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Conserved domains on  [gi|1532241072|gb|RRQ14868|]
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sugar ABC transporter substrate-binding protein [Corynebacterium bovis]

Protein Classification

type 1 periplasmic-binding domain-containing protein( domain architecture ID 70)

type 1 periplasmic-binding domain-containing protein such as the ligand binding domains of the LacI family of transcriptional regulators, the ABC transporter substrate-binding proteins, the family C GPCRs, membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal LIVBP-like domains of the ionotropic glutamate receptors (iGluRs); contains the Venus flytrap-like domain which undergoes transition from an open to a closed conformational state upon ligand binding

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Periplasmic_Binding_Protein_type1 super family cl10011
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
2-291 5.63e-83

Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.


The actual alignment was detected with superfamily member cd06312:

Pssm-ID: 471960 [Multi-domain]  Cd Length: 272  Bit Score: 251.38  E-value: 5.63e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGAPGDTFWDLVRKGAEDAARKDNVELRYSSDPQ--APNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVD 79
Cdd:cd06312     1 TIYVISHGSPSDPFWSVVKKGAKDAAKDLGVTVQYLGPQNndIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  80 AGVTVVGLNAGMDQY-RRYGMSGFFGQEEGVAGEQAGRRLAADGATKALCVIHEQGNSSQEARCAGLRKGLAAgagerat 158
Cdd:cd06312    81 AGIPVIAINSGDDRSkERLGALTYVGQDEYLAGQAAGERALEAGPKNALCVNHEPGNPGLEARCKGFADAFKG------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 159 ggngngggasggsrAGGTVETLYVnGQDLTAVQSTVQAKPAQDRGIDWVVGLVAPVALTAVSAARDAGSSAK--IATFDT 236
Cdd:cd06312   154 --------------AGILVELLDV-GGDPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKvkIGTFDL 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1532241072 237 NAELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLARRNGsTVGGGRPVYTGPSFV 291
Cdd:cd06312   219 SPETLEAIKDGKILFAIDQQPYLQGYLAVVFLYLYKRYG-TLPPPEPILTGPGFV 272
 
Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
2-291 5.63e-83

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


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 251.38  E-value: 5.63e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGAPGDTFWDLVRKGAEDAARKDNVELRYSSDPQ--APNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVD 79
Cdd:cd06312     1 TIYVISHGSPSDPFWSVVKKGAKDAAKDLGVTVQYLGPQNndIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  80 AGVTVVGLNAGMDQY-RRYGMSGFFGQEEGVAGEQAGRRLAADGATKALCVIHEQGNSSQEARCAGLRKGLAAgagerat 158
Cdd:cd06312    81 AGIPVIAINSGDDRSkERLGALTYVGQDEYLAGQAAGERALEAGPKNALCVNHEPGNPGLEARCKGFADAFKG------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 159 ggngngggasggsrAGGTVETLYVnGQDLTAVQSTVQAKPAQDRGIDWVVGLVAPVALTAVSAARDAGSSAK--IATFDT 236
Cdd:cd06312   154 --------------AGILVELLDV-GGDPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKvkIGTFDL 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1532241072 237 NAELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLARRNGsTVGGGRPVYTGPSFV 291
Cdd:cd06312   219 SPETLEAIKDGKILFAIDQQPYLQGYLAVVFLYLYKRYG-TLPPPEPILTGPGFV 272
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
6-296 3.74e-45

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: 155.47  E-value: 3.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   6 VSHGAPGDTFWDLVRKGAEDAARKDNVELRY-SSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTV 84
Cdd:COG1879    38 FVVKTLGNPFFVAVRKGAEAAAKELGVELIVvDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPV 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  85 VGLNAGMDQYRRygmSGFFGQEEGVAGEQAGRRLAAD--GATKALCVIHEQGNSSQEARCAGLRKGLAAGAGERAtggng 162
Cdd:COG1879   118 VTVDSDVDGSDR---VAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPAANERTDGFKEALKEYPGIKV----- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 163 ngggasggsraggtVETLYVNGQD---LTAVQSTVQAKPaqdrGIDWVVGLVAPVALTAVSAARDAGSSAKI--ATFDTN 237
Cdd:COG1879   190 --------------VAEQYADWDRekaLEVMEDLLQAHP----DIDGIFAANDGMALGAAQALKAAGRKGDVkvVGFDGS 251
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1532241072 238 AELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLArRNGSTVGGgrPVYTGPSFVDADTV 296
Cdd:COG1879   252 PEALQAIKDGTIDATVAQDPYLQGYLAVDAALKL-LKGKEVPK--EILTPPVLVTKENV 307
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
3-269 7.08e-31

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: 116.64  E-value: 7.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   3 VAMVSHGApGDTFWDLVRKGAEDAARKDNVELRYSSDPQ--APNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDA 80
Cdd:pfam13407   1 IGVVPKST-GNPFFQAAEEGAEEAAKELGGEVIVVGPAEadAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  81 GVTVVGLNAGMDQYRRYgmsGFFGQEEGVAGEQAGRRLAAD--GATKALCVIHEQGNSSQEARCAGLRKGLAAGAGErat 158
Cdd:pfam13407  80 GIPVVTFDSDAPSSPRL---AYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPG--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 159 ggngngggasggsragGTVETLYVNGQDL--TAVQSTVQAKPAQDRGIDWVVGLVAPVALTAVSAARDAGSSAK--IATF 234
Cdd:pfam13407 154 ----------------IKVVAEVEGTNWDpeKAQQQMEALLTAYPNPLDGIISPNDGMAGGAAQALEAAGLAGKvvVTGF 217
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1532241072 235 DTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDALW 269
Cdd:pfam13407 218 DATPEALEAIKDGTIDATVLQDPYGQGYAAVELAA 252
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
21-85 2.14e-05

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 45.56  E-value: 2.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1532241072  21 KGAEDAARKDNVELRYS--SDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVV 85
Cdd:PRK15408   43 NGAKEAGKELGVDVTYDgpTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVL 109
 
Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
2-291 5.63e-83

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


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 251.38  E-value: 5.63e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGAPGDTFWDLVRKGAEDAARKDNVELRYSSDPQ--APNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVD 79
Cdd:cd06312     1 TIYVISHGSPSDPFWSVVKKGAKDAAKDLGVTVQYLGPQNndIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  80 AGVTVVGLNAGMDQY-RRYGMSGFFGQEEGVAGEQAGRRLAADGATKALCVIHEQGNSSQEARCAGLRKGLAAgagerat 158
Cdd:cd06312    81 AGIPVIAINSGDDRSkERLGALTYVGQDEYLAGQAAGERALEAGPKNALCVNHEPGNPGLEARCKGFADAFKG------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 159 ggngngggasggsrAGGTVETLYVnGQDLTAVQSTVQAKPAQDRGIDWVVGLVAPVALTAVSAARDAGSSAK--IATFDT 236
Cdd:cd06312   154 --------------AGILVELLDV-GGDPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKvkIGTFDL 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1532241072 237 NAELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLARRNGsTVGGGRPVYTGPSFV 291
Cdd:cd06312   219 SPETLEAIKDGKILFAIDQQPYLQGYLAVVFLYLYKRYG-TLPPPEPILTGPGFV 272
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
6-296 3.74e-45

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: 155.47  E-value: 3.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   6 VSHGAPGDTFWDLVRKGAEDAARKDNVELRY-SSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTV 84
Cdd:COG1879    38 FVVKTLGNPFFVAVRKGAEAAAKELGVELIVvDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPV 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  85 VGLNAGMDQYRRygmSGFFGQEEGVAGEQAGRRLAAD--GATKALCVIHEQGNSSQEARCAGLRKGLAAGAGERAtggng 162
Cdd:COG1879   118 VTVDSDVDGSDR---VAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPAANERTDGFKEALKEYPGIKV----- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 163 ngggasggsraggtVETLYVNGQD---LTAVQSTVQAKPaqdrGIDWVVGLVAPVALTAVSAARDAGSSAKI--ATFDTN 237
Cdd:COG1879   190 --------------VAEQYADWDRekaLEVMEDLLQAHP----DIDGIFAANDGMALGAAQALKAAGRKGDVkvVGFDGS 251
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1532241072 238 AELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLArRNGSTVGGgrPVYTGPSFVDADTV 296
Cdd:COG1879   252 PEALQAIKDGTIDATVAQDPYLQGYLAVDAALKL-LKGKEVPK--EILTPPVLVTKENV 307
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
3-275 2.45e-39

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: 138.94  E-value: 2.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   3 VAMVSHGApGDTFWDLVRKGAEDAARKDNVELRY--SSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDA 80
Cdd:cd19965     2 FVFVTHVT-TNPFFQPVKKGMDDACELLGAECQFtgPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  81 GVTVVGLNAGMDQYRRYGMSgFFGQEEGVAGEQAGRRLA---ADGATKALCVIHEQGNSSQEARCAGLRKGLA-AGAGER 156
Cdd:cd19965    81 GIPVVAFNVDAPGGENARLA-FVGQDLYPAGYVLGKRIAekfKPGGGHVLLGISTPGQSALEQRLDGIKQALKeYGRGIT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 157 atggngngggasggsraGGTVETlyvnGQDLTAVQSTVQAKPAQDRGIDWVVGlvAPVALTAVSA--ARDAGSSAKI--A 232
Cdd:cd19965   160 -----------------YDVIDT----GTDLAEALSRIEAYYTAHPDIKAIFA--TGAFDTAGAGqaIKDLGLKGKVlvG 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1532241072 233 TFDTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLARRNG 275
Cdd:cd19965   217 GFDLVPEVLQGIKAGYIDFTIDQQPYLQGFYPVMQLFLYKKFG 259
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
2-271 9.20e-34

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: 124.22  E-value: 9.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGaPGDTFWDLVRKGAEDAARKDNVELRYSSDPQAPN-QANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDA 80
Cdd:cd01536     1 KIGVVVKD-LTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAkQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  81 GVTVVGLNAGMDQyrRYGMSGFFGQEEGVAGEQAGRRLA--ADGATKALCVIHEQGNSSQEARCAGLRKGLAAGAGERat 158
Cdd:cd01536    80 GIPVVAVDTDIDG--GGDVVAFVGTDNYEAGKLAGEYLAeaLGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYPDIE-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 159 ggngngggasggsraggTVETLYVNGQD---LTAVQSTVQAKPAqdrgIDWVVGLVAPVALTAVSAARDAGSSAKI--AT 233
Cdd:cd01536   156 -----------------IVAEQPANWDRakaLTVTENLLQANPD----IDAVFAANDDMALGAAEALKAAGRTGDIkiVG 214
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1532241072 234 FDTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLA 271
Cdd:cd01536   215 VDGTPEALKAIKDGELDATVAQDPYLQGYLAVEAAVKL 252
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
3-269 7.08e-31

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: 116.64  E-value: 7.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   3 VAMVSHGApGDTFWDLVRKGAEDAARKDNVELRYSSDPQ--APNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDA 80
Cdd:pfam13407   1 IGVVPKST-GNPFFQAAEEGAEEAAKELGGEVIVVGPAEadAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  81 GVTVVGLNAGMDQYRRYgmsGFFGQEEGVAGEQAGRRLAAD--GATKALCVIHEQGNSSQEARCAGLRKGLAAGAGErat 158
Cdd:pfam13407  80 GIPVVTFDSDAPSSPRL---AYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPG--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 159 ggngngggasggsragGTVETLYVNGQDL--TAVQSTVQAKPAQDRGIDWVVGLVAPVALTAVSAARDAGSSAK--IATF 234
Cdd:pfam13407 154 ----------------IKVVAEVEGTNWDpeKAQQQMEALLTAYPNPLDGIISPNDGMAGGAAQALEAAGLAGKvvVTGF 217
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1532241072 235 DTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDALW 269
Cdd:pfam13407 218 DATPEALEAIKDGTIDATVLQDPYGQGYAAVELAA 252
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
2-291 8.31e-25

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: 100.86  E-value: 8.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGAPGDTFWDLVRKGAEDAARKDNVELRY---SSDPQAPNQAnlVQNAVDSRVDGIAVTMPTPD-AIGPAVQRA 77
Cdd:cd19966     1 KIYFIPGGAPGDPFWTVVYNGAKDAAADLGVDLDYvfsSWDPEKMVEQ--FKEAIAAKPDGIAIMGHPGDgAYTPLIEAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  78 VDAGVTVVGLNaGMDQYRRYGMSGFF--GQEEGVAGEQAGRRLAADGATK----ALCVIHEQGNSSQEARCAGLRKGL-A 150
Cdd:cd19966    79 KKAGIIVTSFN-TDLPKLEYGDCGLGyvGADLYAAGYTLAKELVKRGGLKtgdrVFVPGLLPGQPYRVLRTKGVIDALkE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 151 AGAgeratggngngggasggsraggTVETLYVNGQDL--TAVQSTVQAKPAQDRGIDWVVGLVAPVALTAVSAARDAGSS 228
Cdd:cd19966   158 AGI----------------------KVDYLEISLEPNkpAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKK 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1532241072 229 AK---IATFDTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLARRNGstvGGGRPVYTGPSFV 291
Cdd:cd19966   216 PGeipVAGFDLSPATVQAIKSGYVNATIDQQPYLQGYLPVLQIYLTKKYG---FSGLDIDTGGGYV 278
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
2-292 8.91e-25

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: 100.35  E-value: 8.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGApGDTFWDLVRKGAEDAARK--DNVELRYSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVD 79
Cdd:cd06314     1 TFALVPKGL-NNPFWDLAEAGAEKAAKElgVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  80 AGVTVVGLNAGMDQYRRYgmsGFFGQEEGVAGEQAGRRLAADGATKALCVIHeQGNSSQE---ARCAGLRKGLAAGAGER 156
Cdd:cd06314    80 KGIPVITFDSDAPDSKRL---AYIGTDNYEAGREAGELMKKALPGGGKVAII-TGGLGADnlnERIQGFKDALKGSPGIE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 157 AtggngngggasggsraggtVETLYVNGQDLTAVQ---STVQAKPaqdrGIDWVVGLVAPVALTAVSAARDAG--SSAKI 231
Cdd:cd06314   156 I-------------------VDPLSDNDDIAKAVQnveDILKANP----DLDAIFGVGAYNGPAIAAALKDAGkvGKVKI 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1532241072 232 ATFDTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLARRNGSTVGGgrPVYTGPSFVD 292
Cdd:cd06314   213 VGFDTLPETLQGIKDGVIAATVGQRPYEMGYLSVKLLYKLLKGGKPVPD--VIDTGVDVVT 271
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
2-265 8.35e-22

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: 92.30  E-value: 8.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGApGDTFWDLVRKGAEDAARKDNVELRYSS-----DPQApnQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQR 76
Cdd:cd20004     1 CIAVIPKGT-THDFWKSVKAGAEKAAQELGVEIYWRGpsredDVEA--QIQIIEYFIDQGVDGIVLAPLDRKALVAPVER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  77 AVDAGVTVVGLNAGMDQYRRygmSGFFGQEEGVAGEQAGRRLAAD--GATKALCVIHEQGNSSQEARCAGLRKGLAAGAG 154
Cdd:cd20004    78 ARAQGIPVVIIDSDLGGDAV---ISFVATDNYAAGRLAAKRMAKLlnGKGKVALLRLAKGSASTTDRERGFLEALKKLAP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 155 ERatggngngggasggsragGTVETLYVNGQDLTAVQSTVQAKPaQDRGIDWVVGLVAPVALTAVSAARDAGSSAKIA-- 232
Cdd:cd20004   155 GL------------------KVVDDQYAGGTVGEARSSAENLLN-QYPDVDGIFTPNESTTIGALRALRRLGLAGKVKfi 215
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1532241072 233 TFDTNAELVAAIRKGDVQWAVDQQPYLQGYLAV 265
Cdd:cd20004   216 GFDASDLLLDALRAGEISALVVQDPYRMGYLGV 248
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
11-296 2.61e-20

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 88.42  E-value: 2.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  11 PGDTFWDLVRKGAEDAARKDNVELRYS---SDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGL 87
Cdd:cd20006    11 PNSDFWQTVKSGAEAAAKEYGVDLEFLgpeSEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  88 NAGMDQYRrygMSGFFGQEEGVAGEQAGRRLA--ADGATKALCVIHEQGNSSQEARCAGLRKGLAAGAGERatggngngg 165
Cdd:cd20006    91 DSPVNSKK---ADSFVATDNYEAGKKAGEKLAslLGEKGKVAIVSFVKGSSTAIEREEGFKQALAEYPNIK--------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 166 gasggsraggTVETLYVNGQDLTAVQSTVQAKpAQDRGIDWVVGLVAPVALTAVSAARDAGSSAKIA--TFDTNAELVAA 243
Cdd:cd20006   159 ----------IVETEYCDSDEEKAYEITKELL-SKYPDINGIVALNEQSTLGAARALKELGLGGKVKvvGFDSSVEEIQL 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1532241072 244 IRKGDVQWAVDQQPYLQGYLAVdalwlarRNGSTVGGGRPVytgPSFVDADTV 296
Cdd:cd20006   228 LEEGIIDALVVQNPFNMGYLSV-------QAAVDLLNGKKI---PKRIDTGSV 270
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
2-268 4.23e-19

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: 84.99  E-value: 4.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGAPGDtFWDLVRKGAEDAARKDNVELRYSSDPQAPN---QANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAV 78
Cdd:cd20005     1 YIAVISKGFQHQ-FWKAVKKGAEQAAKELGVKITFEGPDTESDvdkQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  79 DAGVTVVGLNAGMDqyrrygmSG----FFGQEEGVAGEQAGRRLAA--DGATKALCVIHEQGNSSQEARCAGLRKGLAAG 152
Cdd:cd20005    80 EKGIPVVTFDSGVP-------SDlplaTVATDNYAAGALAADHLAEliGGKGKVAIVAHDATSETGIDRRDGFKDEIKEK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 153 AGERAtggngngggasggsraggTVETLYVNGQDLTA---VQSTVQAKPaQDRGIDWVVGLVAPVALTAVSAARDAGsSA 229
Cdd:cd20005   153 YPDIK------------------VVNVQYGVGDHAKAadiAKAILQANP-DLKGIYATNEGAAIGVANALKEMGKLG-KI 212
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1532241072 230 KIATFDTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDAL 268
Cdd:cd20005   213 KVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAA 251
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
2-265 1.42e-18

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


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 83.55  E-value: 1.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGAPGDtFWDLVRKGAEDAARKDNVEL-----RYSSDPQApnQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQR 76
Cdd:cd06310     1 KIGVVLKGTTSA-FWRTVREGAEAAAKDLGVKIifvgpESEEDVAG--QNSLLEELINKKPDAIVVAPLDSEDLVDPLKD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  77 AVDAGVTVVGLNAGMDQyrrYGMSGFFGQEEGVAGEQAGRRLAA--DGATKALCVIHEQGNSSQEARCAGLRKGLAAGAG 154
Cdd:cd06310    78 AKDKGIPVIVIDSGIKG---DAYLSYIATDNYAAGRLAAQKLAEalGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 155 EratggngngggasggsragGTVETLYVNGQDLTAVQSTVQAKPAQDRGIDWVVGLVAPVALTAVSAARDAGSSAKIAT- 233
Cdd:cd06310   155 G-------------------IKVLASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIv 215
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1532241072 234 -FDTNAELVAAIRKGDVQWAVDQQPYLQGYLAV 265
Cdd:cd06310   216 gFDSQEELLDALKNGKIDALVVQNPYEIGYEGI 248
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
12-279 3.99e-18

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: 82.28  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  12 GDTFWDLVRKGAEDAARKDNVELRYssdpQAPN-------QANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAvDAGVTV 84
Cdd:cd20008    10 DSEYWQTVLKGAEKAAKELGVEVTF----LGPAteadiagQVNLVENAISRKPDAIVLAPNDTAALVPAVEAA-DAGIPV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  85 VGLNAGM--DQYrrygmSGFFGQEEGVAGEQAGRRLAA------DGATKALCVIHEQGNSSQEARCAGLRKGLAAGAGEr 156
Cdd:cd20008    85 VLVDSGAntDDY-----DAFLATDNVAAGALAADELAEllkasgGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKYPD- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 157 atggngngggasggsraGGTVETLYVNGqDLTAVQSTVQAKPAQDRGIDWVVGLVAPVALTAVSAARDAGSSAKIA--TF 234
Cdd:cd20008   159 -----------------IEIVDVQYSDG-DIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAGKIVlvGF 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1532241072 235 DTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLARRNGSTVG 279
Cdd:cd20008   221 DSSPDEVALLKSGVIKALVVQDPYQMGYEGVKTAVKALKGEEIVE 265
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
12-272 8.55e-18

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: 81.61  E-value: 8.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  12 GDTFWDLVRKGAEDAARKDNVELRYSSDPQA--PNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNA 89
Cdd:cd19969    10 GHPYWDDVKEGFEDAGAELGVKTEYTGPATAdvNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  90 GMDQYRR--YGMSGFFGqeegvAGEQAGRRLA-ADGATKALCVIHEQGNSSQEARCAGLRKGLAAGAGeratggngnggg 166
Cdd:cd19969    90 DAPESKRisYVGTDNYE-----AGYAAAEKLAeLLGGKGKVAVLTGPGQPNHEERVEGFKEAFAEYPG------------ 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 167 asggsraGGTVETLYVNGQDLTAVQST---VQAKPAqdrgidwVVGLVAPVALTAVSAA---RDAGSSA--KIATFDTNA 238
Cdd:cd19969   153 -------IEVVAVGDDNDDPEKAAQNTsalLQAHPD-------LVGIFGVDASGGVGAAqavREAGKTGkvKIVAFDDDP 218
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1532241072 239 ELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLAR 272
Cdd:cd19969   219 ETLDLIKDGVIDASIAQRPWMMGYWSLQFLYDLA 252
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
13-267 1.92e-16

TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.


Pssm-ID: 380529 [Multi-domain]  Cd Length: 269  Bit Score: 77.62  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  13 DTFWDLVRKGAEDAARKDNVELRYS---SDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNA 89
Cdd:cd06306    11 DSYWVGVNYGIVDEAKRLGVKLTVYeagGYTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  90 GMDQYrryGMSGFFGQEEGVAGEQAGRRLAADGATKALCVIH---EQGNSSQEARCAGLRKGLAAGAGEratggngnggg 166
Cdd:cd06306    91 GIDSP---KVAARVLVDFYDMGYLAGEYLVEHHPGKPVKVAWfpgPAGAGWAEDREKGFKEALAGSNVE----------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 167 asggsraggTVETLY----VNGQdLTAVQSTVQAKPAqdrgIDWVVGlVAPVALTAVSAARDAG--SSAKIATFDTNAEL 240
Cdd:cd06306   157 ---------IVATKYgdtgKAVQ-LNLVEDALQAHPD----IDYIVG-NAVAAEAAVGALREAGltGKVKVVSTYLTPGV 221
                         250       260
                  ....*....|....*....|....*..
gi 1532241072 241 VAAIRKGDVQWAVDQQPYLQGYLAVDA 267
Cdd:cd06306   222 YRGIKRGKILAAPSDQPVLQGRIAVDQ 248
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
9-266 2.93e-16

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


Pssm-ID: 380662 [Multi-domain]  Cd Length: 271  Bit Score: 76.89  E-value: 2.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   9 GAPGDTFWDLVRKGAEDAARKDNVELRYSSDPQ--APNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVG 86
Cdd:cd20007     7 GVTGDPFYITMQCGAEAAAKELGVELDVQGPPTfdPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  87 LNAGMDQyrRYGMSGFFGQEEGVAGEQAGRRLA--ADGATKALCVIHEQGNSSQEARcaglRKGLAAGAGEratggngng 164
Cdd:cd20007    87 VDTTLGD--PSFVLSQIASDNVAGGALAAEALAelIGGKGKVLVINSTPGVSTTDAR----VKGFAEEMKK--------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 165 ggasggSRAGGTVETLYVNGQDLTA---VQSTVQAKPaqdrGIDWVVGLVAPVALTAVSAARDAGSSA--KIATFDTNAE 239
Cdd:cd20007   152 ------YPGIKVLGVQYSENDPAKAasiVAAALQANP----DLAGIFGTNTFSAEGAAAALRNAGKTGkvKVVGFDASPA 221
                         250       260
                  ....*....|....*....|....*..
gi 1532241072 240 LVAAIRKGDVQWAVDQQPYLQGYLAVD 266
Cdd:cd20007   222 QVEQLKAGTIDALIAQKPAEIGYLAVE 248
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
14-276 8.41e-16

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


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 75.86  E-value: 8.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  14 TFWDLVRKGAEDAARKDNVELR-YSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVV--GLNAG 90
Cdd:cd06319    12 PFWQIMERGVQAAAEELGYEFVtYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIPVViaDIGTG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  91 MDQYRRYGMSGFFGQEEGvAGEQAGRRLAADGATK---ALCVIHEQGNSSQeARCAGLRKGL-AAGAGERATGGNGNGgg 166
Cdd:cd06319    92 GGDYVSYIISDNYDGGYQ-AGEYLAEALKENGWGGgsvGIIAIPQSRVNGQ-ARTAGFEDALeEAGVEEVALRQTPNS-- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 167 asggsraggTVETLYVNGQDLTAvqstvqakpaQDRGIDWVVGLVAPVALTAVSAARDAGSSAKI--ATFDTNAELVAAI 244
Cdd:cd06319   168 ---------TVEETYSAAQDLLA----------ANPDIKGIFAQNDQMAQGALQAIEEAGRTGDIlvVGFDGDPEALDLI 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1532241072 245 RKGDVQWAVDQQPYLQGYLAVDALwLARRNGS 276
Cdd:cd06319   229 KDGKLDGTVAQQPFGMGARAVELA-IQALNGD 259
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
2-297 3.36e-12

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: 65.73  E-value: 3.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHgAPGDTFWDLVRKGAEDAARKDNVELRYSSDPQA--PNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVD 79
Cdd:cd06302     1 KIAFVPK-VVGIPYFDAAEEGAKKAAKELGVEVVYTGPTQAdaAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  80 AGVTVVGLNAGMDQYRRygmSGFFGQ-EEGVAGEQAGRRLAADGATKALCVIHEQGNSS--QEARCAGLRKGLAAgager 156
Cdd:cd06302    80 AGIKVITWDSDAPPSAR---DYFVNQaDDEGLGEALVDSLAKEIGGKGKVAILSGSLTAtnLNAWIKAMKEYLKS----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 157 atggngngggasgGSRAGGTVETLYVNG---QDLTAVQSTVQAKPaqdrGIDWVVGLVAPVALTAVSAARDAGSSAKIAT 233
Cdd:cd06302   152 -------------KYPDIELVDTYYTDDdqqKAYTQAQNLIQAYP----DLKGIIGVSTTAPPAAAQAVEEAGKTGKVAV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 234 --FDTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDALWLARRNGS----------------TVGGGRPVYTGPSFVDADT 295
Cdd:cd06302   215 tgIGLPNTARPYLKDGSVKEGVLWDPAKLGYLTVYAAYQLLKGKGftedsddvgtggkvkvDVAGGEILLGPPLVFTKDN 294

                  ..
gi 1532241072 296 VD 297
Cdd:cd06302   295 VD 296
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
13-150 2.86e-11

periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily.


Pssm-ID: 380524 [Multi-domain]  Cd Length: 272  Bit Score: 62.63  E-value: 2.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  13 DTFWDLVRKGAEDAARK-DNVELRYSS-DPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAG 90
Cdd:cd06301    12 DEFLTYLRDAIEAYAKEyPGVKLVIVDaQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPLVYVNRE 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1532241072  91 MDQYRRYgmSGFFGQEEGVAGEQAGRRLA--ADGATKALCVIHEQGNSSQEARCAGLRKGLA 150
Cdd:cd06301    92 PDSKPKG--VAFVGSDDIESGELQMEYLAklLGGKGNIAILDGVLGHEAQILRTEGNKDVLA 151
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
14-260 4.45e-11

periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 62.02  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  14 TFWDLVRKGAEDAARKDNVELR-YSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNagmd 92
Cdd:cd19968    12 PFFVYMHEQAVDEAAKLGVKLVvLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAGIPVVTVD---- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  93 qyRRYGMSG---FFGQEEGVAGEQAGRRLAAD--GATKALCVIHEQGNSSQEARCAGLRKGLAAGAGERATGGNGNGgga 167
Cdd:cd19968    88 --RRAEGAApvpHVGADNVAGGREVAKFVVDKlpNGAKVIELTGTPGSSPAIDRTKGFHEELAAGPKIKVVFEQTGN--- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 168 sggsraggtvetlYVNGQDLTAVQSTVQAKPAQdrgIDWVVGLVAPVALTAVSAARDAG---SSAKIATFDTNAELVAAI 244
Cdd:cd19968   163 -------------FERDEGLTVMENILTSLPGP---PDAIICANDDMALGAIEAMRAAGldlKKVKVIGFDAVPDALQAI 226
                         250
                  ....*....|....*.
gi 1532241072 245 RKGDVQWAVDQQPYLQ 260
Cdd:cd19968   227 KDGELYATVEQPPGGQ 242
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
2-89 5.19e-11

ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380658  Cd Length: 298  Bit Score: 62.29  E-value: 5.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHgAPGDTFWDLVRKGAEDAARKDNVELRY--SSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVD 79
Cdd:cd20003     1 TIAMIPK-LVGVPYFTAAGQGAQEAAKELGVDVTYdgPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMK 79
                          90
                  ....*....|
gi 1532241072  80 AGVTVVGLNA 89
Cdd:cd20003    80 KGIKVVTWDS 89
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
13-268 9.59e-11

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: 61.24  E-value: 9.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  13 DTFWDLVRKGAEDAARKDNVEL---RYSSDPQApnQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNA 89
Cdd:cd06317    11 AQFFNQINQGAQAAAKDLGVDLvvfNANDDPSK--QNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  90 GMDQyrrYGMSGFFGQEEGVAGEQAGrRLAAD------GATKALCVIHEQGNSSQEARCAGLRKGLAAGAGeratggngn 163
Cdd:cd06317    89 VIPS---DFQAAQVGVDNLEGGKEIG-KYAADyikaelGGQAKIGVVGALSSLIQNQRQKGFEEALKANPG--------- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 164 gggasggSRAGGTVETLYVNGQDLTAVQSTVQAKPaqdrGIDWVVGLVAPVALTAVSAARDAGSSAKIATFDTNAELVAA 243
Cdd:cd06317   156 -------VEIVATVDGQNVQEKALSAAENLLTANP----DLDAIYATGEPALLGAVAAVRSQGRQGKIKVFGWDLTKQAI 224
                         250       260
                  ....*....|....*....|....*...
gi 1532241072 244 IRKGDVQW---AVDQQPYLQGYLAVDAL 268
Cdd:cd06317   225 FLGIDEGVlqaVVQQDPEKMGYEAVKAA 252
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
15-297 1.21e-10

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: 61.12  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  15 FWDLVRKGAEDAARKDNVELryssDPQAPN-------QANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGL 87
Cdd:cd06320    13 FWVAMKDGIEAEAKKLGVKV----DVQAAPsetdtqgQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKKGIPVINL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  88 NAGMDQYRRYGMSG----FFGQEEGVAGEQAGRRLAA--DGATKALCVIHEQGNSSQEARCAGLRKGLAAGAGeratggn 161
Cdd:cd06320    89 DDAVDADALKKAGGkvtsFIGTDNVAAGALAAEYIAEklPGGGKVAIIEGLPGNAAAEARTKGFKETFKKAPG------- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 162 gngggasggsraGGTVETL---YVNGQDLTAVQSTVQAKPAqdrgidwVVGLVAP---VALTAVSAARDAGSSAKIATF- 234
Cdd:cd06320   162 ------------LKLVASQpadWDRTKALDAATAILQAHPD-------LKGIYAAndtMALGAVEAVKAAGKTGKVLVVg 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1532241072 235 -DTNAELVAAIRKGDVQWAVDQQPYLQGYLAVD-ALWLARrngstvGGGRP--VYTGPSFVDADTVD 297
Cdd:cd06320   223 tDGIPEAKKSIKAGELTATVAQYPYLEGAMAVEaALRLLQ------GQKVPavVATPQALITKDNVD 283
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
12-297 1.53e-10

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: 60.73  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  12 GDTFWDLVRKGAEDAARKDNVELRYS--SDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNA 89
Cdd:cd20000    10 GNPYFDAARDGAKEAAKELGGELIFVgpTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAAGIKVVTFDS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  90 GMDQYRRygmSGFFGQeegVAGEQAGR---RLAAD--GATKALCVIHEQGNSS-QEARCAGLRKGLAAGAGERATGgngn 163
Cdd:cd20000    90 DVAPEAR---DLFVNQ---ADADGIGRaqvDMMAEliGGEGEFAILSATPTATnQNAWIDAMKKELASPEYAGMKL---- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 164 gggasggsraggtVETLYVNGQDLTAVQST---VQAKPAqdrgidwVVGLVAPVALTAVSAAR---DAGSSAKIAT--FD 235
Cdd:cd20000   160 -------------VKVAYGDDDAQKSYQEAealLQAYPD-------LKGIIAPTTVGIAAAARaleDSGLKGKVKVtgLG 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1532241072 236 TNAELVAAIRKGDVQWAVDQQPYLQGYLAVDALWL---------------ARRNGS-TVGGGRPVYTGPSFV-DADTVD 297
Cdd:cd20000   220 LPSEMAKYVKDGTVPAFALWNPIDLGYLAAYAAAAlaqgeitgkegetftAGRLGEyTVGEGGEVVLGPPFVfTADNID 298
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
15-268 4.31e-10

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: 59.21  E-value: 4.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  15 FWDLVRKGAEDAARKDNVELR-YSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAGMDQ 93
Cdd:cd06322    13 FFVDIKDAMKKEAAELGVKVVvADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFTVDVKADG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  94 YRrygMSGFFGQEEGVAGEQAGR---RLAADGATKALCVIHEQGNSSQEaRCAGLRKGLAAGAGERatggngngggasgg 170
Cdd:cd06322    93 AK---VVTHVGTDNYAGGKLAGEyalKALLGGGGKIAIIDYPEVESVVL-RVNGFKEAIKKYPNIE-------------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 171 sraggTVETLYVNGQDLTAVQST---VQAKPaqdrGIDWVVGLVAPVALTAVSAARDAGSSAKIAT--FDTNAELVAAIR 245
Cdd:cd06322   155 -----IVAEQPGDGRREEALAATedmLQANP----DLDGIFAIGDPAALGALTAIESAGKEDKIKVigFDGNPEAIKAIA 225
                         250       260
                  ....*....|....*....|....
gi 1532241072 246 KGDVQWA-VDQQPYLQGYLAVDAL 268
Cdd:cd06322   226 KGGKIKAdIAQQPDKIGQETVEAI 249
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
21-278 8.63e-10

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: 58.45  E-value: 8.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  21 KGAEDAARKDNVELRY---SSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAGMDqyrry 97
Cdd:cd06321    19 RGAEEAAAEINPGAKVtvvDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVVAVDVAAE----- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  98 GMSGFFGQEEGVAGEQAGRRLAAD-GATKALCVIHEQGNSSQEARCAGLRKGLAAGAGeratggngngggasggsraggt 176
Cdd:cd06321    94 GADATVTTDNVQAGYLACEYLVEQlGGKGKVAIIDGPPVSAVIDRVNGCKEALAEYPG---------------------- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 177 veTLYVNGQD--------LTAVQSTVQAKPAqdrgIDWVVGLVAPVALTAVSAARDAGSSA-KIATFDTNAELVAAIRKG 247
Cdd:cd06321   152 --IKLVDDQNgkgsraggLSVMTRMLTAHPD----VDGVFAINDPGAIGALLAAQQAGRDDiVITSVDGSPEAVAALKRE 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1532241072 248 D--VQWAVDQQPYLQGYLAVdALWLARRNGSTV 278
Cdd:cd06321   226 GspFIATAAQDPYDMARKAV-ELALKILNGQEP 257
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
14-267 5.69e-09

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: 55.76  E-value: 5.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  14 TFWDLVRKGAEDAARKDNVEL--RYSSDPQApNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAGM 91
Cdd:cd06323    12 PFFVSLKDGAQAEAKELGVELvvLDAQNDPA-KQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  92 DQYRRYgmsGFFGQEEGVAGEQAGRRLAADGATKALCVIHE--QGNSSQEARCAGLRKGLAAGAGeratggngngggasg 169
Cdd:cd06323    91 TGGKVV---SHIASDNVAGGEMAAEYIAKKLGGKGKVVELQgiPGTSAARERGKGFHNAIAKYPK--------------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 170 gsRAGGTVETLYVNGQD-LTAVQSTVQAKPAqdrgIDWVVGLVAPVALTAVSAARDAG-SSAKIATFDTNAELVAAIRKG 247
Cdd:cd06323   153 --INVVASQTADFDRTKgLNVMENLLQAHPD----IDAVFAHNDEMALGAIQALKAAGrKDVIVVGFDGTPDAVKAVKDG 226
                         250       260
                  ....*....|....*....|
gi 1532241072 248 DVQWAVDQQPYLQGYLAVDA 267
Cdd:cd06323   227 KLAATVAQQPEEMGAKAVET 246
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
20-267 6.28e-09

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


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 55.72  E-value: 6.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  20 RKGAEDAARKDNvelRYSSDPQAPN-------QANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAGMD 92
Cdd:cd19970    18 EKGARKHAKEAN---GYELLVKGIKqetdieqQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNRLD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  93 QyRRYGMSG----FFGQEEGVAGEQAGRRLAADGATKALCVIHE--QGNSSQEARCAGLRKGLAAgageratggngnggg 166
Cdd:cd19970    95 A-DALKEGGinvpFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEgiPGADNAQQRKAGFLKAFEE--------------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 167 asggsraggtvetlyvNGQDLTAVQS----TVQAKPA------QDRGIDWVVGLVAPVALTAVSAARDAGSSAK--IATF 234
Cdd:cd19970   159 ----------------AGMKIVASQSanweIDEANTVaanlltAHPDIRGILCANDNMALGAIKAVDAAGKAGKvlVVGF 222
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1532241072 235 DTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDA 267
Cdd:cd19970   223 DNIPAVRPLLKDGKMLATIDQHPAKQAVYGIEY 255
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
10-268 8.19e-09

periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.


Pssm-ID: 380530 [Multi-domain]  Cd Length: 275  Bit Score: 55.64  E-value: 8.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  10 APGDTFWDLVRKGAEDAARK---DNVELRYSS-DPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVV 85
Cdd:cd06307     8 SPENPFYELLRRAIEAAAAAlrdRRVRLRIHFvDSLDPEALAAALRRLAAGCDGVALVAPDHPLVRAAIDELAARGIPVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  86 GLNAGMDQYRRygmSGFFGQEEGVAGEQAGR---RLAADGATKALCVIHEQGNSSQEARCAGLRKGLAAGAGEratggng 162
Cdd:cd06307    88 TLVSDLPGSRR---LAYVGIDNRAAGRTAAWlmgRFLGRRPGKVLVILGSHRFRGHEEREAGFRSVLRERFPD------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 163 ngggasggsraGGTVETLYVNGQDLTAVQSTVQA-KPAQD-RGIdWVVGlvapVALTAVSAA-RDAGSSAKIA--TFDTN 237
Cdd:cd06307   158 -----------LTVLEVLEGLDDDELAYELLRELlARHPDlVGI-YNAG----GGNEGIARAlREAGRARRVVfiGHELT 221
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1532241072 238 AELVAAIRKGDVQWAVDQQPYLQGYLAVDAL 268
Cdd:cd06307   222 PETRRLLRDGTIDAVIDQDPELQARRAIEVL 252
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
21-150 2.38e-08

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: 54.20  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  21 KGAEDAARKDNVELR-YSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAGM--DQYrry 97
Cdd:cd06313    19 EAMKAVAKELNVDLVvLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAGIPLVGVNALIenEDL--- 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1532241072  98 gmSGFFGQEEGVAGEQAGRRLAADGATKALCVIHEQ--GNSSQEARCAGLRKGLA 150
Cdd:cd06313    96 --TAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGpiGQSAQIDRGKGIENVLK 148
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
22-294 3.09e-07

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: 50.87  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  22 GAEDAARKDNVELRYSsDPQA--PNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAGMDQyrRYGM 99
Cdd:cd06318    20 AAKAEAKKLGVELVVT-DAQNdlTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGIPVITVDSALDP--SANV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 100 SGFFGQEEGVAGEQAGRRLA---ADGATKALCVIHEQGNSSQEARcaglRKGLAAGAGERAtggngnggGASGGSRAGGT 176
Cdd:cd06318    97 ATQVGRDNKQNGVLVGKEAAkalGGDPGKIIELSGDKGNEVSRDR----RDGFLAGVNEYQ--------LRKYGKSNIKV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 177 VETLYVNGQD---LTAVQSTVQAKPaqdrGIDWVVGLVAPVALTAVSAARDAG--SSAKIATFDTNAELVAAIRKGDVQW 251
Cdd:cd06318   165 VAQPYGNWIRsgaVAAMEDLLQAHP----DINVVYAENDDMALGAMKALKAAGmlDKVKVAGADGQKEALKLIKDGKYVA 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1532241072 252 AVDQQPYLQGYLAVDALWLARRNGSTVggGRPVYTGPSFVDAD 294
Cdd:cd06318   241 TGLNDPDLLGKTAVDTAAKVVKGEESF--PEFTYTPTALITKD 281
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
15-281 2.75e-06

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380628 [Multi-domain]  Cd Length: 285  Bit Score: 47.85  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  15 FWDLVRKGAEDAARKDNVELRYS---SDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAGM 91
Cdd:cd19973    13 FFVKMKEGAQKAAKALGIKLMTAagkIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVLVIALDTPT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  92 DQYRryGMSGFFGQEEGVAGEQAGRRLAADGATKALCVIHEQGNSSQEA---RCAGLRKGLAAGAGERATGGNGNGGGAS 168
Cdd:cd19973    93 DPID--AADATFATDNFKAGVLIGEWAKAALGAKDAKIATLDLTPGHTVgvlRHQGFLKGFGIDEKDPESNEDEDDSQVV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 169 GGSRAGGTVETlyvnGQdlTAVQSTVQAKPaqdrGIDWVVGLVAPVALTAVSAARDAG--SSAKIATFDTNAELVAAIRK 246
Cdd:cd19973   171 GSADTNGDQAK----GQ--TAMENLLQKDP----DINLVYTINEPAAAGAYQALKAAGkeKGVLIVSVDGGCPGVKDVKD 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1532241072 247 GDVQWAVDQQPYLQGYLAVDALWLARRNGSTVGGG 281
Cdd:cd19973   241 GIIGATSQQYPLRMAALGVEAIAAFAKTGGTKGSG 275
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
2-90 4.02e-06

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380651 [Multi-domain]  Cd Length: 302  Bit Score: 47.62  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMvSHGAPGDTFWDLVRKGAEDAA---RKDNVELRY-SSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRA 77
Cdd:cd19996     1 TIGF-SNAGLGNSWRVQMIAEFEAEAaklKKLIKELIYtDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKA 79
                          90
                  ....*....|...
gi 1532241072  78 VDAGVTVVGLNAG 90
Cdd:cd19996    80 AAAGIPVVLFDSG 92
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
13-267 4.90e-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: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  13 DTFWDLVRKGAEDAARKDNVELrYSSDPQA-PN-QANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAG 90
Cdd:cd19971    11 NPFFIAINDGIKKAVEANGDEL-ITRDPQLdQNkQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  91 M------------DQYRrygmsgffgqeegvAGEQAGRRLAADGATKA-LCVIHEQGNSSQEARCAGLRKGLAAGAGera 157
Cdd:cd19971    90 VkdtdlvdstiasDNYN--------------AGKLCGEDMVKKLPEGAkIAVLDHPTAESCVDRIDGFLDAIKKNPK--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 158 tggngngggasggsraGGTVETLYVNGQ---DLTAVQSTVQAKPAqdrgIDWVVGLVAPVALTAVSAARDAGSSAKIATF 234
Cdd:cd19971   153 ----------------FEVVAQQDGKGQlevAMPIMEDILQAHPD----LDAVFALNDPSALGALAALKAAGKLGDILVY 212
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1532241072 235 --DTNAELVAAIRKGDVQWAVDQQPYLQGYLAVDA 267
Cdd:cd19971   213 gvDGSPDAKAAIKDGKMTATAAQSPIEIGKKAVET 247
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
18-85 1.45e-05

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380653 [Multi-domain]  Cd Length: 302  Bit Score: 45.74  E-value: 1.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1532241072  18 LVRKGAEDAARKDNVELR-YSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVV 85
Cdd:cd19998    20 IAKAAAKQPPYADKVELKvVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVV 88
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
42-151 1.57e-05

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380652 [Multi-domain]  Cd Length: 305  Bit Score: 45.74  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  42 APNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAGMDQYRRYGMSGFFGQEEGVAGEQAGRRLaaD 121
Cdd:cd19997    46 ATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGVTEPCAYILNNDFEDYGAASVEYVADRL--G 123
                          90       100       110
                  ....*....|....*....|....*....|
gi 1532241072 122 GATKALCVIHEQGNSSQEARCAGLRKGLAA 151
Cdd:cd19997   124 GKGNVLEVRGVAGTSPDEEIYAGQVEALKK 153
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
21-85 2.14e-05

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 45.56  E-value: 2.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1532241072  21 KGAEDAARKDNVELRYS--SDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVV 85
Cdd:PRK15408   43 NGAKEAGKELGVDVTYDgpTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVL 109
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
21-268 5.72e-05

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: 43.75  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  21 KGAEDAARKDNVELRYS---SDPQapNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNAGMDQYRRY 97
Cdd:cd06309    19 KSIKEAAKKRGYELVYTdanQDQE--KQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVDRTIDGEDGS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  98 GMSGFFGQEEGVAGEQAGRRLAADGATKALCVIHEQGN---SSQEARCAGLRKGLAAGAGERATggngngggasggsrag 174
Cdd:cd06309    97 LYVTFIGSDFVEEGRRAAEWLVKNYKGGKGNVVELQGTagsSVAIDRSKGFREVIKKHPNIKIV---------------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 175 GTVETLYVNGQDLTAVQSTVQAKPaqdRGIDWVVGLVAPVALTAVSAARDAGSSA----KIATFDTNAELVAAIRKGDVQ 250
Cdd:cd06309   161 ASQSGNFTREKGQKVMENLLQAGP---GDIDVIYAHNDDMALGAIQALKEAGLKPgkdvLVVGIDGQKDALEAIKAGELN 237
                         250
                  ....*....|....*...
gi 1532241072 251 WAVDQQPYlQGYLAVDAL 268
Cdd:cd06309   238 ATVECNPL-FGPTAFDTI 254
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
15-267 5.73e-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: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 43.97  E-value: 5.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  15 FWDLVRKGAEDAARKDNVELRYSSDPQAP-NQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLnagmDQ 93
Cdd:cd19972    13 FFNQIKQSVEAEAKKKGYKVITVDAKGDSaTQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAV----DR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  94 YRRYGMSGFFGQEEGVAGEQAGRRLAAD--GATKALCVIHEQ-GNSSQEARCAGLRKGLAAGAGERATGGNgngggasgg 170
Cdd:cd19972    89 NPEDAPGDTFIATDSVAAAKELGEWVIKqtGGKGEIAILHGQlGTTPEVDRTKGFQEALAEAPGIKVVAEQ--------- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 171 sraggTVETLYVNGQDLTavQSTVQAKPaqdrGIDWVVGLVAPVALTAVSAARDAGSSAKI--ATFDTNAELVAAIRKGD 248
Cdd:cd19972   160 -----TADWDQDEGFKVA--QDMLQANP----NITVFFGQSDAMALGAAQAVKVAGLDHKIwvVGFDGDVAGLKAVKDGV 228
                         250
                  ....*....|....*....
gi 1532241072 249 VQWAVDQQPYLQGYLAVDA 267
Cdd:cd19972   229 LDATMTQQTQKMGRLAVDS 247
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
2-95 6.99e-05

similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380528 [Multi-domain]  Cd Length: 273  Bit Score: 43.44  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGapGDTFWDL-VRKGAEDAARKDNVELR-YSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVD 79
Cdd:cd06305     1 TIAVVRNG--TSGDWDQqALQGAVAEAEKLGGTVIvFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALD 78
                          90
                  ....*....|....*.
gi 1532241072  80 AGVTVVGLNAGMDQYR 95
Cdd:cd06305    79 AGIPVVTFDTDSQVPG 94
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
6-150 7.11e-05

periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.


Pssm-ID: 380531 [Multi-domain]  Cd Length: 268  Bit Score: 43.69  E-value: 7.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   6 VSHGAPGDTFWDLVRKGAEDAARK-DNVELRYSS-DPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVT 83
Cdd:cd06308     4 FSQCSLNDPWRAAMNEEIKAEAAKyPNVELIVTDaQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIP 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1532241072  84 VVGLNAGM--DQYrrygmSGFFGQEEGVAGEQAGRRLAA--DGATKALCVIHEQGNSSQEARCAGLRKGLA 150
Cdd:cd06308    84 VIVLDRKVsgDDY-----TAFIGADNVEIGRQAGEYIAEllNGKGNVVEIQGLPGSSPAIDRHKGFLEAIA 149
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
49-151 8.84e-05

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


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 43.29  E-value: 8.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  49 VQNAVDSRVDGIAVTMPTPDAigPAVQRAVDAGVTVVGLNagmdqyrRYGmsgffgQEEGV---------AGEQAGRRLA 119
Cdd:cd06278    47 LRQLLQYRVDGVIVTSATLSS--ELAEECARRGIPVVLFN-------RVV------EDPGVdsvscdnraGGRLAADLLL 111
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1532241072 120 ADGATKALCVIHEQGNSSQEARCAGLRKGLAA 151
Cdd:cd06278   112 AAGHRRIAFLGGPEGTSTSRERERGFRAALAE 143
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
36-94 3.16e-04

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380654 [Multi-domain]  Cd Length: 313  Bit Score: 41.91  E-value: 3.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1532241072  36 YSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVG----------LNAGMDQY 94
Cdd:cd19999    40 QNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSfdqpvsspdaINVVIDQY 108
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
2-86 7.06e-04

ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380656  Cd Length: 296  Bit Score: 40.72  E-value: 7.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072   2 TVAMVSHGApGDTFWDLVRKGAEDAArKD---NVELRYSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAV 78
Cdd:cd20001     1 TIAVVVKVT-GIAWFDRMETGVEQFA-KDtgvNVYQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKAR 78

                  ....*...
gi 1532241072  79 DAGVTVVG 86
Cdd:cd20001    79 DAGIVVIT 86
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
21-85 1.70e-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: 39.61  E-value: 1.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1532241072  21 KGAEDAARKDNVELRY--SSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVV 85
Cdd:cd20002    19 QGVKKAGKEFGVNAYQvgPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVI 85
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
32-85 1.75e-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: 39.54  E-value: 1.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1532241072  32 VELRYSsDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVV 85
Cdd:cd19994    32 VDLQYA-DDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVI 84
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
15-296 2.17e-03

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 39.09  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  15 FWDLVRKGAEDAARKDNVELRY---SSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNA-- 89
Cdd:PRK09701   38 FWVDMKKGIEDEAKTLGVSVDIfasPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEki 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  90 GMDQYRRYG--MSGFFGQEEGVAGEQAGR----RLAADGATKALcVIHEQGNSSQEARCAGLRKGLAAGAGERATGGNGN 163
Cdd:PRK09701  118 DMDNLKKAGgnVEAFVTTDNVAVGAKGASfiidKLGAEGGEVAI-IEGKAGNASGEARRNGATEAFKKASQIKLVASQPA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 164 GGGASGGSRAGGTVETLYVNGQDLTAVQSTvqakpaqdrgidwvvglvapVALTAVSAARDAGSSAKIATF--DTNAELV 241
Cdd:PRK09701  197 DWDRIKALDVATNVLQRNPNIKAIYCANDT--------------------MAMGVAQAVANAGKTGKVLVVgtDGIPEAR 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1532241072 242 AAIRKGDVQWAVDQQPYLQGYLAVDALWLARRNGSTVgggrPVYTGPSFVDADTV 296
Cdd:PRK09701  257 KMVEAGQMTATVAQNPADIGATGLKLMVDAEKSGKVI----PLDKAPEFKLVDSI 307
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
11-266 7.24e-03

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: 37.30  E-value: 7.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  11 PGDTFWDLVRKGAEDAARKDNVELR-YSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVVGLNA 89
Cdd:cd19967     9 PNNPFFVVEAEGAKEKAKELGYEVTvFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLIDR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  90 GMDQyrrygmsgffgqeEGVAGEQ------AGRRLAA---------DGATKAL--------CVIHEQGNSSQEARCAGLR 146
Cdd:cd19967    89 EINA-------------EGVAVAQivsdnyQGAVLLAqyfvklmgeKGLYVELlgkesdtnAQLRSQGFHSVIDQYPELK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072 147 KGLAAGAGERATGGngngggasggsraggtvetlyvngqdLTAVQSTVQAKPAqdrgIDWVVGLVAPVALTAVSAARDAG 226
Cdd:cd19967   156 MVAQQSADWDRTEA--------------------------FEKMESILQANPD----IKGVICGNDEMALGAIAALKAAG 205
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1532241072 227 SSAKIAT--FDTNAELVAAIRKGDVQWAVDQQPYLQGYLAVD 266
Cdd:cd19967   206 RAGDVIIvgFDGSNDVRDAIKEGKISATVLQPAKLIARLAVE 247
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
19-154 8.00e-03

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


Pssm-ID: 380534 [Multi-domain]  Cd Length: 270  Bit Score: 37.34  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532241072  19 VRKGAEDAARK-DNVELRYSSDPQAPNQANLVQNAVDSRVDGIAVTMPTPDAIGPAVQRAVDAGVTVV----GLNAGMDQ 93
Cdd:cd06311    17 VAYYAEKQAKElADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVnfdrGLNVLIYD 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1532241072  94 YRRYGMSGFFGQEegvAGEQAGRRLAADGATKALCVIheQGNSSQEARCAGLRKGLAAGAG 154
Cdd:cd06311    97 LYVAGDNPGMGVV---SAEYIGKKLGGKGNVVVLEVP--SSGSVNEERVAGFKEVIKGNPG 152
 
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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