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Conserved domains on  [gi|383106048|gb|AFG36381|]
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ABC-type xylose transport system, periplasmic component [Spirochaeta africana DSM 8902]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
45-347 1.28e-130

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


:

Pssm-ID: 380646 [Multi-domain]  Cd Length: 284  Bit Score: 375.81  E-value: 1.28e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:cd19991    1 KIGFSMDSLRVERWQRDRDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 125 IPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVEAgqeaaaaqkadvagqnaaarDTPIQLLVINGAVSDYNSYMINR 204
Cdd:cd19991   81 VPVLAYDRLILNADVDLYVSFDNEKVGELQAEALVKA--------------------KPKGNYVLLGGSPTDNNAKLFRE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 205 GIVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGFARFD-HIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDG 283
Cdd:cd19991  141 GQMKVLQPLIDSGDIKVVGDQWVDDWDPEEALKIMENALTANNnKIDAVIASNDGTAGGAIQALAEQGLAGKVAVSGQDA 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383106048 284 DLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGELIFNGSVEVPFIKLNPVTV 347
Cdd:cd19991  221 DLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKNEANRTINNGKKEVPSILLDPIAV 284
 
Name Accession Description Interval E-value
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
45-347 1.28e-130

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


Pssm-ID: 380646 [Multi-domain]  Cd Length: 284  Bit Score: 375.81  E-value: 1.28e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:cd19991    1 KIGFSMDSLRVERWQRDRDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 125 IPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVEAgqeaaaaqkadvagqnaaarDTPIQLLVINGAVSDYNSYMINR 204
Cdd:cd19991   81 VPVLAYDRLILNADVDLYVSFDNEKVGELQAEALVKA--------------------KPKGNYVLLGGSPTDNNAKLFRE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 205 GIVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGFARFD-HIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDG 283
Cdd:cd19991  141 GQMKVLQPLIDSGDIKVVGDQWVDDWDPEEALKIMENALTANNnKIDAVIASNDGTAGGAIQALAEQGLAGKVAVSGQDA 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383106048 284 DLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGELIFNGSVEVPFIKLNPVTV 347
Cdd:cd19991  221 DLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKNEANRTINNGKKEVPSILLDPIAV 284
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
42-367 3.84e-99

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 296.66  E-value: 3.84e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  42 SDVRIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIR 121
Cdd:COG4213    1 GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 122 NRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVeagqeaaaaqkadvagqNAAARDTPIQLLVINGAVSDYNSYM 201
Cdd:COG4213   81 AAGIPVIAYDRLILNSDVDYYVSFDNVKVGELQGQYLV-----------------DGLPLKGKGNIELFGGSPTDNNATL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 202 INRGIVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGFARFD-HIDGVVAANDLIADAVVHAAAVRGLAGRLQVSG 280
Cdd:COG4213  144 FFEGAMSVLQPYIDSGKLVVVSGQWTLGWDPETAQKRMENLLTANGnKVDAVLAPNDGLAGGIIQALKAQGLAGKVVVTG 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 281 MDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGELIFNGSVEVPFIKLNPVTVTRDTIMETVIADG 360
Cdd:COG4213  224 QDAELAAVQRILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPEVNGTYDNGKKDVPSYLLEPVAVTKDNVKETLIDSG 303

                 ....*..
gi 383106048 361 FHRWEDV 367
Cdd:COG4213  304 YYTAEQV 310
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
34-367 3.59e-80

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 248.89  E-value: 3.59e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  34 GQRGLAdrSDVRIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEAL 113
Cdd:PRK10355  18 SVAAHA--KEVKIGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQVL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 114 SDTIEQIRNRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVEAGQEAaaaqkadvagqnaaardtpiQLLVINGA 193
Cdd:PRK10355  96 SNVIKEAKQEGIKVLAYDRMINNADIDFYISFDNEKVGELQAKALVDKVPQG--------------------NYFLMGGS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 194 VSDYNSYMINRGIVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGF-ARFDHIDGVVAANDLIADAVVHAAAVRGL 272
Cdd:PRK10355 156 PVDNNAKLFRAGQMKVLKPYIDSGKIKVVGDQWVDGWLPENALKIMENALtANNNKIDAVVASNDATAGGAIQALSAQGL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 273 AGRLQVSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGELIFNGSVEVPFIKLNPVTVTRDTI 352
Cdd:PRK10355 236 SGKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKANTTLNNGLKDVPSRLLTPIDVNKNNI 315
                        330
                 ....*....|....*
gi 383106048 353 METVIADGFHRWEDV 367
Cdd:PRK10355 316 DSTVIKDGFHKKSEL 330
xylF TIGR02634
D-xylose ABC transporter, substrate-binding protein; Members of this family are periplasmic ...
46-367 5.10e-76

D-xylose ABC transporter, substrate-binding protein; Members of this family are periplasmic (when in Gram-negative bacteria) binding proteins for D-xylose import by a high-affinity ATP-binding cassette (ABC) transporter. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 188237  Cd Length: 302  Bit Score: 237.44  E-value: 5.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048   46 IGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGI 125
Cdd:TIGR02634   1 IGMSIDDLRLERWQKDRDIFVAKAESLGAKVFVQSANGNEAKQISQIENLINRGVDVLVIIPYNGEVLSNAVQEAKDEGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  126 PVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVeagqeaaaaqkadvagqnAAARDTpiQLLVINGAVSDYNSYMINRG 205
Cdd:TIGR02634  81 KVLAYDRLINDADIDFYLSFDNEKVGEMQAKAVL------------------AAAPKG--NYFLMGGSPTDNNAKLLRGG 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  206 IVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGFARFDH-IDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDGD 284
Cdd:TIGR02634 141 QMKVLQPAIDSGDIKIVGDQWVDGWLPENALKIMENALTANDNkIDAVVASNDATAGGAIQALSAQGLSGKVPISGQDAD 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  285 LAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGELIFNGSVEVPFIKLNPVTVTRDTImETVIADGFHRW 364
Cdd:TIGR02634 221 LAAIKRVADGTQTMTVYKPITLLANKAAEIAVELGNGEKPGADTTLNNGLKKVPARLLTPIPVTKDNI-KTVVKDGFHTK 299

                  ...
gi 383106048  365 EDV 367
Cdd:TIGR02634 300 ETL 302
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
46-323 4.34e-37

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: 134.74  E-value: 4.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048   46 IGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANEN-VEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEAdAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  125 IPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVveagqeaaaaqkadvagqnAAARDTPIQLLVINGAVSDYNSYMINR 204
Cdd:pfam13407  81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELL-------------------AEALGGKGKVAILSGSPGDPNANERID 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  205 GIVTALRPyiERGQVRLLDNLWLQAWRNEEAREAIEDGFARFDH-IDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDG 283
Cdd:pfam13407 142 GFKKVLKE--KYPGIKVVAEVEGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDA 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 383106048  284 DLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRE 323
Cdd:pfam13407 220 TPEALEAIKDGTIDATVLQDPYGQGYAAVELAAALLKGKK 259
ChvE NF040907
sugar ABC transporter substrate-binding protein;
46-362 2.50e-35

sugar ABC transporter substrate-binding protein;


Pssm-ID: 468842  Cd Length: 319  Bit Score: 131.90  E-value: 2.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  46 IGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGI 125
Cdd:NF040907   1 VGIAMPTKSSERWIADGNNMVKQLEAAGYKTDLQYAEDDVPTQVSQIENMITKGAKVLVIAAIDGTALTDVLQQAADAGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 126 PVLAYDRLVRNTP-IDGYISFDNQGIGATMAEMVVeagqeaaaaqkadvAGQNAAARDTPIQLLVINGAVSDYNSYMINR 204
Cdd:NF040907  81 PVIAYDRLIRGSEnVDYYATFDNFKVGVLQGTYIV--------------DGLGLKDGKGPFNIELFAGSPDDNNAYFFFD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 205 GIVTALRPYIERGQVRL------LDNLWLQAWRNEEAREAIED---GFARFDHIDGVVAANDLIadavvhaaaVRGLAGR 275
Cdd:NF040907 147 GAMSVLQPYIDSGKLVVrsgqtdFDQVATLRWDGATAQARMDNllsAFYTDKKVDAVLSPYDGI---------SIGIISA 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 276 LQ-------------VSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATG--ELIFNGSVEVPFI 340
Cdd:NF040907 218 LKgvgygsgdkplpvVTGQDAEVASVKSIIAGEQTSTIFKDTRELAKVTVKMVDAVLKGEEPEVNdtKTYDNGVKVVPSY 297
                        330       340
                 ....*....|....*....|..
gi 383106048 341 KLNPVTVTRDTIMETVIADGFH 362
Cdd:NF040907 298 LLEPVSVDKDNYKEVLVDSGYY 319
 
Name Accession Description Interval E-value
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
45-347 1.28e-130

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


Pssm-ID: 380646 [Multi-domain]  Cd Length: 284  Bit Score: 375.81  E-value: 1.28e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:cd19991    1 KIGFSMDSLRVERWQRDRDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 125 IPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVEAgqeaaaaqkadvagqnaaarDTPIQLLVINGAVSDYNSYMINR 204
Cdd:cd19991   81 VPVLAYDRLILNADVDLYVSFDNEKVGELQAEALVKA--------------------KPKGNYVLLGGSPTDNNAKLFRE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 205 GIVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGFARFD-HIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDG 283
Cdd:cd19991  141 GQMKVLQPLIDSGDIKVVGDQWVDDWDPEEALKIMENALTANNnKIDAVIASNDGTAGGAIQALAEQGLAGKVAVSGQDA 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383106048 284 DLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGELIFNGSVEVPFIKLNPVTV 347
Cdd:cd19991  221 DLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKNEANRTINNGKKEVPSILLDPIAV 284
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
42-367 3.84e-99

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 296.66  E-value: 3.84e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  42 SDVRIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIR 121
Cdd:COG4213    1 GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 122 NRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVeagqeaaaaqkadvagqNAAARDTPIQLLVINGAVSDYNSYM 201
Cdd:COG4213   81 AAGIPVIAYDRLILNSDVDYYVSFDNVKVGELQGQYLV-----------------DGLPLKGKGNIELFGGSPTDNNATL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 202 INRGIVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGFARFD-HIDGVVAANDLIADAVVHAAAVRGLAGRLQVSG 280
Cdd:COG4213  144 FFEGAMSVLQPYIDSGKLVVVSGQWTLGWDPETAQKRMENLLTANGnKVDAVLAPNDGLAGGIIQALKAQGLAGKVVVTG 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 281 MDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGELIFNGSVEVPFIKLNPVTVTRDTIMETVIADG 360
Cdd:COG4213  224 QDAELAAVQRILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPEVNGTYDNGKKDVPSYLLEPVAVTKDNVKETLIDSG 303

                 ....*..
gi 383106048 361 FHRWEDV 367
Cdd:COG4213  304 YYTAEQV 310
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
34-367 3.59e-80

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 248.89  E-value: 3.59e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  34 GQRGLAdrSDVRIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEAL 113
Cdd:PRK10355  18 SVAAHA--KEVKIGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQVL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 114 SDTIEQIRNRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVEAGQEAaaaqkadvagqnaaardtpiQLLVINGA 193
Cdd:PRK10355  96 SNVIKEAKQEGIKVLAYDRMINNADIDFYISFDNEKVGELQAKALVDKVPQG--------------------NYFLMGGS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 194 VSDYNSYMINRGIVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGF-ARFDHIDGVVAANDLIADAVVHAAAVRGL 272
Cdd:PRK10355 156 PVDNNAKLFRAGQMKVLKPYIDSGKIKVVGDQWVDGWLPENALKIMENALtANNNKIDAVVASNDATAGGAIQALSAQGL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 273 AGRLQVSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGELIFNGSVEVPFIKLNPVTVTRDTI 352
Cdd:PRK10355 236 SGKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKANTTLNNGLKDVPSRLLTPIDVNKNNI 315
                        330
                 ....*....|....*
gi 383106048 353 METVIADGFHRWEDV 367
Cdd:PRK10355 316 DSTVIKDGFHKKSEL 330
xylF TIGR02634
D-xylose ABC transporter, substrate-binding protein; Members of this family are periplasmic ...
46-367 5.10e-76

D-xylose ABC transporter, substrate-binding protein; Members of this family are periplasmic (when in Gram-negative bacteria) binding proteins for D-xylose import by a high-affinity ATP-binding cassette (ABC) transporter. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 188237  Cd Length: 302  Bit Score: 237.44  E-value: 5.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048   46 IGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGI 125
Cdd:TIGR02634   1 IGMSIDDLRLERWQKDRDIFVAKAESLGAKVFVQSANGNEAKQISQIENLINRGVDVLVIIPYNGEVLSNAVQEAKDEGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  126 PVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVeagqeaaaaqkadvagqnAAARDTpiQLLVINGAVSDYNSYMINRG 205
Cdd:TIGR02634  81 KVLAYDRLINDADIDFYLSFDNEKVGEMQAKAVL------------------AAAPKG--NYFLMGGSPTDNNAKLLRGG 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  206 IVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGFARFDH-IDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDGD 284
Cdd:TIGR02634 141 QMKVLQPAIDSGDIKIVGDQWVDGWLPENALKIMENALTANDNkIDAVVASNDATAGGAIQALSAQGLSGKVPISGQDAD 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  285 LAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGELIFNGSVEVPFIKLNPVTVTRDTImETVIADGFHRW 364
Cdd:TIGR02634 221 LAAIKRVADGTQTMTVYKPITLLANKAAEIAVELGNGEKPGADTTLNNGLKKVPARLLTPIPVTKDNI-KTVVKDGFHTK 299

                  ...
gi 383106048  365 EDV 367
Cdd:TIGR02634 300 ETL 302
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
45-345 2.11e-70

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


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 222.07  E-value: 2.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:cd19992    1 KIGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 125 IPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVEAGQEAaaaqkadvagqNAAardtpiqllVINGAVSDYNSYMINR 204
Cdd:cd19992   81 VPVISYDRLILNADVDLYVGRDNYKVGQLQAEYALEAVPKG-----------NYV---------ILSGDPGDNNAQLITA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 205 GIVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGFARF-DHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDG 283
Cdd:cd19992  141 GAMDVLQPAIDSGDIKIVLDQYVKGWSPDEAMKLVENALTANnNNIDAVLAPNDGMAGGAIQALKAQGLAGKVFVTGQDA 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383106048 284 DLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGREL-ATGELIFNGSVEVPFIKLNPV 345
Cdd:cd19992  221 ELAALKRIVEGTQTMTVWKDLKELARAAADAAVKLAKGEKPqTTDETINNGGKDVPAILIPGV 283
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
46-345 3.63e-63

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


Pssm-ID: 380480 [Multi-domain]  Cd Length: 283  Bit Score: 203.81  E-value: 3.63e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  46 IGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGI 125
Cdd:cd01538    2 IGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 126 PVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVEAGQeaaaaqkadvagqnaaardtPIQLLVINGAVSDYNSYMINRG 205
Cdd:cd01538   82 KVIAYDRLILNADVDYYISFDNEKVGELQAQALLDAKP--------------------EGNYVLIGGSPTDNNAKLFRDG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 206 IVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGFARFDH-IDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDGD 284
Cdd:cd01538  142 QMKVLQPAIDSGKIKVVGDQWVDDWLPANAQQIMENALTANGNnVDAVVASNDGTAGGAIAALKAQGLSGGVPVSGQDAD 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383106048 285 LAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGELIFNGSVEVPFIKLNPV 345
Cdd:cd01538  222 LAAIKRILAGTQTMTVYKDIRLLADAAAEVAVALMRGEKPPINGTTNNGLKDVPSYLLEPV 282
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
45-347 5.97e-57

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: 188.22  E-value: 5.97e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:cd19994    1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 125 IPVLAYDRLVRNTP-IDGYISFDNQGIGATMAEMVVeagqeaaaaqkadvAGQNAAARDTPIQLLVINGAVSDYNSYMIN 203
Cdd:cd19994   81 IPVIAYDRLIMNTDaVDYYVTFDNEKVGELQGQYLV--------------DKLGLKDGKGPFNIELFAGSPDDNNAQLFF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 204 RGIVTALRPYIERGQ--VRLLDNLWLQA----WRNEEAREAIE---DGFARFD-HIDGVVAANDLIADAVVHAAAVRGLA 273
Cdd:cd19994  147 KGAMEVLQPYIDDGTlvVRSGQTTFEQVatpdWDTETAQARMEtllSAYYTGGkKLDAVLSPNDGIARGVIEALKAAGYD 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383106048 274 GRLQ--VSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGR--ELATGELIFNGSVEVPFIKLNPVTV 347
Cdd:cd19994  227 TGPWpvVTGQDAEDASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEevEVNDTKTYDNGVKVVPSYLLDPVIV 304
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
46-345 1.11e-49

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


Pssm-ID: 380650 [Multi-domain]  Cd Length: 294  Bit Score: 169.01  E-value: 1.11e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  46 IGFSMDSFVVERW-QRDRDAFLKAAG--SHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRN 122
Cdd:cd19995    2 VAFLLPDTTSARWeQQDAPGFEKAMKklCPDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 123 RGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVEagqeaaaaqkadvagQNAAARDTPIQLLVINGAVSDYNSYMI 202
Cdd:cd19995   82 AGVPVIAYDRLILGGPADYYVSFDNVAVGEAQAQSLVD---------------HLKAIGKKGVNIVMINGSPTDNNAGLF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 203 NRGIVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGFARF-DHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGM 281
Cdd:cd19995  147 KKGAHEVLDPLGDSGELKLVCEYDTPDWDPANAQTAMEQALTKLgNNIDGVLSANDGLAGGAIAALKAQGLAGKVPVTGQ 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383106048 282 DGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHG----RELATGElIFNGSVEVPFIKLNPV 345
Cdd:cd19995  227 DATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGetppSDLVTGT-VTNGGDKVPAVLLPPV 293
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
46-345 4.64e-49

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


Pssm-ID: 380648 [Multi-domain]  Cd Length: 287  Bit Score: 167.27  E-value: 4.64e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  46 IGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGI 125
Cdd:cd19993    2 VGVSWSNFQEERWKTDEAAMKKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 126 PVLAYDRLVRNtPIDGYISFDNQGIGATMAEMVVEAGQEAaaaqkadvagqnaaardtpiQLLVINGAVSDYNSYMINRG 205
Cdd:cd19993   82 PVIAYDRLIEN-PIAFYISFDNVEVGRMQARGVLKAKPEG--------------------NYVFIKGSPTDPNADFLRAG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 206 IVTALRPYIERGQVRLLDNLWLQAWRNEEAREAIEDGF-ARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDGD 284
Cdd:cd19993  141 QMEVLQPAIDSGKIKIVGEQYTDGWKPANAQKNMEQILtANNNKVDAVVASNDGTAGGAVAALAAQGLAGKVPVSGQDAD 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383106048 285 LAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELAT---GELIFNGS--VEVPFIKLNPV 345
Cdd:cd19993  221 KAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKGTKIEAikgAALTNDGPkkVAVPSIFLKPI 286
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
46-323 4.34e-37

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: 134.74  E-value: 4.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048   46 IGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANEN-VEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEAdAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  125 IPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVveagqeaaaaqkadvagqnAAARDTPIQLLVINGAVSDYNSYMINR 204
Cdd:pfam13407  81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELL-------------------AEALGGKGKVAILSGSPGDPNANERID 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  205 GIVTALRPyiERGQVRLLDNLWLQAWRNEEAREAIEDGFARFDH-IDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDG 283
Cdd:pfam13407 142 GFKKVLKE--KYPGIKVVAEVEGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDA 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 383106048  284 DLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRE 323
Cdd:pfam13407 220 TPEALEAIKDGTIDATVLQDPYGQGYAAVELAAALLKGKK 259
ChvE NF040907
sugar ABC transporter substrate-binding protein;
46-362 2.50e-35

sugar ABC transporter substrate-binding protein;


Pssm-ID: 468842  Cd Length: 319  Bit Score: 131.90  E-value: 2.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  46 IGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGI 125
Cdd:NF040907   1 VGIAMPTKSSERWIADGNNMVKQLEAAGYKTDLQYAEDDVPTQVSQIENMITKGAKVLVIAAIDGTALTDVLQQAADAGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 126 PVLAYDRLVRNTP-IDGYISFDNQGIGATMAEMVVeagqeaaaaqkadvAGQNAAARDTPIQLLVINGAVSDYNSYMINR 204
Cdd:NF040907  81 PVIAYDRLIRGSEnVDYYATFDNFKVGVLQGTYIV--------------DGLGLKDGKGPFNIELFAGSPDDNNAYFFFD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 205 GIVTALRPYIERGQVRL------LDNLWLQAWRNEEAREAIED---GFARFDHIDGVVAANDLIadavvhaaaVRGLAGR 275
Cdd:NF040907 147 GAMSVLQPYIDSGKLVVrsgqtdFDQVATLRWDGATAQARMDNllsAFYTDKKVDAVLSPYDGI---------SIGIISA 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 276 LQ-------------VSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATG--ELIFNGSVEVPFI 340
Cdd:NF040907 218 LKgvgygsgdkplpvVTGQDAEVASVKSIIAGEQTSTIFKDTRELAKVTVKMVDAVLKGEEPEVNdtKTYDNGVKVVPSY 297
                        330       340
                 ....*....|....*....|..
gi 383106048 341 KLNPVTVTRDTIMETVIADGFH 362
Cdd:NF040907 298 LLEPVSVDKDNYKEVLVDSGYY 319
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
23-352 2.66e-35

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 131.20  E-value: 2.66e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  23 IAGCSQhrdDEGQRGLADRSDVRIGFSM----DSFvverWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQS 98
Cdd:COG1879   16 LAACGS---AAAEAAAAAAKGKTIGFVVktlgNPF----FVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  99 GIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVveagqeaaaaqkadvagqnA 178
Cdd:COG1879   89 GVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYL-------------------A 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 179 AARDTPIQLLVINGAVSDYNSYMINRGIVTALRPYierGQVRLLDNLWLQaWRNEEAREAIEDGFARFDHIDGVVAANDL 258
Cdd:COG1879  150 KALGGKGKVAILTGSPGAPAANERTDGFKEALKEY---PGIKVVAEQYAD-WDREKALEVMEDLLQAHPDIDGIFAANDG 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 259 IADAVVHAAAVRGLAGRLQVSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELAtgelifngsvevP 338
Cdd:COG1879  226 MALGAAQALKAAGRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVP------------K 293
                        330
                 ....*....|....
gi 383106048 339 FIKLNPVTVTRDTI 352
Cdd:COG1879  294 EILTPPVLVTKENV 307
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
45-324 1.71e-31

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


Pssm-ID: 380478 [Multi-domain]  Cd Length: 268  Bit Score: 119.98  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:cd01536    1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 125 IPVLAYDRLV-RNTPIDGYISFDNQGIGATMAEMVveagqeaaaaqkadvagqnAAARDTPIQLLVINGAVSdyNSYMIN 203
Cdd:cd01536   81 IPVVAVDTDIdGGGDVVAFVGTDNYEAGKLAGEYL-------------------AEALGGKGKVAILEGPPG--SSTAID 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 204 R--GIVTALRPYierGQVRLLDNLWlQAWRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGM 281
Cdd:cd01536  140 RtkGFKEALKKY---PDIEIVAEQP-ANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGDIKIVGV 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 383106048 282 DGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGREL 324
Cdd:cd01536  216 DGTPEALKAIKDGELDATVAQDPYLQGYLAVEAAVKLLNGEKV 258
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
45-323 1.89e-26

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: 106.48  E-value: 1.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSH-GAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNR 123
Cdd:cd06308    1 VIGFSQCSLNDPWRAAMNEEIKAEAAKYpNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 124 GIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVveagqeaaaaqkadvagqnAAARDTPIQLLVINGAVSDYNSYMIN 203
Cdd:cd06308   81 GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYI-------------------AELLNGKGNVVEIQGLPGSSPAIDRH 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 204 RGIVTALRPYIERGQVRLLDNLWLQAwrneEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDG 283
Cdd:cd06308  142 KGFLEAIAKYPGIKIVASQDGDWLRD----KAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKEIKIIGVDG 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 383106048 284 DLAAVQR-VAEGTQLMTIYKPVEelAAQALDTAVQLAHGRE 323
Cdd:cd06308  218 LPEAGEKaVKDGILAATFLYPTG--GKEAIEAALKILNGEK 256
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
81-330 6.72e-18

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: 82.70  E-value: 6.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  81 ANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVE 160
Cdd:cd06313   37 GNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAGIPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVAD 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 161 AGQEAAaaqkadvagqnaaardtpiQLLVINGAVSdyNSYMINR--GIVTALRPYIErgqVRLLDNLWLQaWRNEEAREA 238
Cdd:cd06313  117 RLGGKG-------------------NVVILEGPIG--QSAQIDRgkGIENVLKKYPD---IKVLAEQTAN-WSRDEAMSL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 239 IEDGFARF-DHIDGVVAANDLIADAVVHAAAVRGLAGrLQVSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQ 317
Cdd:cd06313  172 MENWLQAYgDEIDGIIAQNDDMALGALQAVKAAGRDD-IPVVGIDGIEDALQAVKSGELIATVLQDAEAQGKGAVEVAVD 250
                        250
                 ....*....|...
gi 383106048 318 LAHGRELATGELI 330
Cdd:cd06313  251 AVKGEGVEKKYYI 263
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
46-323 2.00e-16

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: 78.61  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  46 IGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGI 125
Cdd:cd06318    2 IGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 126 PVLAYDR-LVRNTPIDGYISFDNQGIGATMAEMVVEagqeaaaaqkadvagqnaAARDTPIQLLVINGA----VSDYNSY 200
Cdd:cd06318   82 PVITVDSaLDPSANVATQVGRDNKQNGVLVGKEAAK------------------ALGGDPGKIIELSGDkgneVSRDRRD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 201 MINRGIVTALRPYIERGQVRLLDNLWLQaWRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSG 280
Cdd:cd06318  144 GFLAGVNEYQLRKYGKSNIKVVAQPYGN-WIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVKVAG 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 383106048 281 MDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRE 323
Cdd:cd06318  223 ADGQKEALKLIKDGKYVATGLNDPDLLGKTAVDTAAKVVKGEE 265
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
47-300 6.87e-14

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


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 71.87  E-value: 6.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  47 GFSMDSFvverWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQS--GIDVLVVVPNDSEAlSDTIEQIRNRG 124
Cdd:cd06324    8 GKEDEPF----WQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARppKPDYLILVNEKGVA-PELLELAEQAK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 125 IPVLAY-------DRLVRNTPIDGY------ISFDNQGIGATMAEMVVEAGqeaaaaqkadvagqNAAARDTPIQLLVIN 191
Cdd:cd06324   83 IPVFLInndltdeERALLGKPREKFkywlgsIVPDNEQAGYLLAKALIKAA--------------RKKSDDGKIRVLAIS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 192 GAVSDYNSYMINRGIVTALRpyiERGQVRLLDNLWLQaWRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRG 271
Cdd:cd06324  149 GDKSTPASILREQGLRDALA---EHPDVTLLQIVYAN-WSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAG 224
                        250       260       270
                 ....*....|....*....|....*....|.
gi 383106048 272 L-AGR-LQVSGMDGDLAAVQRVAEGTQLMTI 300
Cdd:cd06324  225 LkPGKdVLVGGIDWSPEALQAVKDGELTASV 255
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
62-321 3.35e-13

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: 68.86  E-value: 3.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  62 RDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDG 141
Cdd:cd06323   18 KDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSVTGGKVVS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 142 YISFDNQGIGATMAEMVVEAGQEAAAAqkadvagqnaaardtpIQLLVINGAvsdynSYMINR--GIVTALRPYierGQV 219
Cdd:cd06323   98 HIASDNVAGGEMAAEYIAKKLGGKGKV----------------VELQGIPGT-----SAARERgkGFHNAIAKY---PKI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 220 RLLDNlwlQA--WRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGrLQVSGMDGDLAAVQRVAEGTQL 297
Cdd:cd06323  154 NVVAS---QTadFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKD-VIVVGFDGTPDAVKAVKDGKLA 229
                        250       260
                 ....*....|....*....|....
gi 383106048 298 MTIYKPVEELAAQALDTAVQLAHG 321
Cdd:cd06323  230 ATVAQQPEEMGAKAVETADKYLKG 253
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
67-331 5.11e-13

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 69.46  E-value: 5.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  67 KAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEalSDTIEQIRNRGIPVLAYDRLVRNTPIDgYISFD 146
Cdd:COG1609   85 EAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLD--DARLERLAEAGIPVVLIDRPLPDPGVP-SVGVD 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 147 NQGIGATMAEMVVeagqeaaaaqkadvagqnaAARDTPIqlLVINGAVSDYNSYMINRGIVTALRpyiERGQVRLLDNLW 226
Cdd:COG1609  162 NRAGARLATEHLI-------------------ELGHRRI--AFIGGPADSSSARERLAGYREALA---EAGLPPDPELVV 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 227 LQAWRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLA--GRLQVSGMDG-DLAAVQRVAegtqLMTIYKP 303
Cdd:COG1609  218 EGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRvpEDVSVVGFDDiPLARYLTPP----LTTVRQP 293
                        250       260
                 ....*....|....*....|....*...
gi 383106048 304 VEELAAQALDTAVQLAHGRELATGELIF 331
Cdd:COG1609  294 IEEMGRRAAELLLDRIEGPDAPPERVLL 321
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
63-325 5.24e-13

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: 68.78  E-value: 5.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  63 DAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGY 142
Cdd:cd06309   19 KSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVDRTIDGEDGSLY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 143 ISF---DNQGIGATMAEMVVeagqeaaaaqkadvagqNAAARDtPIQLLVINGAVSDynSYMINR--GIVTALRPY---- 213
Cdd:cd06309   99 VTFigsDFVEEGRRAAEWLV-----------------KNYKGG-KGNVVELQGTAGS--SVAIDRskGFREVIKKHpnik 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 214 IERGQVrlldnlwlQAWRNEEAREAIEDGFARFDH-IDGVVAANDLIADAVVHAAAVRGL--AGRLQVSGMDGDLAAVQR 290
Cdd:cd06309  159 IVASQS--------GNFTREKGQKVMENLLQAGPGdIDVIYAHNDDMALGAIQALKEAGLkpGKDVLVVGIDGQKDALEA 230
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 383106048 291 VAEGTQLMTI-YKPveELAAQALDTAVQLAHGRELA 325
Cdd:cd06309  231 IKAGELNATVeCNP--LFGPTAFDTIAKLLAGEKVP 264
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
45-159 6.14e-13

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: 68.81  E-value: 6.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSmDSFVVERWQRD-RDAFLKAAGSHGAQV---LLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQI 120
Cdd:cd19996    1 TIGFS-NAGLGNSWRVQmIAEFEAEAAKLKKLIkelIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKA 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 383106048 121 RNRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVV 159
Cdd:cd19996   80 AAAGIPVVLFDSGVGSDKYTAFVGVDDAAFGRVGAEWLV 118
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
45-328 1.24e-12

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: 67.39  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:cd06319    1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 125 IPVLAYDRLVRNTPIDGYISFDN----QGIGATMAEMVveagqeaaaaqkadvagqnAAARDTPIQLLVINGAVSDYNSY 200
Cdd:cd06319   81 IPVVIADIGTGGGDYVSYIISDNydggYQAGEYLAEAL-------------------KENGWGGGSVGIIAIPQSRVNGQ 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 201 MINRGIVTALRPY-IERGQVRLLDNLwlqawRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVS 279
Cdd:cd06319  142 ARTAGFEDALEEAgVEEVALRQTPNS-----TVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGDILVV 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 383106048 280 GMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGE 328
Cdd:cd06319  217 GFDGDPEALDLIKDGKLDGTVAQQPFGMGARAVELAIQALNGDNTVEKE 265
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
45-324 2.53e-12

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


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 66.60  E-value: 2.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTA--NENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRN 122
Cdd:cd06310    1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPesEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 123 RGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVveagqeaaaaqkadvagqnAAARDTPIQLLVINGAVSDYNSYMI 202
Cdd:cd06310   81 KGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKL-------------------AEALGGKGKVAVLSLTAGNSTTDQR 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 203 NRGIVTALRP-----YIERGQVRLLDNLwlqawrneEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQ 277
Cdd:cd06310  142 EEGFKEYLKKhpggiKVLASQYAGSDYA--------KAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIK 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 383106048 278 VSGMDGDLAAVQRVAEGT-QLMTIYKPvEELAAQALDTAVQLAHGREL 324
Cdd:cd06310  214 IVGFDSQEELLDALKNGKiDALVVQNP-YEIGYEGIKLALKLLKGEEV 260
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
62-324 1.46e-11

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


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 64.38  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  62 RDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDG 141
Cdd:cd19972   18 KQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNPEDAPGDT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 142 YISFDNQGIGATMAEMVVeagqeaaaaqkaDVAGQNAaardtpiQLLVINGAVSDYNSYMINRGIVTALRpyiERGQVRL 221
Cdd:cd19972   98 FIATDSVAAAKELGEWVI------------KQTGGKG-------EIAILHGQLGTTPEVDRTKGFQEALA---EAPGIKV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 222 LDNLWLQaWRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDGDLAAVQRVAEGTQLMTIY 301
Cdd:cd19972  156 VAEQTAD-WDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDHKIWVVGFDGDVAGLKAVKDGVLDATMT 234
                        250       260
                 ....*....|....*....|...
gi 383106048 302 KPVEELAAQALDTAVQLAHGREL 324
Cdd:cd19972  235 QQTQKMGRLAVDSAIDLLNGKAV 257
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
83-330 4.98e-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: 380534 [Multi-domain]  Cd Length: 270  Bit Score: 62.77  E-value: 4.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  83 ENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVveag 162
Cdd:cd06311   39 SNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYDLYVAGDNPGMGVVSAEYI---- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 163 qeaaaaqkadvaGQNAAARDTPIQLLVIN-GAVSDYNSyminRGIVTALR--PYIErgqvrlldNLWLQA--WRNEEARE 237
Cdd:cd06311  115 ------------GKKLGGKGNVVVLEVPSsGSVNEERV----AGFKEVIKgnPGIK--------ILAMQAgdWTREDGLK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 238 AIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDGDLAAVQRVAEG---TQLMTIYKPveELAAQALDT 314
Cdd:cd06311  171 VAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIKVMTGGGGSQEYFKRIMDGdpiWPASATYSP--AMIADAIKL 248
                        250
                 ....*....|....*.
gi 383106048 315 AVQLAHGRELATGELI 330
Cdd:cd06311  249 AVLILKGGKTVEKEVI 264
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
58-156 1.91e-10

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


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 61.09  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  58 WQRDRDAFLKAAGSHGAQVLLR-TANEN-VEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVR 135
Cdd:cd20004   14 WKSVKAGAEKAAQELGVEIYWRgPSREDdVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDSDLG 93
                         90       100
                 ....*....|....*....|.
gi 383106048 136 NTPIDGYISFDNQGIGATMAE 156
Cdd:cd20004   94 GDAVISFVATDNYAAGRLAAK 114
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
83-325 4.23e-10

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: 59.90  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  83 ENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVeag 162
Cdd:cd06306   41 TNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNGIDSPKVAARVLVDFYDMGYLAGEYLV--- 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 163 qeaaaaqkadvagqnAAARDTPIQLLVINGAVsdynsymiNRGIVTA----LRPYIERGQVRLLDNLWLQAWRNEeAREA 238
Cdd:cd06306  118 ---------------EHHPGKPVKVAWFPGPA--------GAGWAEDrekgFKEALAGSNVEIVATKYGDTGKAV-QLNL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 239 IEDGFARFDHIDgVVAANDLIADAVVHAAAVRGLAGRLQVSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQL 318
Cdd:cd06306  174 VEDALQAHPDID-YIVGNAVAAEAAVGALREAGLTGKVKVVSTYLTPGVYRGIKRGKILAAPSDQPVLQGRIAVDQAVRA 252

                 ....*..
gi 383106048 319 AHGRELA 325
Cdd:cd06306  253 LEGKPVP 259
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
85-324 1.15e-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: 58.80  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  85 VEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYD-RL--------VRNTPidgYISFDNQGiGATMA 155
Cdd:cd19970   44 IEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDnRLdadalkegGINVP---FVGPDNRQ-GAYLA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 156 EMVVeagqeaaaaqkadvagqnAAARDTPIQLLVINGAVSDYNSYMINRGIVTAlrpyIERGQVRLLDnlwLQA--WRNE 233
Cdd:cd19970  120 GDYL------------------AKKLGKGGKVAIIEGIPGADNAQQRKAGFLKA----FEEAGMKIVA---SQSanWEID 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 234 EAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALD 313
Cdd:cd19970  175 EANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGKVLVVGFDNIPAVRPLLKDGKMLATIDQHPAKQAVYGIE 254
                        250
                 ....*....|.
gi 383106048 314 TAVQLAHGREL 324
Cdd:cd19970  255 YALKMLNGEEV 265
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
67-331 3.36e-09

ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.


Pssm-ID: 380491 [Multi-domain]  Cd Length: 264  Bit Score: 57.14  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  67 KAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEAlsDTIEQIRNRGIPVLAYDRLVRNTPIDgYISFD 146
Cdd:cd06267   23 DAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDD--ELLEELLAAGIPVVLIDRRLDGLGVD-SVVVD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 147 NQGIGATMAEMVveagqeaaaaqkadvagqnaaardtpIQL-----LVINGAVSDYNSYMINRGIVTALRpyiERGqVRL 221
Cdd:cd06267  100 NYAGAYLATEHL--------------------------IELghrriAFIGGPLDLSTSRERLEGYRDALA---EAG-LPV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 222 LDNLWLQA-WRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLA--GRLQVSGMDG-DLAAVQRVAegtqL 297
Cdd:cd06267  150 DPELVVEGdFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRvpEDISVVGFDDiPLAALLTPP----L 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 383106048 298 MTIYKPVEELAAQALDTAVQLAHGRELATGELIF 331
Cdd:cd06267  226 TTVRQPAYEMGRAAAELLLERIEGEEEPPRRIVL 259
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
62-341 3.81e-09

periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 57.21  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  62 RDAFLKAAGSHG-AQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPID 140
Cdd:cd01539   19 RKALEKAAKAGGkIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVIFFNREPSREDLK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 141 GY-----ISFDNQGIGATMAEMVVEAGQEaaaaqkadvagqNAAA---RDTPIQLLVINGAVSDYNSYMINRGIVTALRp 212
Cdd:cd01539   99 SYdkayyVGTDAEESGIMQGEIIADYWKA------------NPEIdknGDGKIQYVMLKGEPGHQDAIARTKYSVKTLN- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 213 yiERG-QVRLLDNLwLQAWRNEEAREAIEDGFARF-DHIDGVVAAND-----LIADAVVHAAAVRGLAGRLQVSGMDGDL 285
Cdd:cd01539  166 --DAGiKTEQLAED-TANWDRAQAKDKMDAWLSKYgDKIELVIANNDdmalgAIEALKAAGYNTGDGDKYIPVFGVDATP 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 383106048 286 AAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRELATGE---LIFNGSVEVPFIK 341
Cdd:cd01539  243 EALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLETGykfLVEGKYVRIPYKK 301
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
58-322 3.90e-09

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 56.84  E-value: 3.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  58 WQRDRDAFLKAAGSHGAQVLLRTAN--ENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVR 135
Cdd:cd20006   16 WQTVKSGAEAAAKEYGVDLEFLGPEseEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSPVN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 136 NTPIDGYISFDNQGIGATMAEMVveagqeaaaaqkadvagqnAAARDTPIQLLVINgavSDYNS-YMINR--GIVTALRP 212
Cdd:cd20006   96 SKKADSFVATDNYEAGKKAGEKL-------------------ASLLGEKGKVAIVS---FVKGSsTAIEReeGFKQALAE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 213 Y--IERGQVRLLDNLwlqawrNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDGDLAAVQR 290
Cdd:cd20006  154 YpnIKIVETEYCDSD------EEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLGGKVKVVGFDSSVEEIQL 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 383106048 291 VAEGT-QLMTIYKP--VEELAAQAldtAVQLAHGR 322
Cdd:cd20006  228 LEEGIiDALVVQNPfnMGYLSVQA---AVDLLNGK 259
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
63-156 5.42e-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: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 56.44  E-value: 5.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  63 DAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTP-IDG 141
Cdd:cd19971   19 DGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPVKDTDlVDS 98
                         90
                 ....*....|....*
gi 383106048 142 YISFDNQGIGATMAE 156
Cdd:cd19971   99 TIASDNYNAGKLCGE 113
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
63-159 7.27e-09

ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380522 [Multi-domain]  Cd Length: 268  Bit Score: 56.13  E-value: 7.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  63 DAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPndSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGY 142
Cdd:cd06299   19 SGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVP--TGENSEGLQALIAQGLPVVFVDREVEGLGGVPV 96
                         90
                 ....*....|....*..
gi 383106048 143 ISFDNQGIGATMAEMVV 159
Cdd:cd06299   97 VTSDNRPGAREAVEYLV 113
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
46-324 3.13e-08

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: 54.20  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  46 IGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGI 125
Cdd:cd06322    2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 126 PVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVeagqeaaaaQKADVAGQNAAARDTP---IQLLVING---AVSDYNs 199
Cdd:cd06322   82 PVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYAL---------KALLGGGGKIAIIDYPeveSVVLRVNGfkeAIKKYP- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 200 ymiNRGIVTALRPYIergqvrlldnlwlqawRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVS 279
Cdd:cd06322  152 ---NIEIVAEQPGDG----------------RREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDKIKVI 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 383106048 280 GMDGDLAAVQRVAEGTQL--MTIYKPvEELAAQALDTAVQLAHGREL 324
Cdd:cd06322  213 GFDGNPEAIKAIAKGGKIkaDIAQQP-DKIGQETVEAIVKYLAGETV 258
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
68-159 4.27e-08

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


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 53.92  E-value: 4.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  68 AAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGYISFDN 147
Cdd:cd06317   24 AAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAVIPSDFQAAQVGVDN 103
                         90
                 ....*....|..
gi 383106048 148 QGIGATMAEMVV 159
Cdd:cd06317  104 LEGGKEIGKYAA 115
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
45-159 8.65e-08

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


Pssm-ID: 380523 [Multi-domain]  Cd Length: 302  Bit Score: 53.10  E-value: 8.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSmDSFVVERWQRDRDAFLKA-AGSHGAQVLL-----RTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIE 118
Cdd:cd06300    1 TIGLS-NTYAGNSWREQMIASLKAdAAQSGQKGLVkelivANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIE 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 383106048 119 QIRNRGIPVLAYDRLVrNTPIDGYISFDNQGIGATMAEMVV 159
Cdd:cd06300   80 QAADAGIPVVAFDGAV-TSPDAYNVSNDQVEWGRLGAKWLF 119
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
45-316 9.26e-08

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: 52.77  E-value: 9.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:cd19968    1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 125 IPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMVVeagqeaaaaqkadvagQNAAARDTPIQLLVINGAvsdynSYMINR 204
Cdd:cd19968   81 IPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVV----------------DKLPNGAKVIELTGTPGS-----SPAIDR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 205 --GIVTALRPYierGQVRLLDNLWLQAWRnEEAREAIEDGFARF-DHIDGVVAANDLIADAVVHAAAVRGL-AGRLQVSG 280
Cdd:cd19968  140 tkGFHEELAAG---PKIKVVFEQTGNFER-DEGLTVMENILTSLpGPPDAIICANDDMALGAIEAMRAAGLdLKKVKVIG 215
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 383106048 281 MDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAV 316
Cdd:cd19968  216 FDAVPDALQAIKDGELYATVEQPPGGQARTALRILV 251
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
46-323 1.86e-07

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: 51.85  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  46 IGFSMDSFVVERWQRDRDAFLKAAGSH-GAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRG 124
Cdd:cd06301    3 IGVSMQNFSDEFLTYLRDAIEAYAKEYpGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 125 IPVLAYDR-LVRNTPIDGYISFDNQGIGATMAEMVVEAGqeaaaaqkadvagqNAAARdtpiqLLVINGAVSdyNSYMIN 203
Cdd:cd06301   83 IPLVYVNRePDSKPKGVAFVGSDDIESGELQMEYLAKLL--------------GGKGN-----IAILDGVLG--HEAQIL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 204 R--GIVTALRPY----IERGQVrlldnlwlQAWRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQ 277
Cdd:cd06301  142 RteGNKDVLAKYpgmkIVAEQT--------ANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDDIL 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 383106048 278 VSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRE 323
Cdd:cd06301  214 VAGIDATPDALKAMKAGRLDATVFQDAAGQGETAVDVAVKAAKGEE 259
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
58-159 2.04e-07

periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).


Pssm-ID: 380537 [Multi-domain]  Cd Length: 271  Bit Score: 51.81  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  58 WQRDRDAFLKAAGSHGAQVLLR-TANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRN 136
Cdd:cd06314   14 WDLAEAGAEKAAKELGVNVEFVgPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFDSDAPD 93
                         90       100
                 ....*....|....*....|...
gi 383106048 137 TPIDGYISFDNQGIGATMAEMVV 159
Cdd:cd06314   94 SKRLAYIGTDNYEAGREAGELMK 116
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
67-341 2.10e-07

ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 51.75  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  67 KAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNdsealSDTIEQIRNRGIPVLAYDR-LVRNTPidgYISF 145
Cdd:cd06291   23 KELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSH-----SLDIEEYKKLNIPIVSIDRyLSEGIP---SVSS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 146 DNQGIGATMAEMVVeagqeaaaaqkadvagqNAAARDtpiqLLVINGAVSDYNSYMINRGIVTALRpyiERG-QVRLLDN 224
Cdd:cd06291   95 DNYQGGRLAAEHLI-----------------EKGCKK----ILHIGGPSNNSPANERYRGFEDALK---EAGiEYEIIEI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 225 LWlQAWRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLA--GRLQVSGMDGdlaavQRVAEGT--QLMTI 300
Cdd:cd06291  151 DE-NDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRvpEDVQIIGFDG-----IEISELLypELTTI 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 383106048 301 YKPVEELAAQALDTAVQLAHGRELATGELIFngsvEVPFIK 341
Cdd:cd06291  225 RQPIEEMAKEAVELLLKLIEGEEIEESRIVL----PVELIE 261
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
45-159 3.49e-07

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: 51.52  E-value: 3.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMdSFVVERWQRDR-DAFLKAAGSHGAQVLLR-----TANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIE 118
Cdd:cd19997    1 VIALSN-SYAGNTWRQQMvDAFEEAAKKAKADGLIAdyivvNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQ 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 383106048 119 QIRNRGIPVLAYDRLVrNTPIDGYISFDNQGIGATMAEMVV 159
Cdd:cd19997   80 QACDAGIKVVVFDSGV-TEPCAYILNNDFEDYGAASVEYVA 119
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
73-325 3.74e-07

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


Pssm-ID: 380544 [Multi-domain]  Cd Length: 270  Bit Score: 51.14  E-value: 3.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  73 GAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRntPIDGYISFDNQGIGA 152
Cdd:cd06321   31 GAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVVAVDVAAE--GADATVTTDNVQAGY 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 153 TMAEMVVEAGQEAAaaqkadvagqnaaardtpiQLLVINGAvsdYNSYMINR--GIVTALRPYierGQVRLLDNlwlQAW 230
Cdd:cd06321  109 LACEYLVEQLGGKG-------------------KVAIIDGP---PVSAVIDRvnGCKEALAEY---PGIKLVDD---QNG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 231 RNEE--AREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGrLQVSGMDGDLAAVQRVA-EGTQLM-TIYKPVEE 306
Cdd:cd06321  161 KGSRagGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDD-IVITSVDGSPEAVAALKrEGSPFIaTAAQDPYD 239
                        250
                 ....*....|....*....
gi 383106048 307 LAAQALDTAVQLAHGRELA 325
Cdd:cd06321  240 MARKAVELALKILNGQEPA 258
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
45-324 4.32e-07

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: 50.72  E-value: 4.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTAN--ENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRN 122
Cdd:cd06320    1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAAPseTDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 123 RGIPVLAYDRLV-------RNTPIDGYISFDNQGIGATMAEMVveagqeaaaaqkadvagqnAAARDTPIQLLVINGAVS 195
Cdd:cd06320   81 KGIPVINLDDAVdadalkkAGGKVTSFIGTDNVAAGALAAEYI-------------------AEKLPGGGKVAIIEGLPG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 196 DYNSymINR--GIVTALR--PYIERGQVRLLDnlwlqaWRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRG 271
Cdd:cd06320  142 NAAA--EARtkGFKETFKkaPGLKLVASQPAD------WDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAG 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 383106048 272 LAGRLQVSGMDGDLAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGREL 324
Cdd:cd06320  214 KTGKVLVVGTDGIPEAKKSIKAGELTATVAQYPYLEGAMAVEAALRLLQGQKV 266
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
67-159 1.35e-06

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: 49.55  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  67 KAAGSHGAQVLLR-TANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGYIS- 144
Cdd:cd06302   23 KAAKELGVEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSDAPPSARDYFVNq 102
                         90
                 ....*....|....*
gi 383106048 145 FDNQGIGATMAEMVV 159
Cdd:cd06302  103 ADDEGLGEALVDSLA 117
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
68-156 1.58e-06

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


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 49.15  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  68 AAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPndSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDgYISFDN 147
Cdd:cd06285   24 AARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITP--ARDDAPDLQELAARGVPVVLVDRRIGDTALP-SVTVDN 100

                 ....*....
gi 383106048 148 QGIGATMAE 156
Cdd:cd06285  101 ELGGRLATR 109
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
68-156 3.35e-06

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


Pssm-ID: 380512 [Multi-domain]  Cd Length: 268  Bit Score: 47.95  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  68 AAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVP-NDSEAlsDTIEQIRNRGIPVLAYDRLVRNTPIDgYISFD 146
Cdd:cd06289   24 ALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPaAGTTA--ELLRRLKAWGIPVVLALRDVPGSDLD-YVGID 100
                         90
                 ....*....|
gi 383106048 147 NQGIGATMAE 156
Cdd:cd06289  101 NRLGAQLATE 110
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
45-159 4.08e-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: 380653 [Multi-domain]  Cd Length: 302  Bit Score: 48.05  E-value: 4.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMdSFVVERWQRDRDAFLKAAGSH---GAQVLLRTAN--ENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQ 119
Cdd:cd19998    1 KIALSN-SYSGNDWRQEMINIAKAAAKQppyADKVELKVVSsgTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 383106048 120 IRNRGIPVLAYDRLVRNTpiDGY-ISFDNQGIGATMAEMVV 159
Cdd:cd19998   80 ACDAGIVVVAFDNVVDEP--CAYnVNTDQAKAGEQTAQWLV 118
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
73-318 1.19e-05

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: 46.55  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  73 GAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPI-DGYISFDNQGIG 151
Cdd:cd19967   29 GYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLIDREINAEGVaVAQIVSDNYQGA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 152 ATMAEMVVeagqeaaaaqkadvagQNAAARDTPIQLLvinGAVSDYNSYMINRGI--VTALRPYIERgQVRLLDNlwlqa 229
Cdd:cd19967  109 VLLAQYFV----------------KLMGEKGLYVELL---GKESDTNAQLRSQGFhsVIDQYPELKM-VAQQSAD----- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 230 WRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVSGMDGDLAAVQRVAEGTQLMTIYKPVEELAA 309
Cdd:cd19967  164 WDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRAGDVIIVGFDGSNDVRDAIKEGKISATVLQPAKLIAR 243

                 ....*....
gi 383106048 310 QALDTAVQL 318
Cdd:cd19967  244 LAVEQADQY 252
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
67-331 1.34e-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: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 46.11  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  67 KAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEalSDTIEQIRNRGIPVLAYDRLVRNTPIDgYISFD 146
Cdd:cd06293   23 DAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDD--LSHLARLRARGTAVVLLDRPAPGPAGC-SVSVD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 147 N-QGIGATMAEMVveagqeaaaaqkadVAGQNAaardtpiqLLVINGAVSDYNSYMINRGIVTALR-----PYIERGQVR 220
Cdd:cd06293  100 DvQGGALAVDHLL--------------ELGHRR--------IAFVSGPLRTRQVAERLAGARAAVAeagldPDEVVRELS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 221 LLDNLwlqawrNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLA--GRLQVSGMDG-DLAAVQRVAegtqL 297
Cdd:cd06293  158 APDAN------AELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRvpDDVSVVGYDDlPFAAAANPP----L 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 383106048 298 MTIYKPVEELAAQALDTAVQLAHGRELATGELIF 331
Cdd:cd06293  228 TTVRQPSYELGRAAADLLLDEIEGPGHPHEHVVF 261
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
62-158 1.70e-05

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: 46.10  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  62 RDAFLKAAGSHGAQVLLRTANEN-VEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPID 140
Cdd:cd20000   18 RDGAKEAAKELGGELIFVGPTTAtAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAAGIKVVTFDSDVAPEARD 97
                         90
                 ....*....|....*....
gi 383106048 141 GYI-SFDNQGIGATMAEMV 158
Cdd:cd20000   98 LFVnQADADGIGRAQVDMM 116
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
84-158 1.91e-05

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: 45.69  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  84 NVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDrlvrnTPID------GYISFDNQGIGA----T 153
Cdd:cd20007   41 DPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVD-----TTLGdpsfvlSQIASDNVAGGAlaaeA 115

                 ....*
gi 383106048 154 MAEMV 158
Cdd:cd20007  116 LAELI 120
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
45-339 4.32e-05

Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.


Pssm-ID: 380479 [Multi-domain]  Cd Length: 265  Bit Score: 44.54  E-value: 4.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVV-VPNDSEALsdTIEQIRNR 123
Cdd:cd01537    1 RIGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAInLVDPAAAG--VAEKARGQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 124 GIPVLAYDRL-VRNTPIDgYISFDNQGIGATMAEMVVeagqeaaaaqkadVAGQnaaardtpIQLLVINGAVSDYNSymi 202
Cdd:cd01537   79 NVPVVFFDKEpSRYDKAY-YVITDSKEGGIIQGDLLA-------------KHGH--------IQIVLLKGPLGHPDA--- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 203 nRGIVTALRPYIERGQVRlLDNLWLQA--WRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVS- 279
Cdd:cd01537  134 -EARLAGVIKELNDKGIK-TEQLQLDTgdWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISv 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 383106048 280 -GMDgdlAAVQRVAEGTQLMTIYKPVEELAAQALDTAVQLAHGRElatgelIFNGSVEVPF 339
Cdd:cd01537  212 fGYD---ALPEALKSGPLLTTILQDANNLGKTTFDLLLNLADNWK------IDNKVVRVPY 263
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
63-159 4.37e-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: 44.59  E-value: 4.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  63 DAFLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDgY 142
Cdd:cd06305   19 QGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAGIPVVTFDTDSQVPGVN-N 97
                         90
                 ....*....|....*..
gi 383106048 143 ISFDNQGIGATMAEMVV 159
Cdd:cd06305   98 ITQDDYALGTLSLGQLV 114
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
49-158 5.43e-05

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: 44.53  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  49 SMDSFvverWQRDRDAFLKAAGSHGAQVLLRT-ANEN-VEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIrNRGIP 126
Cdd:cd20008    9 TDSEY----WQTVLKGAEKAAKELGVEVTFLGpATEAdIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAA-DAGIP 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 383106048 127 VLAYDRLVRNTPIDGYISFDNQGIGA----TMAEMV 158
Cdd:cd20008   84 VVLVDSGANTDDYDAFLATDNVAAGAlaadELAELL 119
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
72-156 5.88e-05

ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 44.47  E-value: 5.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  72 HGAQVLLRTANENVEVQRRQLNELAQSGIDVLVV------VPNDSEALsdtIEQIRNRGIPVLAYDRLVRNTPIDgYISF 145
Cdd:cd01541   28 NGYSLLLALTNNDVEKEREILESLLDQNVDGLIIeptksaLPNPNLDL---YEELQKKGIPVVFINSYYPELDAP-SVSL 103
                         90
                 ....*....|.
gi 383106048 146 DNQGIGATMAE 156
Cdd:cd01541  104 DDEKGGYLATK 114
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
67-151 8.68e-05

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


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 43.79  E-value: 8.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  67 KAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEalSDTIEQIRNRGIPVLAYDRLVRNTPIDGYISfD 146
Cdd:cd06280   23 DAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGP--SRELKRLLKHGIPIVLIDREVEGLELDLVAG-D 99

                 ....*
gi 383106048 147 NQGIG 151
Cdd:cd06280  100 NREGA 104
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
84-159 1.04e-04

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: 43.81  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  84 NVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGYIsfdNQ----GIGATMAEMVV 159
Cdd:cd20003   41 SVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVTWDSDVNPDARDFFV---NQatpeGIGKTLVDMVA 117
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
81-159 1.07e-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: 43.84  E-value: 1.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 383106048  81 ANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVrNTPIDGYISFDNQGIGATMAEMVV 159
Cdd:cd19999   42 ADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPV-SSPDAINVVIDQYKWAAIQAQWLA 119
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
68-149 1.38e-04

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


Pssm-ID: 380632 [Multi-domain]  Cd Length: 264  Bit Score: 42.90  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  68 AAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPndSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDgYISFDN 147
Cdd:cd19977   24 EAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAP--TGGNEDLIEKLVKSGIPVVFVDRYIPGLDVD-TVVVDN 100

                 ..
gi 383106048 148 QG 149
Cdd:cd19977  101 FK 102
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
63-259 1.70e-04

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


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 42.91  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  63 DAFLKAAGSHGAQVLLRTANENVEVQRrQLNELAQSGIDVLVVVpndSEALSD-TIEQIRNRGIPVLAYDRLVRNTPIDg 141
Cdd:cd06278   19 EELSRALQARGLRPLLFNVDDEDDVDD-ALRQLLQYRVDGVIVT---SATLSSeLAEECARRGIPVVLFNRVVEDPGVD- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 142 YISFDNQGIGATMAEMVVeagqeaaaaqkadvagqNAAARdtpiQLLVINGAVSDYNSYMINRGIVTALRpyiERGqvrl 221
Cdd:cd06278   94 SVSCDNRAGGRLAADLLL-----------------AAGHR----RIAFLGGPEGTSTSRERERGFRAALA---ELG---- 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 383106048 222 LDNLWLQA--WRNEEAREAIEDGFARFDHIDGVVAANDLI 259
Cdd:cd06278  146 LPPPAVEAgdYSYEGGYEAARRLLAAPDRPDAIFCANDLM 185
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
73-151 1.89e-04

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: 42.64  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  73 GAQV-LLRTANENVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYdrlvrNTPIDGYISFDNQGIG 151
Cdd:cd19965   29 GAECqFTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAF-----NVDAPGGENARLAFVG 103
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
45-158 3.63e-04

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: 41.78  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  45 RIGFSMDSFVVERWQRDRDAFLKAAGSHGAQVL----LRTANENVEVQRRQLNELAQsGIDVLVVVPNDSEALSDTIEQI 120
Cdd:cd06307    1 RFGFLLPSPENPFYELLRRAIEAAAAALRDRRVrlriHFVDSLDPEALAAALRRLAA-GCDGVALVAPDHPLVRAAIDEL 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 383106048 121 RNRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAEMV 158
Cdd:cd06307   80 AARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLM 117
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
84-156 5.04e-04

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


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 41.46  E-value: 5.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 383106048  84 NVEVQRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGYISFDNQGIGATMAE 156
Cdd:cd20005   42 DVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGVPSDLPLATVATDNYAAGALAAD 114
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
95-156 8.78e-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: 8.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 383106048  95 LAQsGIDVLVVVPNDSEALSDTIEQIRNRGIPVLAYD-RLVRNTPIDgyI-SFDNQGIGATMAE 156
Cdd:cd20001   53 IAQ-GVDAICVVPNDPEALEPVLKKARDAGIVVITHEaSNLKNVDYD--VeAFDNAAYGAFIMD 113
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
71-156 1.43e-03

ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor


Pssm-ID: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 39.88  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  71 SHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPndSEALSDTIEQIRNRGIPVLAYDRLVRNTPIDGYISfDNQGI 150
Cdd:cd06274   27 ERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAP--STPPDDIYYLCQAAGLPVVFLDRPFSGSDAPSVVS-DNRAG 103

                 ....*.
gi 383106048 151 GATMAE 156
Cdd:cd06274  104 ARALTE 109
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
65-156 5.88e-03

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: 38.07  E-value: 5.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  65 FLKAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVPNDS-EALSDTIEQIRNRGIPVLAYD----RLVRNTPI 139
Cdd:cd19966   22 AKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGdGAYTPLIEAAKKAGIIVTSFNtdlpKLEYGDCG 101
                         90
                 ....*....|....*..
gi 383106048 140 DGYISFDNQGIGATMAE 156
Cdd:cd19966  102 LGYVGADLYAAGYTLAK 118
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
67-330 6.44e-03

ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 37.89  E-value: 6.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048  67 KAAGSHGAQVLLRTANENVEVQRRQLNELAQSGIDVLVVVpndSEALSDT-IEQIRNRGIPVLAYDRLVRNTPiDGYISF 145
Cdd:cd06270   23 RVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILH---SRALSDEeLILIAEKIPPLVVINRYIPGLA-DRCVWL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 146 DNQGIGATMAEMVVEAgqeaaaaqkadvaGQNAAArdtpiqllVINGAVSDYNSymINR--GIVTALRPY-IErgqvrlL 222
Cdd:cd06270   99 DNEQGGRLAAEHLLDL-------------GHRRIA--------CITGPLDIPDA--RERlaGYRDALAEAgIP------L 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383106048 223 DNLWLQA--WRNEEAREAIEDGFARFDHIDGVVAANDLIADAVVHAAAVRGLAGRLQVS--GMDG-DLAAVQRVAegtqL 297
Cdd:cd06270  150 DPSLIIEgdFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSviGFDDvPLARYLSPK----L 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 383106048 298 MTIYKPVEELAAQALDTAVQLAHGRELA-----TGELI 330
Cdd:cd06270  226 TTVHYPIEEMAQAAAELALNLAYGEPLPishefTPTLI 263
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
88-128 9.69e-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: 37.68  E-value: 9.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 383106048  88 QRRQLNELAQSGIDVLVVVPNDSEALSDTIEQIRNRGIPVL 128
Cdd:cd20002   45 QVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVI 85
 
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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