------NTENITSYVGTVSYD---AGKKLGEY-TKKYIDEKLGGKSE-IAIVTDLKSQIQMQRIDGFKDALKG 193
Cdd:cd06324 90 NDLtdeerallgkPREKFKYWLGSIVPDneqAGYLLAKAlIKAARKKSDDGKIRvLAISGDKSTPASILREQGLRDALAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 194 SANVKILNSQPGY-DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAK---NKDVKIVGFDLTEEASSGITDG 269
Cdd:cd06324 170 HPDVTLLQIVYANwSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGlkpGKDVLVGGIDWSPEALQAVKDG 249
|
....
gi 489531185 270 TILA 273
Cdd:cd06324 250 ELTA 253
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
54-287 |
8.82e-20 |
|
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: 87.38 E-value: 8.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 54 QFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTD-NSAIVPAVEGAFEK-MPVVTVDAVL 131
Cdd:cd19966 13 PFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPgDGAYTPLIEAAKKAgIIVTSFNTDL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 132 ----NTENITSYVGTVSYDAGKKLGEYTKKYIDEKLGgkSEIAIVTDLKSQI-QMQRIDGFKDALK-GSANVKILNSQPG 205
Cdd:cd19966 93 pkleYGDCGLGYVGADLYAAGYTLAKELVKRGGLKTG--DRVFVPGLLPGQPyRVLRTKGVIDALKeAGIKVDYLEISLE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 206 -YDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESA--KNKDVKIVGFDLTEEASSGITDGTILAMIQQQPKEM 282
Cdd:cd19966 171 pNKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAgkKPGEIPVAGFDLSPATVQAIKSGYVNATIDQQPYLQ 250
|
....*
gi 489531185 283 GRLAV 287
Cdd:cd19966 251 GYLPV 255
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
43-306 |
1.89e-19 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380513 [Multi-domain] Cd Length: 267 Bit Score: 86.13 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVpaVEGAFEKM 122
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEEL--LKLLAEGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 PVVTVD--------AVLNTENitsYVGTvsYDAGKKLGEYtkkyideklgGKSEIAIVTDLKSQIQMQ-RIDGFKDALKg 193
Cdd:cd06290 79 PVVLVDreleglnlPVVNVDN---EQGG--YNATNHLIDL----------GHRRIVHISGPEDHPDAQeRYAGYRRALE- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 194 SANVKILNS--QPGYDREES-LNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNK---DVKIVGFDLTEEASSgit 267
Cdd:cd06290 143 DAGLEVDPRliVEGDFTEESgYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRvpdDVSVIGFDDLPFSKY--- 219
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489531185 268 dgTI--LAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVP 306
Cdd:cd06290 220 --TTppLTTVRQPLYEMGKTAAEILLELIEGKGRPPRRIIL 258
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
51-300 |
2.07e-19 |
|
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380507 [Multi-domain] Cd Length: 267 Bit Score: 86.05 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 51 LQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGT--------DNSAIVPAVEgAFEKM 122
Cdd:cd06284 9 ISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGrldaellsELSKRYPIVQ-CCEYI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 PVVTVdavlntenitSYVGTVSYDAGKKLGEYtkkYIDEklgGKSEIAIVT-DLKSQIQMQRIDGFKDALK--GSANVKI 199
Cdd:cd06284 88 PDSGV----------PSVSIDNEAAAYDATEY---LISL---GHRRIAHINgPLDNVYARERLEGYRRALAeaGLPVDED 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 200 LNSQPGYDREESLNTVENLIQSNPDVDIIYATAENSVLGA-KAALESAKN--KDVKIVGFDLTEEA---SSGITdgTIla 273
Cdd:cd06284 152 LIIEGDFSFEAGYAAARALLALPERPTAIFCASDELAIGAiKALRRAGLRvpEDVSVIGFDDIEFAemfSPSLT--TI-- 227
|
250 260
....*....|....*....|....*...
gi 489531185 274 miqQQPK-EMGRLAVEAVVKAIKGEKVE 300
Cdd:cd06284 228 ---RQPRyEIGETAAELLLEKIEGEGVP 252
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
43-300 |
2.55e-19 |
|
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: 86.18 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQ-DVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK 121
Cdd:cd20001 1 TIAVVVKVTGIAWFDRMETGVEQFAKDTGVNVYQIGPATaDAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 -MPVVTVDAvlntenitSYVGTVSYDA----GKKLGEYTKKYIDEKLGGKSE-IAIVTDLKSQIQMQRIDGFKDALKgSA 195
Cdd:cd20001 81 gIVVITHEA--------SNLKNVDYDVeafdNAAYGAFIMDKLAEAMGGKGKyVTFVGSLTSTSHMEWANAAVAYQK-AN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 196 NVKILNSQPGYDREESLNT----VENLIQSNPDVDIIYATAENSVLGAKAALESAKNKD-VKIVGFDLTEEASSGITDGT 270
Cdd:cd20001 152 YPDMLLVTDRVETNDDSETayekAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGkIAVVGTGLPSVAGEYLEDGT 231
|
250 260 270
....*....|....*....|....*....|
gi 489531185 271 ILAMIQQQPKEMGRLAVEAVVKAIKGEKVE 300
Cdd:cd20001 232 IDYIQFWDPADAGYAMNALAVMVLEGEKIT 261
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
61-306 |
1.07e-18 |
|
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380484 [Multi-domain] Cd Length: 259 Bit Score: 83.70 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 61 EGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTdnsAIVPAVEGAFEKM--PVVTVDavLNTENITS 138
Cdd:cd01542 19 EGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFAT---EITDEHRKALKKLkiPVVVLG--QEHEGFSC 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 139 yvgtVSYD---AGKKLGEYTKKYideklgGKSEIAI--VTDLKSQIQMQRIDGFKDALKGSANVKILNSQPGYDREESLN 213
Cdd:cd01542 94 ----VYHDdygAGKLLGEYLLKK------GHKNIAYigVDEEDIAVGVARKQGYLDALKEHGIDEVEIVETDFSMESGYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 214 TVENLIQSNPDVDIIYATaENSVLGA-KAALESAKN--KDVKIVGF---DLTEEASSGITdgTilamIQQQPKEMGRLAV 287
Cdd:cd01542 164 AAKELLKENKPDAIICAT-DNIALGAiKALRELGIKipEDISVAGFggyDLSEFVSPSLT--T----VKFDYEEAGEKAA 236
|
250
....*....|....*....
gi 489531185 288 EAVVKAIKGEKVEKNIPVP 306
Cdd:cd01542 237 ELLLDMIEGEKVPKKQKLP 255
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
63-317 |
2.30e-18 |
|
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: 83.53 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 63 IKEKAKELGVK-----VIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLNTENi 136
Cdd:cd06300 21 LKADAAQSGQKglvkeLIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAgIPVVAFDGAVTSPD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 137 tSYVGTVSYdagKKLGEYTKKYIDEKLGGKSEIAIVTDLK-SQIQMQRIDGFKDALKGSANVKILNS-QPGYDREESLNT 214
Cdd:cd06300 100 -AYNVSNDQ---VEWGRLGAKWLFEALGGKGNVLVVRGIAgAPASADRHAGVKEALAEYPGIKVVGEvFGGWDEATAQTA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 215 VENLIQSNPDVDIIYATAENSvLGAKAALESAKNKDVKIVGFDLTEEASSGITD---GTILAMIQQQPKEMGrLAVEAVV 291
Cdd:cd06300 176 MLDFLATHPQVDGVWTQGGED-TGVLQAFQQAGRPPVPIVGGDENGFAKQWWKHpkkGLTGAAVWPPPAIGA-AGLEVAL 253
|
250 260
....*....|....*....|....*..
gi 489531185 292 KAIKGEK-VEKNIPVPALLYDKENIKD 317
Cdd:cd06300 254 RLLEGQGpKPQSVLLPPPLITNDDAKA 280
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
82-320 |
4.25e-18 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380653 [Multi-domain] Cd Length: 302 Bit Score: 83.11 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 82 DVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLNTENITsyvgTVSYDAgKKLGEYTKKYID 160
Cdd:cd19998 44 DVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAgIVVVAFDNVVDEPCAY----NVNTDQ-AKAGEQTAQWLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 161 EKLGGKSEIAIVTDLK-SQIQMQRIDGFKDALKGSANVKILNSQPG-YDREESLNTVENLIQSNPDVDIIYATAenSVLG 238
Cdd:cd19998 119 DKLGGKGNILMVRGVPgTSVDRDRYEGAKEVFKKYPDIKVVAEYYGnWDDGTAQKAVADALAAHPDVDGVWTQG--GETG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 239 AKAALESAKNKDVKIVGFD--LTEEASSGITDGTILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYDKENIK 316
Cdd:cd19998 197 VIKALQAAGHPLVPVGGEAenGFRKAMLEPLANGLPGISAGSPPALSAVALKLAVAVLEGEKEPKTIELPLPWVTTDDVK 276
|
....
gi 489531185 317 DFKN 320
Cdd:cd19998 277 LCQG 280
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
43-302 |
1.20e-17 |
|
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: 81.31 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAV-EGAFEK 121
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVaEAKAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYvgtVSYDaGKKLGEYTKKYIDEKLGGKSEIAIV-------TDLKSQIQMQRIDGFKDalkgS 194
Cdd:cd01538 81 IKVIAYDRLILNADVDYY---ISFD-NEKVGELQAQALLDAKPEGNYVLIGgsptdnnAKLFRDGQMKVLQPAID----S 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 195 ANVKILNSQ--PGYDREESLNTVENLIQSN-PDVDIIYATAENSVLGAKAALESAK-NKDVKIVGFDLTEEASSGITDGT 270
Cdd:cd01538 153 GKIKVVGDQwvDDWLPANAQQIMENALTANgNNVDAVVASNDGTAGGAIAALKAQGlSGGVPVSGQDADLAAIKRILAGT 232
|
250 260 270
....*....|....*....|....*....|..
gi 489531185 271 ILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKN 302
Cdd:cd01538 233 QTMTVYKDIRLLADAAAEVAVALMRGEKPPIN 264
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
55-301 |
4.14e-17 |
|
ligand-binding domain of putative DNA transcription regulators highly similar to that of the transcription regulator DegA; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the transcription regulator DegA, which is involved in the control of degradation of Bacillus subtilis amidophosphoribosyltransferase (purF). This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380631 [Multi-domain] Cd Length: 268 Bit Score: 79.60 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 55 FFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEKMPVVTVDAVLNTE 134
Cdd:cd19976 13 FFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLLKEEKIPVVVLDRYIEDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 135 NiTSYVGTVSYDAGkklgeYT-KKYIDEKlgGKSEIAIVTDLKS-QIQMQRIDGFKDALKgSANVKILNSQpGYDREESL 212
Cdd:cd19976 93 D-SDSVGVDDYRGG-----YEaTKYLIEL--GHTRIGCIVGPPStYNEHERIEGYKNALQ-DHNLPIDESW-IYSGESSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 213 NT----VENLIQSNPDVDIIyatAENSVLGA---KAALESAKN--KDVKIVGFD---LTEEASSGITdgTIlamiqQQP- 279
Cdd:cd19976 163 EGgykaAEELLKSKNPTAIF---AGNDLIAMgvyRAALELGLKipEDLSVIGFDniiLSEYITPALT--TI-----AQPi 232
|
250 260
....*....|....*....|..
gi 489531185 280 KEMGRLAVEAVVKAIKGEKVEK 301
Cdd:cd19976 233 FEMGQEAAKLLLKIIKNPAKKK 254
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
43-306 |
4.01e-16 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 76.94 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMI--VLGTDNSAIVPAVEGafE 120
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLIltVGDAQGSEALELLEE--E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 KMPVVTvdaVLNTENiTSYVGTVSYD---AGKKLGEYTKkyideKLGGKSeIAIVT-DLK-SQIQMQRIDGFKDALKgSA 195
Cdd:cd06282 79 GVPYVL---LFNQTE-NSSHPFVSVDnrlASYDVAEYLI-----ALGHRR-IAMVAgDFSaSDRARLRYQGYRDALK-EA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 196 NVKILN----SQPGYDREESLNtvENLIQSNPDVDIIyatAEN-----SVLGAKAALESAKNKDVKIVGFDlteeassGI 266
Cdd:cd06282 148 GLKPIPivevDFPTNGLEEALT--SLLSGPNPPTALF---CSNdllalSVISALRRLGIRVPDDVSVIGFD-------GI 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489531185 267 TDGTI----LAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVP 306
Cdd:cd06282 216 AIGELltptLATVVQPSRDMGRAAADLLLAEIEGESPPTSIRLP 259
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
43-296 |
4.12e-16 |
|
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: 76.88 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAvEGAFEKM 122
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQ-ELAARGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 PVVTVD-----AVLNTENITSYVGtvSYDAGKKLgeytkkyidekLG-GKSEIAIVTD-LKSQIQMQRIDGFKDALKgSA 195
Cdd:cd06285 80 PVVLVDrrigdTALPSVTVDNELG--GRLATRHL-----------LElGHRRIAVVAGpLNASTGRDRLRGYRRALA-EA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 196 NVKILNS---QPGYDREESLNTVENLIQSNPDVDIIYATaeNSVLgAKAALESAKN------KDVKIVGFDLTEEAS--- 263
Cdd:cd06285 146 GLPVPDErivPGGFTIEAGREAAYRLLSRPERPTAVFAA--NDLM-AIGVLRAARDlglrvpEDLSVVGFDDIPLAAflp 222
|
250 260 270
....*....|....*....|....*....|....
gi 489531185 264 SGITdgTIlamiqQQPK-EMGRLAVEAVVKAIKG 296
Cdd:cd06285 223 PPLT--TV-----RQPKyEMGRRAAELLLQLIEG 249
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
44-309 |
8.24e-16 |
|
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: 75.75 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 44 IGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEKMP 123
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQNVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 124 VVTVDAVLNTENITSYVGTVSYDAGKKLGEYTKKYideklgGKSEIAIVT-DLKSQIQMQRIDGFKDAL--KGSANVKIL 200
Cdd:cd01537 82 VVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKH------GHIQIVLLKgPLGHPDAEARLAGVIKELndKGIKTEQLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 NSQPGYDREESLNTVENLIQSNPDVDIIYATAENSVLGA-KAALESAKN--KDVKIVGFDLTEEASSGitdGTILAMIQQ 277
Cdd:cd01537 156 LDTGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAvEALKEHGLRvpSDISVFGYDALPEALKS---GPLLTTILQ 232
|
250 260 270
....*....|....*....|....*....|...
gi 489531185 278 QPKEMGRLAVE-AVVKAIKGEKVEKNIPVPALL 309
Cdd:cd01537 233 DANNLGKTTFDlLLNLADNWKIDNKVVRVPYVL 265
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
61-307 |
8.94e-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: 76.58 E-value: 8.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 61 EGIKEKAKEL---GV--KVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLNTE 134
Cdd:cd19999 19 ADFEEVAAEYkeeGVisDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAgILVVSFDQPVSSP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 135 nitsYVGTVSYDAGKKLGEYTkKYIDEKLGGKSEIAIVTDLK-SQIQMQRIDGFKDALKGSANVKILNSQPG-YDREESL 212
Cdd:cd19999 99 ----DAINVVIDQYKWAAIQA-QWLAEQLGGKGNIVAINGVAgNPANEARVKAADDVFAKYPGIKVLASVPGgWDQATAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 213 NTVENLIQSNPDVDIIYaTAENSVLGAKAALESAkNKDVKI------VGFdLTEEASSGITDgtILAMIQQQPKEMGRLA 286
Cdd:cd19999 174 QVMATLLATYPDIDGVL-TQDGMAEGVLRAFQAA-GKDPPVmtgdyrKGF-LRKWKELDLPD--FESIGVVNPPGIGATA 248
|
250 260
....*....|....*....|.
gi 489531185 287 VEAVVKAIKGEKVEKNIPVPA 307
Cdd:cd19999 249 LRIAVRLLQGKELKEDALNPL 269
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
42-313 |
1.23e-15 |
|
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: 75.62 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 42 LTIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIV--LGTDNSAIVPAVEGaf 119
Cdd:pfam00532 2 LKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIIttPAPSGDDITAKAEG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 120 EKMPVVTVDAVLNTENITSYVGTVSYDAGKKLGEYTKkyideKLGGKSEIAIVTDLKSQI-QMQRIDGFKDALKGSA-NV 197
Cdd:pfam00532 80 YGIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLI-----AEGHKRPIAVMAGPASALtARERVQGFMAALAAAGrEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 198 KILNSQPGY-DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALEsaKNKDVKI-----------VGFDLTEEASSG 265
Cdd:pfam00532 155 KIYHVATGDnDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALL--KQGRVKIpdivgiginsvVGFDGLSKAQDT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489531185 266 ITDGTILAMIQQQPKEMGRLAVEAVVKAI-KGEKVEKNIPVPALLYDKE 313
Cdd:pfam00532 233 GLYLSPLTVIQLPRQLLGIKASDMVYQWIpKFREHPRVLLIPRDFFKET 281
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
64-311 |
4.16e-15 |
|
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: 74.19 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 64 KEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLNTENITSYvgt 142
Cdd:cd19991 22 VKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAgVPVLAYDRLILNADVDLY--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 143 VSYDAgKKLGEYTKKYIdEKLGGKSEIAI----VTDLKSqIQMQRidGFKDALK---GSANVKILNSQ--PGYDREESLN 213
Cdd:cd19991 99 VSFDN-EKVGELQAEAL-VKAKPKGNYVLlggsPTDNNA-KLFRE--GQMKVLQpliDSGDIKVVGDQwvDDWDPEEALK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 214 TVENLI-QSNPDVDIIYATAENSVLGAKAALESAK-NKDVKIVGFDLTEEASSGITDGTILAMIQQQPKEMGRLAVEAVV 291
Cdd:cd19991 174 IMENALtANNNKIDAVIASNDGTAGGAIQALAEQGlAGKVAVSGQDADLAACQRIVEGTQTMTIYKPIKELAEKAAELAV 253
|
250 260
....*....|....*....|....*..
gi 489531185 292 KAIKGEKVEKN-------IPVPALLYD 311
Cdd:cd19991 254 ALAKGEKNEANrtinngkKEVPSILLD 280
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
56-300 |
2.70e-14 |
|
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: 380657 Cd Length: 295 Bit Score: 71.97 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 56 FIDIDEGIKEKAKELGVKVIVNDP-DQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVT------V 127
Cdd:cd20002 14 FNRMEQGVKKAGKEFGVNAYQVGPaDADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKgIVVIThespgqK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 128 DAVLNTENITSyvgtvsydagKKLGEYTKKYIDEKLGGKSEIAI-VTDLKSQIQMQRID-GFKDALKGSANVKILNSQ-- 203
Cdd:cd20002 94 GADWDVELIDN----------EKFGEAQMELLAKEMGGKGEYAIfVGSLTVPLHNLWADaAVEYQKEKYPNMKQVTDRip 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 204 PGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAK-NKDVKIVGFDLTEEASSGITDGTILAMIQQQPKEM 282
Cdd:cd20002 164 GGEDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGlKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDPADA 243
|
250
....*....|....*....
gi 489531185 283 GRlAVEAVVKAI-KGEKVE 300
Cdd:cd20002 244 GY-AMVYIAKMLlDGKRKE 261
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
62-301 |
3.26e-14 |
|
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: 71.43 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 62 GIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIV--LGTDNSAIVPAVEgafEKMPVVTVDAVLnTENITSY 139
Cdd:cd06283 20 GIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILqpTGNNNDAYLELAQ---KGLPVVLVDRQI-EPLNWDT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 140 VGTVSYDAGKKLGEytkkYIDEKlgGKSEIAIVT-DLK-SQIQMQRIDGFKDALK-GSANVKILNSQPGyDREESLNTVE 216
Cdd:cd06283 96 VVTDNYDATYEATE----HLKEQ--GYERIVFVTePIKgISTRRERLQGFLDALArYNIEGDVYVIEIE-DTEDLQQALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 217 NLIQSNPDVD-IIYATaeNS-----VLGAKAALESAKNKDVKIVGFDLTEEA---SSGITdgtilaMIQQQPKEMGRLAV 287
Cdd:cd06283 169 AFLSQHDGGKtAIFAA--NGvvllrVLRALKALGIRIPDDVGLCGFDDWDWAdliGPGIT------TIRQPTYEIGKAAA 240
|
250
....*....|....
gi 489531185 288 EAVVKAIKGEKVEK 301
Cdd:cd06283 241 EILLERIEGDSGEP 254
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
43-313 |
3.47e-14 |
|
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380483 [Multi-domain] Cd Length: 274 Bit Score: 71.43 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTdNSAIVPAVEGAFEKM 122
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPT-KSALPNPNLDLYEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 -----PVVTVDAVLNTENItSYVGTVSYDAGKKLGEYTKKYideklgGKSEIAIVT---DLKSQIQMQridGFKDALKgS 194
Cdd:cd01541 80 qkkgiPVVFINSYYPELDA-PSVSLDDEKGGYLATKHLIDL------GHRRIAGIFksdDLQGVERYQ---GFIKALR-E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 195 ANVKILNSQ-PGYDREE-----SLNTVENLIQSNPDVD-IIYATAENSVLGAKAALESAKN--KDVKIVGFDLTEEASSG 265
Cdd:cd01541 149 AGLPIDDDRiLWYSTEDledrfFAEELREFLRRLSRCTaIVCYNDEIALRLIQALREAGLRvpEDLSVVGFDDSYLASLS 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489531185 266 itdGTILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYDKE 313
Cdd:cd01541 229 ---EPPLTSVVHPKEELGRKAAELLLRMIEEGRKPESVIFPPELIERE 273
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
43-307 |
6.88e-14 |
|
ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380517 [Multi-domain] Cd Length: 269 Bit Score: 70.30 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGV----STITL-QHQFFIDIDEGIKEKAKELGVKVIVNDpDQDVAKQTSAIEDFIQQN-VDGMIVLGT-DNSAIVPAV 115
Cdd:cd06294 1 TIGLvlpsSAEELfQNPFFSEVLRGISQVANENGYSLLLAT-GNTEEELLEEVKRMVRGRrVDGFILLYSkEDDPLIEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 116 -EgafEKMPVVTVDAVLNTENITsYVGTVSYDAGKKLgeyTKKYIDEklgGKSEIA-IVTDLKSQIQMQRIDGFKDALK- 192
Cdd:cd06294 80 kE---EGFPFVVIGKPLDDNDVL-YVDNDNVQAGYEA---TEYLIDK---GHKRIAfIGGDKNLVVSIDRLQGYKQALKe 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 193 -GSANVKILNSQPGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNK---DVKIVGFD---LTEEASSG 265
Cdd:cd06294 150 aGLPLDDDYILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRvpeDVSIISFNnspLAELASPP 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489531185 266 ITDGTIlamiqqQPKEMGRLAVEAVVKAIKGEKVE-KNIPVPA 307
Cdd:cd06294 230 LTSVDI------NPYELGREAAKLLINLLEGPESLpKNVIVPH 266
|
|
| PRK15408 |
PRK15408 |
autoinducer 2 ABC transporter substrate-binding protein LsrB; |
55-298 |
8.12e-14 |
|
autoinducer 2 ABC transporter substrate-binding protein LsrB;
Pssm-ID: 237961 Cd Length: 336 Bit Score: 70.98 E-value: 8.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 55 FFIDIDEGIKEKAKELGVKVIVNDPDQ-DVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLN 132
Cdd:PRK15408 37 FFTSGGNGAKEAGKELGVDVTYDGPTEpSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRgVKVLTWDSDTK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 133 TENITSYV--GTVSyDAGKKLGEYTKKYIDEKlggKSEIAI------VTDlksqiQMQRIDGFKDAL-KGSANVKILNSQ 203
Cdd:PRK15408 117 PECRSYYInqGTPE-QLGSMLVEMAAKQVGKD---KAKVAFfyssptVTD-----QNQWVKEAKAKIaKEHPGWEIVTTQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 204 PGY-DREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNKDVKIVGFDLTEEASSGITDGTILAMIQQQPKEM 282
Cdd:PRK15408 188 FGYnDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRDKVAIVGFSTPNVMRPYVKRGTVKEFGLWDVVQQ 267
|
250
....*....|....*.
gi 489531185 283 GRLAVEAVVKAIKGEK 298
Cdd:PRK15408 268 GKISVYVANELLKKGK 283
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
43-306 |
9.43e-14 |
|
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: 69.98 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEKM 122
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAALRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 PVVTVD---AVLNTENIT--SYVGtvSYDAGKKLGEYtkkyideklgGKSEIAIVTD-LKSQIQMQRIDGFKDALkGSAN 196
Cdd:cd06275 81 PVVVLDreiAGDNADAVLddSFQG--GYLATRHLIEL----------GHRRIGCITGpLEHSVSRERLAGFRRAL-AEAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 197 VKI---------LNSQPGYDreeslnTVENLIQSNPDVDIIYATAENSVLGA-KAALESAKN--KDVKIVGFDLTeEASS 264
Cdd:cd06275 148 IEVppswivegdFEPEGGYE------AMQRLLSQPPRPTAVFACNDMMALGAlRAAQEQGLRvpQDISIIGYDDI-ELAR 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489531185 265 GITDGtiLAMIQQQPKEMGRLAVEAVVKAIKG-EKVEKNIPVP 306
Cdd:cd06275 221 YFSPA--LTTIHQPKDELGELAVELLLDRIENkREEPQSIVLE 261
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
43-315 |
1.35e-13 |
|
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: 69.97 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK- 121
Cdd:cd19994 1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVD-AVLNTENITSYVGTVSYdagkKLGEYTKKYIDEKLGGKSEIAIVT---------DLKSQI----QMQRIDGF 187
Cdd:cd19994 81 IPVIAYDrLIMNTDAVDYYVTFDNE----KVGELQGQYLVDKLGLKDGKGPFNielfagspdDNNAQLffkgAMEVLQPY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 188 KDA---LKGSANVKIL-NSQPGYDREESLNTVENLIQSNP----DVDIIYATAENSVLGAKAALESA----KNKDVkIVG 255
Cdd:cd19994 157 IDDgtlVVRSGQTTFEqVATPDWDTETAQARMETLLSAYYtggkKLDAVLSPNDGIARGVIEALKAAgydtGPWPV-VTG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489531185 256 FDLTEEASSGITDGTILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKN---------IPVPALLYDKENI 315
Cdd:cd19994 236 QDAEDASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVEVNdtktydngvKVVPSYLLDPVIV 304
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
43-302 |
1.41e-13 |
|
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: 69.92 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELG-VKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVlgtdNSAIVPAVEGAFEK 121
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGkIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVV----NLVDRTAAQTIIDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 M-----PVV-----TVDAVLNTENITSYVGTVSYDAGKKLGEYTKKYIDE-----KLG-GKSEIAIVT-DLKSQIQMQRI 184
Cdd:cd01539 78 AkaaniPVIffnrePSREDLKSYDKAYYVGTDAEESGIMQGEIIADYWKAnpeidKNGdGKIQYVMLKgEPGHQDAIART 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 185 DGFKDALKGSA-NVKILNSQPG-YDREESLNTVENLIQSNPD-VDIIYATAENSVLGAKAALESA------KNKDVKIVG 255
Cdd:cd01539 158 KYSVKTLNDAGiKTEQLAEDTAnWDRAQAKDKMDAWLSKYGDkIELVIANNDDMALGAIEALKAAgyntgdGDKYIPVFG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489531185 256 FDLTEEASSGITDGTILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKN 302
Cdd:cd01539 238 VDATPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLET 284
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
43-313 |
1.44e-13 |
|
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380522 [Multi-domain] Cd Length: 268 Bit Score: 69.61 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIG--VSTITlqHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVL--GTDNSAIVPAVEga 118
Cdd:cd06299 1 TIGllVPDIR--NPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVptGENSEGLQALIA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 119 fEKMPVVTVDAVLNtenITSYVGTVSYDAGKKLGEYTKKYIDEklgGKSEIAIVT-DLKSQIQMQRIDGFKDALkgSANV 197
Cdd:cd06299 77 -QGLPVVFVDREVE---GLGGVPVVTSDNRPGAREAVEYLVSL---GHRRIGYISgPLSTSTGRERLAAFRAAL--TAAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 198 KILNSQ----PGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAK---NKDVKIVGFD---LTEEASSGIT 267
Cdd:cd06299 148 IPIDEElvafGDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGlriGDDVSLISFDdvpWFELLSPPLT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489531185 268 dgtilaMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALLYDKE 313
Cdd:cd06299 228 ------VIAQPVERIGRRAVELLLALIENGGRATSIRVPTELIPRE 267
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
43-306 |
2.16e-13 |
|
ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380630 [Multi-domain] Cd Length: 269 Bit Score: 69.12 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGtdnSAIVPAVEGAFEKM 122
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFAS---GTLTEENKQLLKNM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 --PVVTVDAVLNTENItSYVGTVSYDAGKklgEYTKKYIDEklgGKSEIAIV----TDLKSQIqmQRIDGFKDALKgSAN 196
Cdd:cd19975 78 niPVVLVSTESEDPDI-PSVKIDDYQAAY---DATNYLIKK---GHRKIAMIsgplDDPNAGY--PRYEGYKKALK-DAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 197 VKI--LNSQPG-YDREESLNTVENLIQSNPDVDIIYATAENSVLGA-KAALESAKN--KDVKIVGFDLTEEASSGITDgt 270
Cdd:cd19975 148 LPIkeNLIVEGdFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGViSAAYDHGIRvpEDISVIGFDNTEIAEMSIPP-- 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 489531185 271 iLAMIQQQPKEMGRLAVEAVVKAIKGEKV-EKNIPVP 306
Cdd:cd19975 226 -LTTVSQPFYEMGKKAVELLLDLIKNEKKeEKSIVLP 261
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
43-303 |
5.04e-13 |
|
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380489 [Multi-domain] Cd Length: 269 Bit Score: 67.91 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAivpavegAFEKM 122
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTP-------ATRKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 ------PVV-TVDavLNTENITSYVGTVSYDAGKKLGEytkkYIDEKlgGKSEIAIV-----TDLKSQiqmQRIDGFKDA 190
Cdd:cd01575 74 lraagiPVVeTWD--LPDDPIDMAVGFSNFAAGRAMAR----HLIER--GYRRIAFVgarldGDSRAR---QRLEGFRDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 191 LK---GSANVKILNSQPG--YDREESLNTvenLIQSNPDVDIIYATaeNSVLGAKAALESAKN-----KDVKIVGF---D 257
Cdd:cd01575 143 LAeagLPLPLVLLVELPSsfALGREALAE---LLARHPDLDAIFCS--NDDLALGALFECQRRgirvpGDIAIAGFgdlD 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489531185 258 LTEEASSGITdgTILAmiqqQPKEMGRLAVEAVVKAIKGEKVEKNI 303
Cdd:cd01575 218 IAAALPPALT--TVRV----PRYEIGRKAAELLLARLEGEEPEPRV 257
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
62-303 |
7.09e-13 |
|
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: 67.70 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 62 GIKEKAKEL--GVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTD-NSAIVPAVEGAFEKMPVVTVDAVLNTENITS 138
Cdd:cd19995 21 GFEKAMKKLcpDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDsNAAAGIVAKAAQAGVPVIAYDRLILGGPADY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 139 YVGTVSYDAGKKLGEYTKKYIDEKLGGKSEIAIV----TDLKSQIQMQRIDGFKDALKGSANVKILNSQ--PGYDREESL 212
Cdd:cd19995 101 YVSFDNVAVGEAQAQSLVDHLKAIGKKGVNIVMIngspTDNNAGLFKKGAHEVLDPLGDSGELKLVCEYdtPDWDPANAQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 213 NTVENLIQSNPD-VDIIYATAENSVLGAKAALESAKNKDVKIV-GFDLTEEASSGITDGTILAMIQQQPKEMGRLAVEAV 290
Cdd:cd19995 181 TAMEQALTKLGNnIDGVLSANDGLAGGAIAALKAQGLAGKVPVtGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVA 260
|
250
....*....|...
gi 489531185 291 VKAIKGEKVEKNI 303
Cdd:cd19995 261 VALLKGETPPSDL 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
53-320 |
2.45e-12 |
|
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: 66.16 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 53 HQFFIDIDEGIKEKAKELGV--KVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDA 129
Cdd:cd19997 14 RQQMVDAFEEAAKKAKADGLiaDYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAgIKVVVFDS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 130 VLNTENITsyvgTVSYDAGkKLGEYTKKYIDEKLGGKSEIAIVTDLK-SQIQMQRIDGFKDALKGSANVKILNSQPG-YD 207
Cdd:cd19997 94 GVTEPCAY----ILNNDFE-DYGAASVEYVADRLGGKGNVLEVRGVAgTSPDEEIYAGQVEALKKYPDLKVVAEVYGnWT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 208 REESLNTVENLIQSNPDVDIIYATAENSvLGAKAALESAKNKDVKIVGFDLTE------EASSGITDGTILAMIqqqPKE 281
Cdd:cd19997 169 QSVAQKAVTGILPSLPEVDAVITQGGDG-YGAAQAFEAAGRPLPIIIGGNRGEflkwwqEEYAKNGYETVSVST---DPG 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 489531185 282 MGRLAVEAVVKAIKGEKVEKNIPVPALLYDKENIKDFKN 320
Cdd:cd19997 245 QGSAAFWVALDILNGKDVPKEMILPVVTITEDDLDAWLA 283
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
43-300 |
3.27e-12 |
|
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: 65.65 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFF-IDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEgaFEK 121
Cdd:cd06288 1 TIGLITDDIATTPFaGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLPPE--LTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSYVgtvsydagkklgeytkkyIDEKLGGK-----------SEIAIVTDLKSQI-QMQRIDGFKD 189
Cdd:cd06288 79 IPLVLLNCFDDDPSLPSVV------------------PDDEQGGYlatrhlieaghRRIAFIGGPEDSLaTRLRLAGYRA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 190 ALkGSANVKILNS---QPGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAK---NKDVKIVGFDLTEEAS 263
Cdd:cd06288 141 AL-AEAGIPYDPSlvvHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGlrvPEDLSVVGFDNQELAA 219
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489531185 264 S---GITdgTIlamiqQQP-KEMGRLAVEAVVKAIKGEKVE 300
Cdd:cd06288 220 YlrpPLT--TV-----ALPyYEMGRRAAELLLDGIEGEPPE 253
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
43-306 |
1.50e-11 |
|
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of LacI is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380488 [Multi-domain] Cd Length: 265 Bit Score: 63.75 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELG--VKVIVNDPDQDVAKQTsAIEDFIQQNVDGMIVLgTDNSAIVPAVEGAFE 120
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGysVSIATVDEDDPASVRE-ALDRLLSQRVDGIIVI-APDEAVLEALRRLPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 KMPVVTVDAVLNTEniTSYVGTVSYDAGKKLGEYtkkYIDekLGGKSeIAIVT-DLKSQIQMQRIDGFKDALK--GSANV 197
Cdd:cd01574 79 GLPVVIVGSGPSPG--VPTVSIDQEEGARLATRH---LLE--LGHRR-IAHIAgPLDWVDARARLRGWREALEeaGLPPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 198 KIL----NSQPGYDREESLntvenliQSNPDVDIIYATAENSVLGA-KAALESAKN--KDVKIVGFDLTEEASSgitdgT 270
Cdd:cd01574 151 PVVegdwSAASGYRAGRRL-------LDDGPVTAVFAANDQMALGAlRALHERGLRvpEDVSVVGFDDIPEAAY-----F 218
|
250 260 270
....*....|....*....|....*....|....*...
gi 489531185 271 I--LAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVP 306
Cdd:cd01574 219 VppLTTVRQDFAELGRRAVELLLALIEGPAPPPESVLL 256
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
43-300 |
2.26e-11 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 63.06 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVlgTDNSAIVPAVEGAFEK- 121
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIV--TPSDDDLSHLARLRARg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVLNTENITSyvgtVSYD--AGKKLGeytkkyIDEKLG-GKSEIAIVTDLKSQIQM-QRIDGFKDALKGSANV 197
Cdd:cd06293 79 TAVVLLDRPAPGPAGCS----VSVDdvQGGALA------VDHLLElGHRRIAFVSGPLRTRQVaERLAGARAAVAEAGLD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 198 KILN----SQPGYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKNK---DVKIVGFDLTEEASSGITDGT 270
Cdd:cd06293 149 PDEVvrelSAPDANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRvpdDVSVVGYDDLPFAAAANPPLT 228
|
250 260 270
....*....|....*....|....*....|.
gi 489531185 271 ILAmiqqQPK-EMGRLAVEAVVKAIKGEKVE 300
Cdd:cd06293 229 TVR----QPSyELGRAAADLLLDEIEGPGHP 255
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
55-300 |
3.22e-11 |
|
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: 62.65 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 55 FFIDIDEGIKEKAKELGVKVIVNDPDQDvakqTSAIEDFIQQN-VDGMIVLGT-DNSAIVPAVEGAfeKMPVVTVDAVLN 132
Cdd:cd06295 24 FFLELLGGISEALTDRGYDMLLSTQDED----ANQLARLLDSGrADGLIVLGQgLDHDALRELAQQ--GLPMVVWGAPED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 133 TENITSyVGTVSYDAGKKLGEYtkkYIDeklGGKSEIAIVTDLKSQIQMQRIDGFKDALKGS-ANVKILNSQPGYDREES 211
Cdd:cd06295 98 GQSYCS-VGSDNVKGGALATEH---LIE---IGRRRIAFLGDPPHPEVADRLQGYRDALAEAgLEADPSLLLSCDFTEES 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 212 -LNTVENLIQSNPDVDIIYATAENSVLGAKAALeSAKNK----DVKIVGFDLTEEASSGITDgtiLAMIQQQPKEMGRLA 286
Cdd:cd06295 171 gYAAMRALLDSGTAFDAIFAASDLIAMGAIRAL-RERGIsvpgDVAVVGYDDIPLAAYFRPP---LTTVRQDLALAGRLL 246
|
250
....*....|....
gi 489531185 287 VEAVVKAIKGEKVE 300
Cdd:cd06295 247 VEKLLALIAGEPVT 260
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
98-300 |
5.56e-11 |
|
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380502 [Multi-domain] Cd Length: 284 Bit Score: 62.23 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 98 VDGMIVLGT-DNSAIVPAVEGAfeKMPVVTVDAVLnTENITSyVGTVSYDAGKKLGEYTKKyideklGGKSEIAIVT--- 173
Cdd:cd06279 57 VDGFIVYGLsDDDPAVAALRRR--GLPLVVVDGPA-PPGIPS-VGIDDRAAARAAARHLLD------LGHRRIAILSlrl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 174 ------------DLKS---QIQMQRIDGFKDALKG----SANVKILNSqPGYDREESLNTVENLIQSNPDVDIIYATaen 234
Cdd:cd06279 127 drgrergpvsaeRLAAatnSVARERLAGYRDALEEagldLDDVPVVEA-PGNTEEAGRAAARALLALDPRPTAILCM--- 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489531185 235 SVLGAKAALESAKN------KDVKIVGFDLTEEASSGITDgtiLAMIQQQPKEMGRLAVEAVVKAIKGEKVE 300
Cdd:cd06279 203 SDVLALGALRAARErglrvpEDLSVTGFDDIPEAAAADPG---LTTVRQPAVEKGRAAARLLLGLLPGAPPR 271
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
43-301 |
6.53e-11 |
|
ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to CcpA which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree.
Pssm-ID: 380509 [Multi-domain] Cd Length: 262 Bit Score: 61.79 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVpaVEGAFEKM 122
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDWEV--IEPYAKYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 PVVTVDAVLNtENITSyVGTVSYDAGKKLGEYTKkyidEKlgGKSEIAIVTD---LKSQIQMQRIDGFKDALKGsanvKI 199
Cdd:cd06286 79 PIVLCEETDS-PDIPS-VYIDRYEAYLEALEYLK----EK--GHRKIGYCLGrpeSSSASTQARLKAYQDVLGE----HG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 200 LNSQP------GYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAALESAKN---KDVKIVGFDLTEEASS-GITdg 269
Cdd:cd06286 147 LSLREewiftnCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIrvpEDLAVIGFDNQPISELlNLT-- 224
|
250 260 270
....*....|....*....|....*....|..
gi 489531185 270 TilamIQQQPKEMGRLAVEAVVKAIKGEKVEK 301
Cdd:cd06286 225 T----IDQPLEEMGKEAFELLLSQLESKEPTK 252
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
74-305 |
3.23e-10 |
|
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: 59.85 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 74 VIVNDPDQDVAkqtSAIEDFIQQNVDGMIVL-GTDNSAIVpaveGAFEK--MPVVTVDAVLNTENItSYVGTVSYDAGKK 150
Cdd:cd06278 34 LFNVDDEDDVD---DALRQLLQYRVDGVIVTsATLSSELA----EECARrgIPVVLFNRVVEDPGV-DSVSCDNRAGGRL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 151 LGEYtkkyidekL--GGKSEIAIVT-DLKSQIQMQRIDGFKDALK--GSANVKILnsQPGYDREESLNTVENLIQSNPDV 225
Cdd:cd06278 106 AADL--------LlaAGHRRIAFLGgPEGTSTSRERERGFRAALAelGLPPPAVE--AGDYSYEGGYEAARRLLAAPDRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 226 DIIYatAENSVLgAKAALESAKNK-------DVKIVGFDLTEEASSGITDgtiLAMIQQQPKEMGRLAVEAVVKAIKG-- 296
Cdd:cd06278 176 DAIF--CANDLM-ALGALDAARQEgglvvpeDISVVGFDDIPMAAWPSYD---LTTVRQPIEEMAEAAVDLLLERIENpe 249
|
250
....*....|
gi 489531185 297 -EKVEKNIPV 305
Cdd:cd06278 250 tPPERRVLPG 259
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
43-300 |
8.23e-10 |
|
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation; This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380519 [Multi-domain] Cd Length: 270 Bit Score: 58.44 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTD-NSAIVPAVEGAfeK 121
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDpTSRQLRLLRSA--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 MPVVTVDAVlNTEN-------ITSYVGtvSYDAGKKLGEytkkyidekLGGKSeIAIVT-DLKSQIQMQRIDGFKDALKg 193
Cdd:cd06296 79 IPFVLIDPV-GEPDpdlpsvgATNWAG--GRLATEHLLD---------LGHRR-IAVITgPPRSVSGRARLAGYRAALA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 194 SANVKI---LNSQPGYDREESLNTVENLIQSnPDVDI-IYATAENSVLGAKAALESAKNK---DVKIVGFDLTEEA---S 263
Cdd:cd06296 145 EAGIAVdpdLVREGDFTYEAGYRAARELLEL-PDPPTaVFAGNDEQALGVYRAARALGLRvpdDLSVIGFDDTPPArwtS 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 489531185 264 SGITdgTIlamiqQQP-KEMGRLAVEAVVKAIKGEKVE 300
Cdd:cd06296 224 PPLT--TV-----HQPlREMGAVAVRLLLRLLEGGPPD 254
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
64-305 |
1.74e-09 |
|
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule 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 LuxPQ to control light production as well as its motility behavior.
Pssm-ID: 380526 [Multi-domain] Cd Length: 320 Bit Score: 58.15 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 64 KEKAKELGVK----VIVNDPDQDVAKQTSAIEDFIQQNVDgMIVLGTDNSAIVPAVEGAF--EKMPVVTvdavlntENIT 137
Cdd:cd06303 51 RKRLDELGIKyqldEFFTRPGAEIRLQALQIREMLKSDPD-YLIFTLDALRHRRFVEILLdsGKPKLIL-------QNIT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 138 S------------YVGTVSYDAGKKLGeytkKYIDEKLGGKSEIAIVTDLKSQIQMQRIDGFKDALKGSANVKILNS-QP 204
Cdd:cd06303 123 TplrdwdnhqpllYVGFDHAEGSRMLA----KHFIKIFPEEGKYAILYLTEGYVSDQRGDTFIDEVARHSNLELVSAyYT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 205 GYDREESLNTVENLIQSNPDVDIIYATAENSVLGAKAAL-ESAKNKDVKIVGFdlteeasSGITDGtiLAMIQQqpkemG 283
Cdd:cd06303 199 DFDRESAREAARALLARHPDLDFIYACSTDIALGAIDALqELGRETDIMINGW-------GGGSAE--LDALQK-----G 264
|
250 260 270
....*....|....*....|....*....|..
gi 489531185 284 RLAVE----------AVVKAIKGEKVEKNIPV 305
Cdd:cd06303 265 GLDVTvmrmnddngiAMAEAIKLDLEGREVPT 296
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
53-300 |
4.12e-09 |
|
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380487 [Multi-domain] Cd Length: 270 Bit Score: 56.41 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 53 HQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQ-NVDGMIVLG--TDNSAIVPAVEGAfeKMPVVTVdA 129
Cdd:cd01545 11 ASYVSALQVGALRACREAGYHLVVEPCDSDDEDLADRLRRFLSRsRPDGVILTPplSDDPALLDALDEL--GIPYVRI-A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 130 VLNTENITSYVGTVSYDAGKKLGEYtkkYIDEklgGKSEIAIVTDLKSQI-QMQRIDGFKDALKgSANVKI---LNSQPG 205
Cdd:cd01545 88 PGTDDDRSPSVRIDDRAAAREMTRH---LIAL---GHRRIGFIAGPPDHGaSAERLEGFRDALA-EAGLPLdpdLVVQGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 206 YDREESLNTVENLIQSNPDVDIIYATAENSVLGA-KAALESAKN--KDVKIVGFDLTEEASS---GITdgTIlamiqQQP 279
Cdd:cd01545 161 FTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVlAAAHRLGLRvpDDLSVAGFDDSPIARLvwpPLT--TV-----RQP 233
|
250 260
....*....|....*....|..
gi 489531185 280 -KEMGRLAVEAVVKAIKGEKVE 300
Cdd:cd01545 234 iAEMARRAVELLIAAIRGAPAG 255
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
43-303 |
5.03e-09 |
|
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380521 [Multi-domain] Cd Length: 268 Bit Score: 56.14 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGtdnSAIVPAVEGAFEK- 121
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMG---DELTEEIREEFKRs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 122 -MPVVTVDAVLNTENITSyvgtVSYDAGKKLGEYTKKYIDEklgGKSEIAIV-TDLKSQI-QMQRIDGFKDALKgSANVK 198
Cdd:cd06298 78 pVPVVLAGTVDSDHEIPS----VNIDYEQAAYDATKSLIDK---GHKKIAFVsGPLKEYInNDKKLQGYKRALE-EAGLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 199 ILNS---QPGYDREESLNTVENLIQSNpDVDIIYATAENSVLG-AKAALESAKN--KDVKIVGFDLTEEASsgITDGTiL 272
Cdd:cd06298 150 FNEPlifEGDYDYDSGYELYEELLESG-EPDAAIVVRDEIAVGlLNAAQDRGLKvpEDLEIIGFDNTRYAT--MSRPQ-L 225
|
250 260 270
....*....|....*....|....*....|.
gi 489531185 273 AMIQQQPKEMGRLAVEAVVKAIKGEKVEKNI 303
Cdd:cd06298 226 TSINQPLYDIGAVAMRLLTKLMNKEEVEETI 256
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
43-309 |
5.36e-08 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 52.90 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSaivPAVEGAFE-- 120
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHD---PELFELLEqr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 KMPVVTVDAVLNTENITSyVGTVSYDAGKKLGEYTKkyideKLGGKsEIAIVT------DLksqiQMQRIDGFKDALK-- 192
Cdd:cd06273 78 QVPYVLTWSYDEDSPHPS-IGFDNRAAAARAAQHLL-----DLGHR-RIAVISgptagnDR----ARARLAGIRDALAer 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 193 ----GSANVkilnSQPGYDREESLNTVENLIQSNPDVDIIYATaeNSVLgAKAALESAKN------KDVKIVGFDLTEEA 262
Cdd:cd06273 147 glelPEERV----VEAPYSIEEGREALRRLLARPPRPTAIICG--NDVL-ALGALAECRRlgisvpEDLSITGFDDLELA 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489531185 263 SS---GITdgTIlamiqQQP-KEMGRLAVEAVVKAIKGEKVEKNIPVPALL 309
Cdd:cd06273 220 AHlspPLT--TV-----RVPaREIGELAARYLLALLEGGPPPKSVELETEL 263
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
40-317 |
6.26e-08 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 53.21 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 40 KDLTIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDgMIVLGTDNSAIVPAV--EG 117
Cdd:PRK10355 24 KEVKIGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQMSQIENMINRGVD-VLVIIPYNGQVLSNVikEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 118 AFEKMPVVTVDAVLNTENITSYvgtVSYDaGKKLGEYTKKYIDEK-------LGGKSEIAIVTDLKSQIQMQRIDGFKDa 190
Cdd:PRK10355 103 KQEGIKVLAYDRMINNADIDFY---ISFD-NEKVGELQAKALVDKvpqgnyfLMGGSPVDNNAKLFRAGQMKVLKPYID- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 191 lkgSANVKILNSQ--PGYDREESLNTVEN-LIQSNPDVDIIYATAENSVLGAKAALES-AKNKDVKIVGFDLTEEASSGI 266
Cdd:PRK10355 178 ---SGKIKVVGDQwvDGWLPENALKIMENaLTANNNKIDAVVASNDATAGGAIQALSAqGLSGKVAISGQDADLAAIKRI 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489531185 267 TDGTILAMIQQQPKEMGRLAVEAVVKAIKGEKVEKNIP-------VPALLY-----DKENIKD 317
Cdd:PRK10355 255 VAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKANTTlnnglkdVPSRLLtpidvNKNNIDS 317
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
51-310 |
1.30e-07 |
|
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
Pssm-ID: 380498 [Multi-domain] Cd Length: 264 Bit Score: 51.82 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 51 LQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLG-TDNSAIVPAveGAFEKMPVVTVDA 129
Cdd:cd06274 9 LANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPsTPPDDIYYL--CQAAGLPVVFLDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 130 VLNTENITSYVgTVSYDAGKKLgeyTKKYIDEK------LGGKSEIAIVTDlksqiqmqRIDGFKDALK--GSANVKILN 201
Cdd:cd06274 87 PFSGSDAPSVV-SDNRAGARAL---TEKLLAAGpgeiyfLGGRPELPSTAE--------RIRGFRAALAeaGITEGDDWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 202 SQPGYDREESLNTVENLIQSN---PDVDIIyataeNSVLGAKAALESAKNKDVKIVG------FDlteeassgitDGTIL 272
Cdd:cd06274 155 LAEGYDRESGYQLMAELLARLgglPQALFT-----SSLTLLEGVLRFLRERLGAIPSdlvlgtFD----------DHPLL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489531185 273 A-------MIQQQPKEMGRLAVEAVVKAIKGEKVEKNIPVPALLY 310
Cdd:cd06274 220 DflpnpvdSVRQDHDEIAEHAFELLDALIEGQPEPGVIIIPPELI 264
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
43-301 |
3.63e-07 |
|
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380494 [Multi-domain] Cd Length: 266 Bit Score: 50.60 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIV--LGTDNSAIVPAVEgafE 120
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILhsRALSDEELILIAE---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 121 KMPVVtvdaVLNtENITSYVG-TVSYDagKKLGEY--TKKYIDEklgGKSEIAIVT-DLKSQIQMQRIDGFKDALKGSA- 195
Cdd:cd06270 78 IPPLV----VIN-RYIPGLADrCVWLD--NEQGGRlaAEHLLDL---GHRRIACITgPLDIPDARERLAGYRDALAEAGi 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 196 ---NVKILNSQPGYDREESLntVENLIQSNPDVDIIYATAENSVLGAKAALESAKNK---DVKIVGFD---LTEEASSGI 266
Cdd:cd06270 148 pldPSLIIEGDFTIEGGYAA--AKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKvpeDVSVIGFDdvpLARYLSPKL 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 489531185 267 TdgTIlamiqQQP-KEMGRLAVEAVVKAIKGEKVEK 301
Cdd:cd06270 226 T--TV-----HYPiEEMAQAAAELALNLAYGEPLPI 254
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
43-297 |
1.28e-06 |
|
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380512 [Multi-domain] Cd Length: 268 Bit Score: 49.10 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMI---VLGTDNSAIVPAVEgaf 119
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLIlspAAGTTAELLRRLKA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 120 EKMPVVTVD-AVLNTEniTSYVGTVSYDAGKKLGEYtkkYIDEklgGKSEIAIVTDLK-SQIQMQRIDGFKDALKGsANV 197
Cdd:cd06289 78 WGIPVVLALrDVPGSD--LDYVGIDNRLGAQLATEH---LIAL---GHRRIAFLGGLSdSSTRRERLAGFRAALAE-AGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 198 KILNSQ--PG-YDREESLNTVENLIQSNPDVDIIYatAENSV--LGAKAALESA---KNKDVKIVGFDLTEEASSGITDg 269
Cdd:cd06289 149 PLDESLivPGpATREAGAEAARELLDAAPPPTAVV--CFNDLvaLGAMLALRRRglePGRDIAVVGFDDVPEAALWTPP- 225
|
250 260
....*....|....*....|....*...
gi 489531185 270 tiLAMIQQQPKEMGRLAVEAVVKAIKGE 297
Cdd:cd06289 226 --LTTVSVHPREIGRRAARLLLRRIEGP 251
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
43-291 |
2.01e-06 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 48.54 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITLQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEKM 122
Cdd:PRK10423 58 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMQRYPSV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 123 PVVTVDAVLnteniTSYVGTVSYDAGKKLGEYTKKYIDEKlgGKSEIAIVTD-LKSQIQMQRIDGFKDALKGSAnvkiLN 201
Cdd:PRK10423 138 PTVMMDWAP-----FDGDSDLIQDNSLLGGDLATQYLIDK--GYTRIACITGpLDKTPARLRLEGYRAAMKRAG----LN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 202 SQPGY----DREES--LNTVENLIQSNPDVDIIYATAENSVLGAKAALESAK---NKDVKIVGFDLTEEASSGITDgtiL 272
Cdd:PRK10423 207 IPDGYevtgDFEFNggFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGlsvPQDIAVIGYDDIELARYMTPP---L 283
|
250
....*....|....*....
gi 489531185 273 AMIQQQPKEMGRLAVEAVV 291
Cdd:PRK10423 284 TTIHQPKDELGELAIDVLI 302
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
98-298 |
2.64e-06 |
|
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380520 [Multi-domain] Cd Length: 268 Bit Score: 47.85 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 98 VDGMIVLGTDNSAIVPAVEGAFEKmPVVTVDAvlNTENITS-YVGTV-------SYDAGKKLGEYTKKYIDEKlggksei 169
Cdd:cd06297 56 CDGLVMASLDLTELFEEVIVPTEK-PVVLIDA--NSMGYDCvYVDNVkggfmatEYLAGLGEREYVFFGIEED------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 170 aivTDLKSQIQMQRIDGFKDALKgSANVKILNSQ---PGYDREESLNTVENLIQSNPDVDIIYATAENSVLGA-KAALES 245
Cdd:cd06297 126 ---TVFTETVFREREQGFLEALN-KAGRPISSSRmfrIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLiRAAQSL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489531185 246 AKN--KDVKIVGFD---LTEEASsgitdgtiLAMIQQQPKEMGRLAVEAVVKAIKGEK 298
Cdd:cd06297 202 GLRvgEDVAVIGFDgqpWAASPG--------LTTVRQPVEEMGEAAAKLLLKRLNEYG 251
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
43-300 |
3.49e-05 |
|
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380515 [Multi-domain] Cd Length: 273 Bit Score: 44.57 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGV----STITLQHQFFIDIDEGIKEKAKELGVKVIV--NDPDQDvakQTSAIEDFIQQN-VDGMIVLGTD-NSAIVPA 114
Cdd:cd06292 1 LIGYvvpeLPGGFSDPFFDEFLAALGHAAAARGYDVLLftASGDED---EIDYYRDLVRSRrVDGFVLASTRhDDPRVRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 115 VEGAfeKMPVVTVDAVlnteNITSYVGTVSYDAGKKLGEYTKKYIDEklgGKSEIAIVT-DLKSQIQMQRIDGFKDALKG 193
Cdd:cd06292 78 LHEA--GVPFVAFGRA----NPDLDFPWVDVDGAAGMRQAVRHLIAL---GHRRIGLIGgPEGSVPSDDRLAGYRAALEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 194 SAnvkiLNSQPGYDREeSLNTVE-------NLIQSNPDVDIIYATAENSVLGAKAALESAK---NKDVKIVGFD---LTE 260
Cdd:cd06292 149 AG----LPFDPGLVVE-GENTEEggyaaaaRLLDLGPPPTAIVCVSDLLALGAMRAARERGlrvGRDVSVVGFDdspLAA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489531185 261 EASSGITdgTIlamiqQQP-KEMGRLAVEAVVKAIKGEKVE 300
Cdd:cd06292 224 FTHPPLT--TV-----RQPiDEIGRAVVDLLLAAIEGNPSE 257
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
55-296 |
3.51e-05 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380629 [Multi-domain] Cd Length: 270 Bit Score: 44.46 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 55 FFIDIDEGIKEKAKELGVK---VIVNDPDQDVAKQTSAIEDfiqQNVDGMIVLGTDNSAIVPAVEGAfeKMPVVTVDAvL 131
Cdd:cd19974 16 FYGKIYQGIEKELSELGYNlvlEIISDEDEEELNLPSIISE---EKVDGIIILGEISKEYLEKLKEL--GIPVVLVDH-Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 132 NTENITSYVGTVSYDAGKKLgeyTKKYIDEklgGKSEIAIVTDLK-SQIQMQRIDGFKDALK--GSANVK---ILNSQP- 204
Cdd:cd19974 90 DEELNADSVLSDNYYGAYKL---TSYLIEK---GHKKIGFVGDINyTSSFMDRYLGYRKALLeaGLPPEKeewLLEDRDd 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 205 GYDREESLNTVENLIQsnPDV-----DIIyataensvlgAKAALESAKNK------DVKIVGFDLTEEASSGITDgtiLA 273
Cdd:cd19974 164 GYGLTEEIELPLKLML--PTAfvcanDSI----------AIQLIKALKEKgyrvpeDISVVGFDNIELAELSTPP---LT 228
|
250 260
....*....|....*....|...
gi 489531185 274 MIQQQPKEMGRLAVEAVVKAIKG 296
Cdd:cd19974 229 TVEVDKEAMGRRAVEQLLWRIEN 251
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
51-297 |
6.03e-05 |
|
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380486 [Multi-domain] Cd Length: 269 Bit Score: 43.67 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 51 LQHQFFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQtsaiedfIQQNVDGMIVLGTDNSAIVPAVEGAFEkmPVVTVDAV 130
Cdd:cd01544 14 LEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLES-------LLEKVDGIIAIGKFSKEEIEKLKKLNP--NIVFVDSN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 131 LNTENITSyvgtVSYDagkkLGEYTKK---YIDEKlgGKSEIAIV------TDLKSQIQMQRIDGFKDALK--GSANVK- 198
Cdd:cd01544 85 PDPDGFDS----VVPD----FEQAVRQaldYLIEL--GHRRIGFIggkeytSDDGEEIEDPRLRAFREYMKekGLYNEEy 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 199 ILNSqpGYDREESLNTVENLIQSNPDVDIIYATAENSVLGA-KAALESAKN--KDVKIVGFDLTEEA-------SSgitd 268
Cdd:cd01544 155 IYIG--EFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGAlRALQEAGIKvpEDISIISFNDIEVAkyvtpplTT---- 228
|
250 260
....*....|....*....|....*....
gi 489531185 269 gtilamIQQQPKEMGRLAVEAVVKAIKGE 297
Cdd:cd01544 229 ------VHIPTEEMGRTAVRLLLERINGG 251
|
|
| PBP1_ABC_sugar_binding-like |
cd06315 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
56-308 |
1.51e-04 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380538 Cd Length: 278 Bit Score: 42.72 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 56 FIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEK-MPVVTVDAVLNTE 134
Cdd:cd06315 15 VLGVGRGVKEAAAALGWKVDVLDGGGTVTGRLAALNQALALKPDGIILGGDDAVELQEPLKKAVKAgIPVVGWHAAASPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 135 NITSY--VGTVSYDAgKKLGEYTKKYIDEKLGGKSEIAIVTDLKSQIQMQRIDGFKDALKGSANVKILNSQ--PGYDREE 210
Cdd:cd06315 95 PIPELglFTNITTDP-REVAETAAALVIAQSGGKAGVVIFTDSRYAIATAKANAMKKAIEACSGCKVLEYVdiPIADTAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 211 SLNTVENLIQSNPDVDIIYATAENSVL--GAKAALESA--KNKDVKIVGFDLTEEASSGITDGTILAMIQQQPKEM-GRL 285
Cdd:cd06315 174 RMPKLIRSLLQRYGDRWTHTLAINDLYfdFAAPALRAAgvEADPVNISAGDGSPSAYDRIRAGEYQVATVAEPLTLqGWQ 253
|
250 260
....*....|....*....|...
gi 489531185 286 AVEAVVKAIKGEKVEKNIPVPAL 308
Cdd:cd06315 254 LVDELNRALAGEPPSGYVQPVHL 276
|
|
| PBP1_PrnA-like |
cd06354 |
periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its ... |
59-303 |
4.76e-04 |
|
periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its homologs from other bacteria and Archaea; Periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its homologs from other bacteria and Archaea. The PnrA lipoprotein, also known as Tp0319 or TmpC, represents a novel family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC) transport system (pnrABCDE). It shows a striking structural similarity to another basic membrane lipoprotein Med which regulates the competence transcription factor gene, comK, in Bacillus subtilis. The members of PnrA-like subgroup are likely to have similar nucleoside-binding functions and a similar type 1 periplasmic sugar-binding protein-like fold.
Pssm-ID: 380577 Cd Length: 268 Bit Score: 41.01 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 59 IDEGIKEKAKELGVKVIVNDPDQDvAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEKMPVVTVDAVLNT--ENI 136
Cdd:cd06354 20 AWEGLQRAAKELGIKVKYLESKSD-ADYEPNLRALADEGYDLIITVGFAMADAVEEAAKANPDTKFIIIDATVDEtpPNV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 137 TSYV---GTVSYDAGKKLGEYTKKYideKLG--GKSEIAIVTDLksqiqmqrIDGFKDALK-----GSANVKILNSQPGY 206
Cdd:cd06354 99 RSIVfreEEAAFLAGYLAALMTKTG---KVGfiGGMDIPPVRRF--------EDGFAAGAKyanpdIVVDVTVIGTYAGS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 207 --DREESLNTVENLIQSnpDVDIIYATAENSVLGakaALESAKNKDVKIVGFDlteEASSGITDGTILA-MIqqqpKEMG 283
Cdd:cd06354 168 fnDPAKGKAIAQEMIDQ--GADVIFAAAGGTGLG---VIEAAKEAGKYAIGVD---VDQNYLAPGNVLTsVV----KRVD 235
|
250 260
....*....|....*....|
gi 489531185 284 RLAVEAVVKAIKGEKVEKNI 303
Cdd:cd06354 236 VAVYDAIKDLVNGKFGGGVI 255
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
169-313 |
5.42e-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: 40.01 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 169 IAIVTDLKSQIQMQRIDGFKDALKgSANVKILNSQPGYDREESLNTVEN-LIQSNPDVDIIYATAENSVLGAKAALESAK 247
Cdd:pfam13377 13 IGPEGDRDDPYSDLRERGFREAAR-ELGLDVEPTLYAGDDEAEAAAARErLRWLGALPTAVFVANDEVALGVLQALREAG 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489531185 248 NK---DVKIVGFDLTEEA---SSGITdgtilaMIQQQPKEMGRLAVEAVVKAIKGEK-VEKNIPVPALLYDKE 313
Cdd:pfam13377 92 LRvpeDLSVIGFDDSPLAalvSPPLT------TVRVDAEELGRAAAELLLDLLNGEPaPPERVLLPPELVERE 158
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
72-242 |
1.27e-03 |
|
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];
Pssm-ID: 440447 [Multi-domain] Cd Length: 314 Bit Score: 39.91 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 72 VKVIV----NDPDQDVAKQTSAIEdfiQQNVDGMI-VLGTDNS-AIVPAVEGAfeKMPVVTV---DAVLNTENITSYV-- 140
Cdd:COG0683 45 IELVVeddaSDPDTAVAAARKLID---QDKVDAIVgPLSSGVAlAVAPVAEEA--GVPLISPsatAPALTGPECSPYVfr 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 141 -GTVSYDAGKKLGeytkKYIDEKLGGKSeIAIVTDlKSQIQMQRIDGFKDALKgSANVKILNSQPgYDREES--LNTVEN 217
Cdd:COG0683 120 tAPSDAQQAEALA----DYLAKKLGAKK-VALLYD-DYAYGQGLAAAFKAALK-AAGGEVVGEEY-YPPGTTdfSAQLTK 191
|
170 180
....*....|....*....|....*
gi 489531185 218 LIQSNPDVDIIYATAENSVLGAKAA 242
Cdd:COG0683 192 IKAAGPDAVFLAGYGGDAALFIKQA 216
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-96 |
1.94e-03 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 39.55 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 1 MRvRKILSLGIAGILAIGMLTGCSMEGPSKSDNKGGSDKKDLTIGVSTITLQhqffiDIDEGIKEKAKELGVKVIVNDPD 80
Cdd:COG2182 1 MK-RRLLAALALALALALALAACGSGSSSSGSSSAAGAGGTLTVWVDDDEAE-----ALEEAAAAFEEEPGIKVKVVEVP 74
|
90
....*....|....*.
gi 489531185 81 QDvakqtSAIEDFIQQ 96
Cdd:COG2182 75 WD-----DLREKLTTA 85
|
|
| Med |
COG1744 |
Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC superfamily, includes NupN [Signal ... |
60-297 |
3.81e-03 |
|
Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC superfamily, includes NupN [Signal transduction mechanisms];
Pssm-ID: 441350 Cd Length: 300 Bit Score: 38.58 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 60 DEGIKEKAKELGVKVIV--NDPDQDVAKqtsAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAFEKMPVVTVD-AVLNTENI 136
Cdd:COG1744 26 YEGLEAAEKELGVEVKYveSVPEADYEP---ALRQLAEQGYDLIIGVGFGFADALLKVAKEFPDVKFAIIDgYVDGAPNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 137 TSYVGTV---SYDAG---------KKLGeytkkYIdeklGGKsEIAIVTDLksqiqmqrIDGFKDALKgSAN--VKIL-- 200
Cdd:COG1744 103 ASYFFREeegSYLAGvlaalmtktGKVG-----FV----GGM-PIPEVIRF--------INGFALGAK-YVNpdIKVLvv 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 201 --NSQpgYDREESLNTVENLIQSNpdVDIIYATAENSVLGA-KAAlesAKNKDVKIVGF--DLTEEASsgitdGTILA-M 274
Cdd:COG1744 164 ytGSF--SDPAKGKEAALALIDQG--ADVIFQAAGGTGVGViQAA---KEAGKVYAIGVdsDQSALAP-----DVVLTsA 231
|
250 260
....*....|....*....|...
gi 489531185 275 IqqqpKEMGRLAVEAVVKAIKGE 297
Cdd:COG1744 232 V----KRVDVAVYDAVKAVLDGT 250
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
43-305 |
4.49e-03 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 38.35 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 43 TIGVSTITlQHQFFIDIDEGIKEKAKELG----VKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGTdNSAIvpAVEGA 118
Cdd:COG2984 4 KIGILQIS-EHPALDAAREGFKDGLAEAGygknLKLDYQNAQGDQATAAQIAAKLVADKPDLIVAIGT-PAAQ--AAANA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 119 FEKMPVV------TVDAVL------NTENITsyvGTVSYDAGKKLGEYTKKYidekLGGKSEIAIVTD---LKSQIQMQR 183
Cdd:COG2984 80 TKDIPVVftavtdPVGAGLvkslekPGGNVT---GVSDLLPIEKQLELIKKL----LPDAKRIGVLYNpseANSVAQVEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 184 IdgfKDALKgSANVKIlNSQPGYDREESLNTVENLIqsnPDVDIIYATAENSVL-GAKAALESAKNKDVKIVGFDlteea 262
Cdd:COG2984 153 L---KKAAK-KLGLEL-VEATVTSSNEIQQALQSLA---GKVDAIYVPTDNTVVsALEAIAKVAARAKIPVFGGD----- 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489531185 263 SSGITDGtILAMIQQQPKEMGRLAVEAVVKAIKGEKVeKNIPV 305
Cdd:COG2984 220 DSSVKAG-ALAGYGIDYYELGRQAAEMALRILKGEKP-ADIPV 260
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
55-145 |
5.24e-03 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 38.05 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 55 FFIDIDEGIKEKAKELGVKVIVNDPDQDVAKQTSAIEDFIQQNVDGMIVLGT----DNS--------AIVPAVEGAFE-K 121
Cdd:PRK11041 49 FFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFVNLIITKQIDGMLLLGSrlpfDASkeeqrnlpPMVMANEFAPElE 128
|
90 100
....*....|....*....|....
gi 489531185 122 MPVVTVDavlnteNITSYVGTVSY 145
Cdd:PRK11041 129 LPTVHID------NLTAAFEAVNY 146
|
|
| PBP1_BmpA_Med_PnrA-like |
cd06304 |
periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and ... |
61-257 |
5.31e-03 |
|
periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and various putative lipoproteins from other bacteria; Periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and various putative lipoproteins from other bacteria. These outer membrane proteins include Med, a cell-surface localized protein regulating the competence transcription factor gene comK in Bacillus subtilis, and PnrA, a periplasmic purine nucleoside binding protein of an ATP-binding cassette (ABC) transport system in Treponema pallidum. All contain the type 1 periplasmic sugar-binding protein-like fold.
Pssm-ID: 380527 Cd Length: 262 Bit Score: 37.90 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 61 EGIKEKAKELGVKVIVNDpDQDVAKQTSAIEDFIQQNVDGMIVLGTDNSAIVPAVEGAF-EKMPVVTVDAVLNTENITSY 139
Cdd:cd06304 21 EGLKKAAKELGIEVAYSE-NVPPADAERVLRDYASQGYDLIIGHGFQFEDAAKEVAPEFpDTKFVVISGNVTAAPNVASY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531185 140 V---GTVSYDAGKKLGEYTKKyideklgGKseIAIV--TDLKSQIQMqrIDGFKDALKgSAN--VKILNSQPG--YDREE 210
Cdd:cd06304 100 DfkeEEGGYLAGALAALMTKT-------GK--VGFVggMEIPPIKRL--LAGFEAGAK-AVNpdAKVLVAYTGswDDVAK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489531185 211 SLNTVENLIQSNpdVDIIYATAENSVLGakaALESAKNKDVKIVGFD 257
Cdd:cd06304 168 AKEAALAMIAQG--ADVIFGAANAAGLG---VIEAAKEKGVYAIGNV 209
|
|
| |
