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Conserved domains on  [gi|16129851|ref|NP_416414|]
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arabinose ABC transporter periplasmic binding protein [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

arabinose ABC transporter substrate-binding protein( domain architecture ID 10107481)

arabinose ABC transporter substrate-binding protein serves as the initial receptor in the high-affinity L-arabinose membrane transport system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 27-321 4.69e-141

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: 400.51  E-value: 4.69e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP-DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYD 105
Cdd:cd01540   1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKmDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 106 MKVIAVDDQFVNakGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGW-DVKESAVMAITANELDTARRRTTGSMDALKA 184
Cdd:cd01540  81 IPVIAVDDQLVD--ADPMKIVPFVGIDAYKIGEAVGEWLAKEMKKRGWdDVKEVGVLAITMDTLSVCVDRTDGAKDALKA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 185 AGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHWLIVGMNDSTVLGGVRATEGQGFKAADIIGIGINGVDAVSELS 264
Cdd:cd01540 159 AGFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKHWLVVGCNDEGVLGAVRALEQAGFDAEDIIGVGIGGYLAADEEF 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129851 265 KAQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDVEPPKFTeVTDVVLITRDNFKEEL 321
Cdd:cd01540 239 KKQPTGFKASLYISPDKHGYIAAEELYNWITDGKPPPAET-LTDGVIVTRDNYKEVM 294
 
Name Accession Description Interval E-value
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 27-321 4.69e-141

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: 400.51  E-value: 4.69e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP-DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYD 105
Cdd:cd01540   1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKmDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 106 MKVIAVDDQFVNakGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGW-DVKESAVMAITANELDTARRRTTGSMDALKA 184
Cdd:cd01540  81 IPVIAVDDQLVD--ADPMKIVPFVGIDAYKIGEAVGEWLAKEMKKRGWdDVKEVGVLAITMDTLSVCVDRTDGAKDALKA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 185 AGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHWLIVGMNDSTVLGGVRATEGQGFKAADIIGIGINGVDAVSELS 264
Cdd:cd01540 159 AGFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKHWLVVGCNDEGVLGAVRALEQAGFDAEDIIGVGIGGYLAADEEF 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129851 265 KAQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDVEPPKFTeVTDVVLITRDNFKEEL 321
Cdd:cd01540 239 KKQPTGFKASLYISPDKHGYIAAEELYNWITDGKPPPAET-LTDGVIVTRDNYKEVM 294
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 25-320 4.67e-105

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: 308.67  E-value: 4.67e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851    25 NLKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTL-NAIDSLAASGAKGFVICTPDPKlGSAIVAKARG 103
Cdd:pfam00532   1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLtNAIDLLLASGADGIIITTPAPS-GDDITAKAEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851   104 YDMKVIAVDDQFVNAkgkpmDTVPLVMMAATKIGERQGQELYKEMQKRGwdvkeSAVMAITANELdTARRRTTGSMDALK 183
Cdd:pfam00532  80 YGIPVIAADDAFDNP-----DGVPCVMPDDTQAGYESTQYLIAEGHKRP-----IAVMAGPASAL-TARERVQGFMAALA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851   184 AAGFPeKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQG-FKAADIIGIGINGVDAVSE 262
Cdd:pfam00532 149 AAGRE-VKIYHVATGDNDIPDAALAANAMLVSHPTID--AIVAMNDEAAMGAVRALLKQGrVKIPDIVGIGINSVVGFDG 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129851   263 LSKAQATGFYGSLLPSPDVH----GYKSSEMLYNWVakdvepPKFTEVTDVVLITRDNFKEE 320
Cdd:pfam00532 226 LSKAQDTGLYLSPLTVIQLPrqllGIKASDMVYQWI------PKFREHPRVLLIPRDFFKET 281
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 7-316 1.12e-35

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: 131.20  E-value: 1.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851   7 ALAAIGLAAVMSQSAMAENLKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVI-KIAVPDGEKTLNAIDSLAASGAKGFV 85
Cdd:COG1879  15 ALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIvVDAEGDAAKQISQIEDLIAQGVDAII 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  86 ICTPDPKLGSAIVAKARGYDMKVIAVDDQFvnakgKPMDTVPLVMMAATKIGERQGQELYKEMQKRGwdvkeSAVMAITA 165
Cdd:COG1879  95 VSPVDPDALAPALKKAKAAGIPVVTVDSDV-----DGSDRVAYVGSDNYAAGRLAAEYLAKALGGKG-----KVAILTGS 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 166 NELDTARRRTTGSMDALKAagFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfK 245
Cdd:COG1879 165 PGAPAANERTDGFKEALKE--YPGIKVVAEQYADWDREKALEVMEDLLQAHPDID--GIFAANDGMALGAAQALKAAG-R 239

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129851 246 AADIIGIGINGV-DAVSELskaQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDvEPPKFTeVTDVVLITRDN 316
Cdd:COG1879 240 KGDVKVVGFDGSpEALQAI---KDGTIDATVAQDPYLQGYLAVDAALKLLKGK-EVPKEI-LTPPVLVTKEN 306
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
1-258 1.02e-05

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 46.62  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851    1 MHKFTKALAAIGLAAVMSQSAMAENlKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKI-AVPDGEKTLNAIDSLAAS 79
Cdd:PRK10653   3 MKKLATLVSAVALSATVSANAMAKD-TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLdSQNNPAKELANVQDLTVR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851   80 GAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDqfVNAKGKPM-----DTVPLVMMAATKIGERQGQELyKEMQKRGwd 154
Cdd:PRK10653  82 GTKILLINPTDSDAVGNAVKMANQANIPVITLDR--GATKGEVVshiasDNVAGGKMAGDFIAKKLGEGA-KVIQLEG-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  155 vkesavMAITAneldTARRRTTGSMDALKAAGFpEKQIYQvptksndiPGAFD------AANSMLVQHPEVKhwLIVGMN 228
Cdd:PRK10653 157 ------IAGTS----AARERGEGFKQAVAAHKF-NVLASQ--------PADFDrtkglnVMQNLLTAHPDVQ--AVFAQN 215

                        250       260       270
                 ....*....|....*....|....*....|
gi 16129851  229 DSTVLGGVRATEGQGfkAADIIGIGINGVD 258
Cdd:PRK10653 216 DEMALGALRALQTAG--KSDVMVVGFDGTP 243
 
Name Accession Description Interval E-value
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 27-321 4.69e-141

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: 400.51  E-value: 4.69e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP-DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYD 105
Cdd:cd01540   1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKmDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 106 MKVIAVDDQFVNakGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGW-DVKESAVMAITANELDTARRRTTGSMDALKA 184
Cdd:cd01540  81 IPVIAVDDQLVD--ADPMKIVPFVGIDAYKIGEAVGEWLAKEMKKRGWdDVKEVGVLAITMDTLSVCVDRTDGAKDALKA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 185 AGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHWLIVGMNDSTVLGGVRATEGQGFKAADIIGIGINGVDAVSELS 264
Cdd:cd01540 159 AGFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKHWLVVGCNDEGVLGAVRALEQAGFDAEDIIGVGIGGYLAADEEF 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16129851 265 KAQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDVEPPKFTeVTDVVLITRDNFKEEL 321
Cdd:cd01540 239 KKQPTGFKASLYISPDKHGYIAAEELYNWITDGKPPPAET-LTDGVIVTRDNYKEVM 294
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 25-320 4.67e-105

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: 308.67  E-value: 4.67e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851    25 NLKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTL-NAIDSLAASGAKGFVICTPDPKlGSAIVAKARG 103
Cdd:pfam00532   1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLtNAIDLLLASGADGIIITTPAPS-GDDITAKAEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851   104 YDMKVIAVDDQFVNAkgkpmDTVPLVMMAATKIGERQGQELYKEMQKRGwdvkeSAVMAITANELdTARRRTTGSMDALK 183
Cdd:pfam00532  80 YGIPVIAADDAFDNP-----DGVPCVMPDDTQAGYESTQYLIAEGHKRP-----IAVMAGPASAL-TARERVQGFMAALA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851   184 AAGFPeKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQG-FKAADIIGIGINGVDAVSE 262
Cdd:pfam00532 149 AAGRE-VKIYHVATGDNDIPDAALAANAMLVSHPTID--AIVAMNDEAAMGAVRALLKQGrVKIPDIVGIGINSVVGFDG 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129851   263 LSKAQATGFYGSLLPSPDVH----GYKSSEMLYNWVakdvepPKFTEVTDVVLITRDNFKEE 320
Cdd:pfam00532 226 LSKAQDTGLYLSPLTVIQLPrqllGIKASDMVYQWI------PKFREHPRVLLIPRDFFKET 281
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 7-316 1.12e-35

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: 131.20  E-value: 1.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851   7 ALAAIGLAAVMSQSAMAENLKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVI-KIAVPDGEKTLNAIDSLAASGAKGFV 85
Cdd:COG1879  15 ALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIvVDAEGDAAKQISQIEDLIAQGVDAII 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  86 ICTPDPKLGSAIVAKARGYDMKVIAVDDQFvnakgKPMDTVPLVMMAATKIGERQGQELYKEMQKRGwdvkeSAVMAITA 165
Cdd:COG1879  95 VSPVDPDALAPALKKAKAAGIPVVTVDSDV-----DGSDRVAYVGSDNYAAGRLAAEYLAKALGGKG-----KVAILTGS 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 166 NELDTARRRTTGSMDALKAagFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfK 245
Cdd:COG1879 165 PGAPAANERTDGFKEALKE--YPGIKVVAEQYADWDREKALEVMEDLLQAHPDID--GIFAANDGMALGAAQALKAAG-R 239

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129851 246 AADIIGIGINGV-DAVSELskaQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDvEPPKFTeVTDVVLITRDN 316
Cdd:COG1879 240 KGDVKVVGFDGSpEALQAI---KDGTIDATVAQDPYLQGYLAVDAALKLLKGK-EVPKEI-LTPPVLVTKEN 306
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 27-310 1.98e-31

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: 118.82  E-value: 1.98e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEV-IKIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYD 105
Cdd:cd01536   1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELvVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 106 MKVIAVDDQFvnakGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGwdvkesAVMAITANEL-DTARRRTTGSMDALKA 184
Cdd:cd01536  81 IPVVAVDTDI----DGGGDVVAFVGTDNYEAGKLAGEYLAEALGGKG------KVAILEGPPGsSTAIDRTKGFKEALKK 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 185 agFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIGIGINGVDAVseLS 264
Cdd:cd01536 151 --YPDIEIVAEQPANWDRAKALTVTENLLQANPDID--AVFAANDDMALGAAEALKAAG-RTGDIKIVGVDGTPEA--LK 223

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 16129851 265 KAQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDvEPPKFTEVTDVV 310
Cdd:cd01536 224 AIKDGELDATVAQDPYLQGYLAVEAAVKLLNGE-KVPKEILTPVTL 268
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 27-316 2.78e-21

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 91.65  E-value: 2.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTL--NAIDsLAASGAKGFVICTPDPKLGSAIVAKARGY 104
Cdd:cd06319   1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQvtNAND-LIAQGVDGIIISPTNSSAAPTVLDLANEA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 105 DMKVIAVDdqfVNAKGKpmDTVPLVMMAATKIGERQGQELYKEMQKRGWDVKESAVMAITANElDTARRRTTGSMDALKA 184
Cdd:cd06319  80 KIPVVIAD---IGTGGG--DYVSYIISDNYDGGYQAGEYLAEALKENGWGGGSVGIIAIPQSR-VNGQARTAGFEDALEE 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 185 AGFPEKQIYQVPTKSNDipGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIGIGINGVDAVSELS 264
Cdd:cd06319 154 AGVEEVALRQTPNSTVE--ETYSAAQDLLAANPDIK--GIFAQNDQMAQGALQAIEEAG-RTGDILVVGFDGDPEALDLI 228

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 16129851 265 KAQatGFYGSLLPSPDVHGYKSSEMLYNWVAKDvEPPKFTEVTDVVLITRDN 316
Cdd:cd06319 229 KDG--KLDGTVAQQPFGMGARAVELAIQALNGD-NTVEKEIYLPVLLVTSEN 277
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 29-292 3.10e-13

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: 68.49  E-value: 3.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851    29 GFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKI--AVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDM 106
Cdd:pfam13407   2 GVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVgpAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851   107 KVIAVDDQFVNAKGkpmdtVPLVMMAATKIGERQGQELYKEMQKRGwdvkesAVMAITANELDT-ARRRTTGSMDALKaA 185
Cdd:pfam13407  82 PVVTFDSDAPSSPR-----LAYVGFDNEAAGEAAGELLAEALGGKG------KVAILSGSPGDPnANERIDGFKKVLK-E 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851   186 GFPEKQIYQVPTKSNDIPG-AFDAANSMLVQHP-EVKHwlIVGMNDSTVLGGVRATEGQGFKAADIIGiginGVDAVSEL 263
Cdd:pfam13407 150 KYPGIKVVAEVEGTNWDPEkAQQQMEALLTAYPnPLDG--IISPNDGMAGGAAQALEAAGLAGKVVVT----GFDATPEA 223

                         250       260       270
                  ....*....|....*....|....*....|
gi 16129851   264 SKAQATG-FYGSLLPSPDVHGYKSSEMLYN 292
Cdd:pfam13407 224 LEAIKDGtIDATVLQDPYGQGYAAVELAAA 253
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 27-313 1.32e-12

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: 66.87  E-value: 1.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP---DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARG 103
Cdd:cd20008   1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPAteaDIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAADA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 104 yDMKVIAVDDQfVNAKgkpmDTVPLVMMAATKIGERQGQELYKEMQKRGWDVKESAVMAITANElDTARRRTTGSMDALK 183
Cdd:cd20008  81 -GIPVVLVDSG-ANTD----DYDAFLATDNVAAGALAADELAELLKASGGGKGKVAIISFQAGS-QTLVDREEGFRDYIK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 184 AAgFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHwlIVGMNDSTVLGGVRATEGQGfKAADIIGIginGVDAVSEL 263
Cdd:cd20008 154 EK-YPDIEIVDVQYSDGDIAKALNQTTDLLTANPDLVG--IFGANNPSAVGVAQALAEAG-KAGKIVLV---GFDSSPDE 226

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 16129851 264 SKAQATGF-YGSLLPSPDVHGYKSSEMLYNWVAKDVEPPKFTEvTDVVLIT 313
Cdd:cd20008 227 VALLKSGViKALVVQDPYQMGYEGVKTAVKALKGEEIVEKNVD-TGVTVVT 276
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 27-316 2.65e-12

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: 66.28  E-value: 2.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKI-AVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYD 105
Cdd:cd06318   1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTdAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 106 MKVIAVDDQfVNAKGKPMDTvplVMMAATKIGERQGQELYKEMQKRgwDVKESAVMAITANELDTARRRT--TGSMDA-L 182
Cdd:cd06318  81 IPVITVDSA-LDPSANVATQ---VGRDNKQNGVLVGKEAAKALGGD--PGKIIELSGDKGNEVSRDRRDGflAGVNEYqL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 183 KAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIgigINGVDAVSE 262
Cdd:cd06318 155 RKYGKSNIKVVAQPYGNWIRSGAVAAMEDLLQAHPDIN--VVYAENDDMALGAMKALKAAG-MLDKVK---VAGADGQKE 228

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16129851 263 LSKAQATGFYG-SLLPSPDVHGYKSSEMLYNWVAKDVEPPKFTEVTDvVLITRDN 316
Cdd:cd06318 229 ALKLIKDGKYVaTGLNDPDLLGKTAVDTAAKVVKGEESFPEFTYTPT-ALITKDN 282
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 32-313 1.20e-08

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: 55.02  E-value: 1.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  32 VKQPEEPWFQTEWKFADKAGKDLGFEViKIAVPDGEKTLNA--IDSLAASGAKGfVICTP-DPKLGSAIVAKARGYDMKV 108
Cdd:cd19967   6 VSTPNNPFFVVEAEGAKEKAKELGYEV-TVFDHQNDTAKEAelFDTAIASGAKA-IILDPaDADASIAAVKKAKDAGIPV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 109 IAVDDQfVNAKGKPMDTVPLVMMAATKIGerqGQELYKEMQKRGWDVKesavmaITANELDT-ARRRTTGSMDALKaaGF 187
Cdd:cd19967  84 FLIDRE-INAEGVAVAQIVSDNYQGAVLL---AQYFVKLMGEKGLYVE------LLGKESDTnAQLRSQGFHSVID--QY 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 188 PEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIGIGING----VDAVSEl 263
Cdd:cd19967 152 PELKMVAQQSADWDRTEAFEKMESILQANPDIK--GVICGNDEMALGAIAALKAAG-RAGDVIIVGFDGsndvRDAIKE- 227

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 16129851 264 SKAQATGfygslLPSPDVHGYKSSEMLYNWVAKDVEPPKFTEVTDVVLIT 313
Cdd:cd19967 228 GKISATV-----LQPAKLIARLAVEQADQYLKGGSTGKEEKQLFDCVLIT 272
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 44-314 1.61e-08

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 54.93  E-value: 1.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  44 WKF----ADKAGKDLGFEVIKIAvPDGEKTLNA----IDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDdqf 115
Cdd:cd20004  14 WKSvkagAEKAAQELGVEIYWRG-PSREDDVEAqiqiIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIID--- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 116 vnakgKPMDTVPLVMMAAT---KIGERQGQELYKEMQKRGwdvkeSAVMAITANELDTARRRTTGSMDALKaAGFPEKQI 192
Cdd:cd20004  90 -----SDLGGDAVISFVATdnyAAGRLAAKRMAKLLNGKG-----KVALLRLAKGSASTTDRERGFLEALK-KLAPGLKV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 193 YQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIGIGIngvDAVSELSKA-QATGF 271
Cdd:cd20004 159 VDDQYAGGTVGEARSSAENLLNQYPDVD--GIFTPNESTTIGALRALRRLG-LAGKVKFIGF---DASDLLLDAlRAGEI 232

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 16129851 272 YGSLLPSPDVHGYKSSEMLYNwVAKDVEPPKFTeVTDVVLITR 314
Cdd:cd20004 233 SALVVQDPYRMGYLGVKTAVA-ALRGKPVPKRI-DTGVVLVTK 273
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 27-316 8.47e-08

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: 52.65  E-value: 8.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP---DGEKTLNAIDSLAASGAKGFVIcTP--DPKLGSAIV-AK 100
Cdd:cd06320   1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAAPsetDTQGQLNLLETMLNKGYDAILV-SPisDTNLIPPIEkAN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 101 ARGydMKVIAVDDQFVNAKGKPM--DTVPLVMMAATKIGERQGQELYKEMQKRGwdvkESAVMAITANElDTARRRTTGS 178
Cdd:cd06320  80 KKG--IPVINLDDAVDADALKKAggKVTSFIGTDNVAAGALAAEYIAEKLPGGG----KVAIIEGLPGN-AAAEARTKGF 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 179 MDALKAAgfPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHwlIVGMNDSTVLGGVRATEGQGfKAADIIGIGINGV- 257
Cdd:cd06320 153 KETFKKA--PGLKLVASQPADWDRTKALDAATAILQAHPDLKG--IYAANDTMALGAVEAVKAAG-KTGKVLVVGTDGIp 227

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129851 258 DAVSELSKAQATgfyGSLLPSPDVHGYKSSEMLYnWVAKDVEPPKFTeVTDVVLITRDN 316
Cdd:cd06320 228 EAKKSIKAGELT---ATVAQYPYLEGAMAVEAAL-RLLQGQKVPAVV-ATPQALITKDN 281
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 47-315 1.58e-07

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 51.86  E-value: 1.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  47 ADKAGKDLGFEVIKIAvPDGE----KTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDdqfvnaKGKP 122
Cdd:cd20005  21 AEQAAKELGVKITFEG-PDTEsdvdKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFD------SGVP 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 123 MDTVplVMMAAT---KIGERQGQELYKEMQKRGwdvkESAVMAITANELdTARRRTTGSMDALKAAgFPEKQIYQVPTKS 199
Cdd:cd20005  94 SDLP--LATVATdnyAAGALAADHLAELIGGKG----KVAIVAHDATSE-TGIDRRDGFKDEIKEK-YPDIKVVNVQYGV 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 200 NDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIGIginGVDAVSELSKAQATG-FYGSLLPS 278
Cdd:cd20005 166 GDHAKAADIAKAILQANPDLK--GIYATNEGAAIGVANALKEMG-KLGKIKVV---GFDSGEAQIDAIKNGvIAGSVTQN 239

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 16129851 279 PDVHGYKSSEMLYNwVAKDVEPPKFTEvTDVVLITRD 315
Cdd:cd20005 240 PYGMGYKTVKAAVK-ALKGEEVEKLID-TGAKWYDKD 274
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 27-268 2.85e-07

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: 51.05  E-value: 2.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVI-KIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYD 105
Cdd:cd19992   1 KIGVSFPTQQEERWQKDKEYMEEEAKELGVELIfQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 106 MKVIAVDDQFVNAKgkpmdtVPL-VMMAATKIGERQGQELYKEMQKRGWdvkesAVMAITANElDTARRRTTGSMDALKA 184
Cdd:cd19992  81 VPVISYDRLILNAD------VDLyVGRDNYKVGQLQAEYALEAVPKGNY-----VILSGDPGD-NNAQLITAGAMDVLQP 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 185 AGFPE--KQIYQVPTKsndipgAFDAANSMlvqhPEVKHWL---------IVGMNDSTVLGGVRATEGQGFkAADIIgig 253
Cdd:cd19992 149 AIDSGdiKIVLDQYVK------GWSPDEAM----KLVENALtannnnidaVLAPNDGMAGGAIQALKAQGL-AGKVF--- 214

                       250
                ....*....|....*
gi 16129851 254 INGVDAvsELSKAQA 268
Cdd:cd19992 215 VTGQDA--ELAALKR 227
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 27-323 3.39e-07

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: 50.68  E-value: 3.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKI-AVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYD 105
Cdd:cd06309   1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTdANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 106 MKVIAVDDQfVNAKGKPmDTVPLVMMAATKIGERQGQELYKEMQKrgwdvKESAVMAITANE-LDTARRRTTGSMDALKA 184
Cdd:cd06309  81 IPVILVDRT-IDGEDGS-LYVTFIGSDFVEEGRRAAEWLVKNYKG-----GKGNVVELQGTAgSSVAIDRSKGFREVIKK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 185 agFPEKQIyqVPTKSNDI--PGAFDAANSMLVQHPEvKHWLIVGMNDSTVLGGVRATEGQGFKAA-DIIGIGINGV-DAV 260
Cdd:cd06309 154 --HPNIKI--VASQSGNFtrEKGQKVMENLLQAGPG-DIDVIYAHNDDMALGAIQALKEAGLKPGkDVLVVGIDGQkDAL 228

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129851 261 SEL--SKAQATGFYgsllpSPDvHGYKSSEMLYNWVAKDvEPPKFTEVTDVVlITRDNFKEELEK 323
Cdd:cd06309 229 EAIkaGELNATVEC-----NPL-FGPTAFDTIAKLLAGE-KVPKLIIVEERL-FDKDNAAEELEP 285
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 38-313 3.70e-07

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: 50.75  E-value: 3.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  38 PWFQTEWKFADKAGKDLGFEViKIAVPDGEKTLNA----IDSLAASGAKGFVICTPDPK-LGSAIvAKARGYDMKVIAVD 112
Cdd:cd06321  12 PFFVAMVRGAEEAAAEINPGA-KVTVVDARYDLAKqfsqIDDFIAQGVDLILLNAADSAgIEPAI-KRAKDAGIIVVAVD 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 113 dqfVNAKGkpMDTVplVMMAATKIGERQGQELYKEMQKRGwdvkesAVMAITANELDTARRRTTGSMDALKAagFPEKQI 192
Cdd:cd06321  90 ---VAAEG--ADAT--VTTDNVQAGYLACEYLVEQLGGKG------KVAIIDGPPVSAVIDRVNGCKEALAE--YPGIKL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 193 YQVPTKSNDIPGAFDAANSMLVQHPEVKHwlIVGMNDSTVLGGVRATEGQGFKaaDIIGIGINGV-DAVSELsKAQATGF 271
Cdd:cd06321 155 VDDQNGKGSRAGGLSVMTRMLTAHPDVDG--VFAINDPGAIGALLAAQQAGRD--DIVITSVDGSpEAVAAL-KREGSPF 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 16129851 272 YGSLLPSPDVHGYKSSEMLYNwVAKDVEPPKFTEVTDVVLIT 313
Cdd:cd06321 230 IATAAQDPYDMARKAVELALK-ILNGQEPAPELVLIPSTLVT 270
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 27-313 6.62e-07

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: 49.89  E-value: 6.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP--DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGY 104
Cdd:cd06314   1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQksDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 105 DMKVIAVDDQFVNAKGKpmdtvplvmmaaTKIG---ERQGQELYKEMQKRgwDVKESAVMAITAN-ELDTARRRTTGSMD 180
Cdd:cd06314  81 GIPVITFDSDAPDSKRL------------AYIGtdnYEAGREAGELMKKA--LPGGGKVAIITGGlGADNLNERIQGFKD 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 181 ALKAAgfpeKQIYQVPTKSN--DIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIGIGINGVD 258
Cdd:cd06314 147 ALKGS----PGIEIVDPLSDndDIAKAVQNVEDILKANPDLD--AIFGVGAYNGPAIAAALKDAG-KVGKVKIVGFDTLP 219

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16129851 259 AVSELSKAQATgfYGSLLPSPDVHGYKSSEMLYNWVAKDVEPPKFTEvTDVVLIT 313
Cdd:cd06314 220 ETLQGIKDGVI--AATVGQRPYEMGYLSVKLLYKLLKGGKPVPDVID-TGVDVVT 271
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
 65-306 6.95e-07

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: 49.94  E-value: 6.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  65 DGEKTLNAIDSLAASGAKGFVICTPDPKlGSAIVAKARGYDMKVIavddqFVNAKGKPMDTVPLVMMAATKIGERQGQEL 144
Cdd:cd01537  40 DQEKQNDQIDVLLAKRVKGLAINLVDPA-AAGVAEKARGQNVPVV-----FFDKEPSRYDKAYYVITDSKEGGIIQGDLL 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 145 YKEMQKRgwdvkesavMAITANELD--TARRRTTGSMDALKAAGFPEKQIyQVPTKSNDIPGAFDAANSMLVQhPEVKHW 222
Cdd:cd01537 114 AKHGHIQ---------IVLLKGPLGhpDAEARLAGVIKELNDKGIKTEQL-QLDTGDWDTASGKDKMDQWLSG-PNKPTA 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 223 LIVGmNDSTVLGGVRATEGQGFKAADiiGIGINGVDAVSELSKaqATGFYGSLLPSPDVHGYKSSEMLYNWVAKDVEPPK 302
Cdd:cd01537 183 VIAN-NDAMAMGAVEALKEHGLRVPS--DISVFGYDALPEALK--SGPLLTTILQDANNLGKTTFDLLLNLADNWKIDNK 257


                ....
gi 16129851 303 FTEV 306
Cdd:cd01537 258 VVRV 261
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 27-313 1.60e-06

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: 48.83  E-value: 1.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKI-AVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYD 105
Cdd:cd06323   1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLdAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 106 MKVIAVDDQFvnAKGKpmdTVPLVMMAATKIGERQGQELYKEMQKRGWDVKESAVMAITAneldtARRRTTGSMDALKAa 185
Cdd:cd06323  81 IPVITVDRSV--TGGK---VVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSA-----ARERGKGFHNAIAK- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 186 gFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHwlIVGMNDSTVLGGVRATEGQGFKaaDIIGIGINGV-DAVSELS 264
Cdd:cd06323 150 -YPKINVVASQTADFDRTKGLNVMENLLQAHPDIDA--VFAHNDEMALGAIQALKAAGRK--DVIVVGFDGTpDAVKAVK 224

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 16129851 265 KAQatgFYGSLLPSPDVHGYKSSEMLYNWVAKDVePPKFTEVtDVVLIT 313
Cdd:cd06323 225 DGK---LAATVAQQPEEMGAKAVETADKYLKGEK-VPKKIPV-PLKLVT 268
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 35-262 2.68e-06

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: 48.37  E-value: 2.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  35 PEEPWFQTEWKFADKAGKDLGFEV-IKIAVPDGEKTLNAIDSLAASGAK-GFVICTPDPKLGSAIVAKARGYDMKVIAVD 112
Cdd:cd06324  10 EDEPFWQNVTRFMQAAAKDLGIELeVLYANRNRFKMLELAEELLARPPKpDYLILVNEKGVAPELLELAEQAKIPVFLIN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 113 DQFVNAK----GKPMDT--------VPlvmmAATKIGERQGQELYKEMQKRGwDVKESAVMAITANELDTA-RRRTTGSM 179
Cdd:cd06324  90 NDLTDEErallGKPREKfkywlgsiVP----DNEQAGYLLAKALIKAARKKS-DDGKIRVLAISGDKSTPAsILREQGLR 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 180 DALKAAgfPEKQIYQVptksndIPG------AFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGFKAADIIGIG 253
Cdd:cd06324 165 DALAEH--PDVTLLQI------VYAnwsedeAYQKTEKLLQRYPDID--IVWAANDAMALGAIDALEEAGLKPGKDVLVG 234


                ....*....
gi 16129851 254 inGVDAVSE 262
Cdd:cd06324 235 --GIDWSPE 241
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 49-300 3.84e-06

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: 47.66  E-value: 3.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  49 KAGKDLGFEVIkIAVPDGE--KTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDdqfVNAKGKPMDtv 126
Cdd:cd06322  23 KEAAELGVKVV-VADANGDlaKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFTVD---VKADGAKVV-- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 127 plvmmaaTKIGERQ---GQELYKEMQKRGWDVKESAVMaITANELDTARRRTTGSMDALKAAgfPEKQIYQVPTKSNDIP 203
Cdd:cd06322  97 -------THVGTDNyagGKLAGEYALKALLGGGGKIAI-IDYPEVESVVLRVNGFKEAIKKY--PNIEIVAEQPGDGRRE 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 204 GAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIGIGINGVDavsELSKAQATG--FYGSLLPSPDV 281
Cdd:cd06322 167 EALAATEDMLQANPDLD--GIFAIGDPAALGALTAIESAG-KEDKIKVIGFDGNP---EAIKAIAKGgkIKADIAQQPDK 240

                       250       260
                ....*....|....*....|
gi 16129851 282 HGYKSSEMLYNWVA-KDVEP 300
Cdd:cd06322 241 IGQETVEAIVKYLAgETVEK 260
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 65-292 4.65e-06

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: 47.19  E-value: 4.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  65 DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDQFVNAkgKPMDTVplVMMAATKIGERQGQEL 144
Cdd:cd19971  40 DQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPVKDT--DLVDST--IASDNYNAGKLCGEDM 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 145 YKEMQKRGwdvkesAVMAITANELDTARRRTTGSMDALKA-AGFpeKQIYQVPTKSnDIPGAFDAANSMLVQHPEVKhwL 223
Cdd:cd19971 116 VKKLPEGA------KIAVLDHPTAESCVDRIDGFLDAIKKnPKF--EVVAQQDGKG-QLEVAMPIMEDILQAHPDLD--A 184

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 224 IVGMNDSTVLGGVRATEGQGFKAadiiGIGINGVDAVSELSKA-QATGFYGSLLPSPDVHGYKSSEMLYN 292
Cdd:cd19971 185 VFALNDPSALGALAALKAAGKLG----DILVYGVDGSPDAKAAiKDGKMTATAAQSPIEIGKKAVETAYK 250
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 65-245 7.07e-06

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: 46.90  E-value: 7.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  65 DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDQFVNAKGKPMDTVPLVmmaatKIGERQGQEL 144
Cdd:cd19995  43 DASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPADYYVSFDNV-----AVGEAQAQSL 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 145 YKEMqkRGWDVKESAVMAITANELDT-ARRRTTGSMDALKAAGFPE--KQIYQVPTKSNDIPGAFDAANSMLVQHPEvKH 221
Cdd:cd19995 118 VDHL--KAIGKKGVNIVMINGSPTDNnAGLFKKGAHEVLDPLGDSGelKLVCEYDTPDWDPANAQTAMEQALTKLGN-NI 194

                       170       180
                ....*....|....*....|....
gi 16129851 222 WLIVGMNDSTVLGGVRATEGQGFK 245
Cdd:cd19995 195 DGVLSANDGLAGGAIAALKAQGLA 218
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
1-258 1.02e-05

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 46.62  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851    1 MHKFTKALAAIGLAAVMSQSAMAENlKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKI-AVPDGEKTLNAIDSLAAS 79
Cdd:PRK10653   3 MKKLATLVSAVALSATVSANAMAKD-TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLdSQNNPAKELANVQDLTVR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851   80 GAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDqfVNAKGKPM-----DTVPLVMMAATKIGERQGQELyKEMQKRGwd 154
Cdd:PRK10653  82 GTKILLINPTDSDAVGNAVKMANQANIPVITLDR--GATKGEVVshiasDNVAGGKMAGDFIAKKLGEGA-KVIQLEG-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  155 vkesavMAITAneldTARRRTTGSMDALKAAGFpEKQIYQvptksndiPGAFD------AANSMLVQHPEVKhwLIVGMN 228
Cdd:PRK10653 157 ------IAGTS----AARERGEGFKQAVAAHKF-NVLASQ--------PADFDrtkglnVMQNLLTAHPDVQ--AVFAQN 215

                        250       260       270
                 ....*....|....*....|....*....|
gi 16129851  229 DSTVLGGVRATEGQGfkAADIIGIGINGVD 258
Cdd:PRK10653 216 DEMALGALRALQTAG--KSDVMVVGFDGTP 243
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 27-269 1.24e-05

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: 46.09  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGK-DLGFEVIKIAVP---DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKAR 102
Cdd:cd19970   1 KVALVMKSLANEFFIEMEKGARKHAKeANGYELLVKGIKqetDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 103 GYDMKVI----AVDDQFVNAKGKPmdtVPLVMMAATKIGERQGQELYKEMQKRGwdvkesAVMAITAN-ELDTARRRTTG 177
Cdd:cd19970  81 DAGIAVInidnRLDADALKEGGIN---VPFVGPDNRQGAYLAGDYLAKKLGKGG------KVAIIEGIpGADNAQQRKAG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 178 SMDALKAAGFpekQIYQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIGIGINGV 257
Cdd:cd19970 152 FLKAFEEAGM---KIVASQSANWEIDEANTVAANLLTAHPDIR--GILCANDNMALGAIKAVDAAG-KAGKVLVVGFDNI 225

                       250
                ....*....|....*
gi 16129851 258 DAVSELSKA---QAT 269
Cdd:cd19970 226 PAVRPLLKDgkmLAT 240
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 65-316 1.43e-05

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: 45.72  E-value: 1.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  65 DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAvddqfVNAKGKPMDTVPLVMMAATKIGERQGQEL 144
Cdd:cd06313  40 DVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAGIPLVG-----VNALIENEDLTAYVGSDDVVAGELEGQAV 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 145 YKEMQKRGWDVKESAVMAITAnELDtarrRTTGSMDALKaagfpekqiyqvptKSNDI------PGAFDAANSMLVqhpe 218
Cdd:cd06313 115 ADRLGGKGNVVILEGPIGQSA-QID----RGKGIENVLK--------------KYPDIkvlaeqTANWSRDEAMSL---- 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 219 VKHWL---------IVGMNDSTVLGGVRATEGQGFKaaDIIGIGINGVDAVseLSKAQATGFYGSLLPSPDVHGYKSSEM 289
Cdd:cd06313 172 MENWLqaygdeidgIIAQNDDMALGALQAVKAAGRD--DIPVVGIDGIEDA--LQAVKSGELIATVLQDAEAQGKGAVEV 247

                       250       260
                ....*....|....*....|....*..
gi 16129851 290 LYNwVAKDVEPPKFTEVtDVVLITRDN 316
Cdd:cd06313 248 AVD-AVKGEGVEKKYYI-PFVLVTKDN 272
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 36-234 2.29e-05

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: 45.34  E-value: 2.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  36 EEPWFQTEWKFADKAGKDLGFEVIKIAVPDG--EKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDd 113
Cdd:cd19965  10 TNPFFQPVKKGMDDACELLGAECQFTGPQTFdvAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAFN- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 114 qfVNAKGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGWDVkesaVMAITANELDTARRRTTGSMDALKAAGFPEKqiY 193
Cdd:cd19965  89 --VDAPGGENARLAFVGQDLYPAGYVLGKRIAEKFKPGGGHV----LLGISTPGQSALEQRLDGIKQALKEYGRGIT--Y 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 16129851 194 QVPTKSNDIPGAFDAANSMLVQHPEVKHWLIVGMNDSTVLG 234
Cdd:cd19965 161 DVIDTGTDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAG 201
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 29-126 3.45e-05

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: 44.77  E-value: 3.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  29 GFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP---DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYD 105
Cdd:cd19973   3 GLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKidgDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAG 82

                        90       100
                ....*....|....*....|.
gi 16129851 106 MKVIAVDDQFvnakgKPMDTV 126
Cdd:cd19973  83 VLVIALDTPT-----DPIDAA 98
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
 27-254 7.09e-05

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: 43.77  E-value: 7.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIA--VPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGY 104
Cdd:cd06302   1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTGptQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 105 DMKVIAVDDQfVNAKGKPMDtvplVMMAATKIgerQGQELYKEMQKRgwdVKESAVMAITANELDTARRRT-TGSMDALK 183
Cdd:cd06302  81 GIKVITWDSD-APPSARDYF----VNQADDEG---LGEALVDSLAKE---IGGKGKVAILSGSLTATNLNAwIKAMKEYL 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129851 184 AAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIGIGI 254
Cdd:cd06302 150 KSKYPDIELVDTYYTDDDQQKAYTQAQNLIQAYPDLK--GIIGVSTTAPPAAAQAVEEAG-KTGKVAVTGI 217
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 35-262 8.36e-05

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: 43.47  E-value: 8.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  35 PEEPWFQTEWKFADKAGKDLGFEViKIAVPDG--EKTLNAIDSLAASGAKGFVICTPDP-KLGSAIVAKARGYDMKVIAV 111
Cdd:cd19966  10 PGDPFWTVVYNGAKDAAADLGVDL-DYVFSSWdpEKMVEQFKEAIAAKPDGIAIMGHPGdGAYTPLIEAAKKAGIIVTSF 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 112 DDqfvnakgkpmdTVPLVMMAATKIG------ERQGQELYKEMQKRGwDVKE--SAVMAITANELDTARRRTTGSMDALK 183
Cdd:cd19966  89 NT-----------DLPKLEYGDCGLGyvgadlYAAGYTLAKELVKRG-GLKTgdRVFVPGLLPGQPYRVLRTKGVIDALK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 184 AAGFpekqIYQVPTKSNDIPGAFDAANSM---LVQHPEVKhwLIVGMNDSTVLGGVRATEGQGFKAADIIGIGI----NG 256
Cdd:cd19966 157 EAGI----KVDYLEISLEPNKPAEGIPVMtgyLAANPDVK--AIVGDGGGLTANVAKYLKAAGKKPGEIPVAGFdlspAT 230


                ....*.
gi 16129851 257 VDAVSE 262
Cdd:cd19966 231 VQAIKS 236
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
 169-243 1.15e-04

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: 42.97  E-value: 1.15e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129851 169 DTARRRTTGSMDALKAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQG 243
Cdd:cd06279 146 SVARERLAGYRDALEEAGLDLDDVPVVEAPGNTEEAGRAAARALLALDPRPT--AILCMSDVLALGALRAARERG 218
PBP1_ABC_unchar_transporter cd06325
type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems ...
 27-118 1.28e-04

type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally.


Pssm-ID: 380548  Cd Length: 282  Bit Score: 42.88  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVkQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTLNAIDSLAASGAKGFVIcTPDPKLGSA---IVAKARG 103
Cdd:cd06325 133 RVGVLY-NPGEPNSVAQLEELEAAAKKLGLELVEVPVSSPADIEQAFASLAGKVADALYV-PTDNTVASArprIAALALK 210

                        90
                ....*....|....*
gi 16129851 104 YDMKVIAVDDQFVNA 118
Cdd:cd06325 211 ARIPVIYSDREFVEA 225
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 47-316 1.56e-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: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 42.75  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  47 ADKAGKDLGFE-VIKIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDQfVNAKgkpmDT 125
Cdd:cd06317  21 AQAAAKDLGVDlVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAV-IPSD----FQ 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 126 VPLVMMAATKIGERQGQELYKEMQKRGWDVKESAVMAITANELDTARRRttGSMDALKAAgfPEKQIYQVPTKSNDIPGA 205
Cdd:cd06317  96 AAQVGVDNLEGGKEIGKYAADYIKAELGGQAKIGVVGALSSLIQNQRQK--GFEEALKAN--PGVEIVATVDGQNVQEKA 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 206 FDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGfKAADIIGIGINGV-DAVSELSKAQAtgFYGSLLPSPDVHGY 284
Cdd:cd06317 172 LSAAENLLTANPDLD--AIYATGEPALLGAVAAVRSQG-RQGKIKVFGWDLTkQAIFLGIDEGV--LQAVVQQDPEKMGY 246

                       250       260       270
                ....*....|....*....|....*....|..
gi 16129851 285 KSSEMLYNwvAKDVEPPKFTEVTDVVLITRDN 316
Cdd:cd06317 247 EAVKAAVK--AIKGEDVEKTIDVPPTIVTKEN 276
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 47-313 9.16e-04

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 40.40  E-value: 9.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  47 ADKAGKDLGFEVIKIAVP---DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDdqfvnAKGKPM 123
Cdd:cd06310  21 AEAAAKDLGVKIIFVGPEseeDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPVIVID-----SGIKGD 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 124 DTVPLVMMAATKIGERQGQELYKEMQKRGwdvkESAVMAITANElDTARRRTTGSMDALKAAGfPEKQIYQVPTKSNDIP 203
Cdd:cd06310  96 AYLSYIATDNYAAGRLAAQKLAEALGGKG----KVAVLSLTAGN-STTDQREEGFKEYLKKHP-GGIKVLASQYAGSDYA 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 204 GAFDAANSMLVQHPEVKHwlIVGMNDSTVLGGVRATEGQGFKAAdiigIGINGVDAVSELSKAQATG-FYGSLLPSPDVH 282
Cdd:cd06310 170 KAANETEDLLGKYPDIDG--IFATNEITALGAAVAIKSRKLSGQ----IKIVGFDSQEELLDALKNGkIDALVVQNPYEI 243

                       250       260       270
                ....*....|....*....|....*....|.
gi 16129851 283 GYKSSEMLYNwVAKDVEPPKFTEvTDVVLIT 313
Cdd:cd06310 244 GYEGIKLALK-LLKGEEVPKNID-TGAELIT 272
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
 34-144 1.12e-03

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: 40.31  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  34 QPEEPWFQTEwKFADKAGKDLGFEV-IKIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVD 112
Cdd:cd19994   9 KSEERWIKDG-ENLKSELEEAGYTVdLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYD 87

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16129851 113 DQfvnakgkPMDTvPLVMMAAT----KIGERQGQEL 144
Cdd:cd19994  88 RL-------IMNT-DAVDYYVTfdneKVGELQGQYL 115
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
 27-112 1.13e-03

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: 39.91  E-value: 1.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQ-PEEPWFQTEWKFADKAgKDLGFEVI-KIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGY 104
Cdd:cd19991   1 KIGFSMDSlRVERWQRDRDYFVKKA-KELGAEVIvQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKA 79


                ....*...
gi 16129851 105 DMKVIAVD 112
Cdd:cd19991  80 GVPVLAYD 87
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
 49-152 1.37e-03

ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 39.73  E-value: 1.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  49 KAGKDLGFEV-IKIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDqfvNAKGKPMD--- 124
Cdd:COG4213  26 AALKELGYEVdVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVIAYDR---LILNSDVDyyv 102

                        90       100
                ....*....|....*....|....*...
gi 16129851 125 TVPLVmmaatKIGERQGQELYKEMQKRG 152
Cdd:COG4213 103 SFDNV-----KVGELQGQYLVDGLPLKG 125
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
 65-301 2.40e-03

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: 39.10  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  65 DGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIavddqFVNAkgKPMDtvpLVMMAATKI-------- 136
Cdd:cd01539  42 DQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVI-----FFNR--EPSR---EDLKSYDKAyyvgtdae 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 137 --GERQGQELYKEMQK-RGWDVKESAVMAIT-----ANELDTArRRTTGSMDALKAAGFPEKQIyQVPTKSNDIPGAFDA 208
Cdd:cd01539 112 esGIMQGEIIADYWKAnPEIDKNGDGKIQYVmlkgePGHQDAI-ARTKYSVKTLNDAGIKTEQL-AEDTANWDRAQAKDK 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 209 ANSMLVQHP---EVkhwlIVGMNDSTVLGGVRATEGQGFKAADII-GIGINGVDAVSELSKAQATGF-YGSLLPSPDVHG 283
Cdd:cd01539 190 MDAWLSKYGdkiEL----VIANNDDMALGAIEALKAAGYNTGDGDkYIPVFGVDATPEALEAIKEGKmLGTVLNDAKAQA 265

                       250
                ....*....|....*...
gi 16129851 284 YKSSEMLYNwVAKDVEPP 301
Cdd:cd01539 266 KAIYELAKN-LANGKEPL 282
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
 28-252 2.54e-03

ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 38.78  E-value: 2.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  28 LGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIkIAV----PDGEKTLnaIDSLAASGAKGfVICTPDPKlGSAIVAKARG 103
Cdd:cd06280   2 IGLIVPDITNPFFTTIARGIEDAAEKHGYQVI-LANtdedPEKEKRY--LDSLLSKQVDG-IILAPSAG-PSRELKRLLK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 104 YDMKVIAVDDQFvnaKGKPMDTVplvmMAATKIGERQG-QELYKEMQKRgwdvkesaVMAITAN-ELDTARRRTTGSMDA 181
Cdd:cd06280  77 HGIPIVLIDREV---EGLELDLV----AGDNREGAYKAvKHLIELGHRR--------IGLITGPlEISTTRERLAGYREA 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129851 182 LKAAGFPEKQIYqVPTKSNDIPGAFDAANSMLVQHPEVKhwLIVGMNDSTVLGGVRATEGQGFKAADIIGI 252
Cdd:cd06280 142 LAEAGIPVDESL-IFEGDSTIEGGYEAVKALLDLPPRPT--AIFATNNLMAVGALRALRERGLEIPQDISV 209
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
 27-113 2.93e-03

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: 38.78  E-value: 2.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIA--VPDGEKTLNAIDSLAASGAKGFVICTPDPklgSAIVA---KA 101
Cdd:cd20000   1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGptTATAEAQIPFINTLIQQGVDAIAISANDP---DALAPalkKA 77

                        90
                ....*....|..
gi 16129851 102 RGYDMKVIAVDD 113
Cdd:cd20000  78 RAAGIKVVTFDS 89
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 27-152 3.33e-03

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: 38.84  E-value: 3.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGE--KTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGY 104
Cdd:cd20002   1 TIVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVGPADADpaQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16129851 105 DMKVIAVDDQfvNAKGKPMDtvpLVMMAATKIGERQGQELYKEMQKRG 152
Cdd:cd20002  81 GIVVITHESP--GQKGADWD---VELIDNEKFGEAQMELLAKEMGGKG 123
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
 38-310 6.25e-03

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: 37.70  E-value: 6.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  38 PWFQTEWKFADKAGKDLGFEVIKI--AVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDdqf 115
Cdd:cd19969  12 PYWDDVKEGFEDAGAELGVKTEYTgpATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFD--- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 116 vnAKGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGwdvkESAVMAITAneLDTARRRTTGSMDALkaAGFPEKQIYQV 195
Cdd:cd19969  89 --SDAPESKRISYVGTDNYEAGYAAAEKLAELLGGKG----KVAVLTGPG--QPNHEERVEGFKEAF--AEYPGIEVVAV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 196 PTKSNDIPGAFDAANSMLVQHPEVKHWliVGMNDSTVLGGVRATEGQGfKAADIIgigINGVDAVSE-LSKAQATGFYGS 274
Cdd:cd19969 159 GDDNDDPEKAAQNTSALLQAHPDLVGI--FGVDASGGVGAAQAVREAG-KTGKVK---IVAFDDDPEtLDLIKDGVIDAS 232

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 16129851 275 LLPSPDVHGYKSSEMLYNWVAKDVEPPKFTEVTDVV 310
Cdd:cd19969 233 IAQRPWMMGYWSLQFLYDLANGLVKDAWQTAGVNPL 268
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 40-259 9.69e-03

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: 37.07  E-value: 9.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851  40 FQTE-WKFAD----KAGKDLGFEVIKI-AVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDd 113
Cdd:cd19993   9 FQEErWKTDEaamkKALEKAGAKYISAdAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYD- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 114 qfvnakgKPMDT--VPLVMMAATKIGERQGQELYKEmqkrgwdVKESAVMAITANELDT-ARRRTTGSMDALKAA----- 185
Cdd:cd19993  88 -------RLIENpiAFYISFDNVEVGRMQARGVLKA-------KPEGNYVFIKGSPTDPnADFLRAGQMEVLQPAidsgk 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129851 186 ----------GF-PE---KQIYQVPTKSNDipgAFDAansmlvqhpevkhwlIVGMNDSTVLGGVRATEGQGFKAadiiG 251
Cdd:cd19993 154 ikivgeqytdGWkPAnaqKNMEQILTANNN---KVDA---------------VVASNDGTAGGAVAALAAQGLAG----K 211


                ....*...
gi 16129851 252 IGINGVDA 259
Cdd:cd19993 212 VPVSGQDA 219
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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