NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1487551699|gb|AYG19909|]
View 

TMAO reductase system periplasmic protein TorT [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

TMAO reductase system protein TorT( domain architecture ID 11485110)

periplasmic sensory protein TorT binds the osmoregulator trimethylamine-N-oxide (TMAO), and together with the TorSR two-component hybrid sensor histidine kinase/response regulator, activates induction of the TMAO reductase (Tor) respiratory system

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
15-335 2.56e-168

TMAO reductase system periplasmic protein TorT; Provisional


:

Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 472.13  E-value: 2.56e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  15 PAFSADNLLRWHDAQHFTVQASTPLKAKRAWKLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQ 94
Cdd:PRK10936   17 TAFAAANLLTWHLAQRTSLQYSPLLKAKKAWKLCALYPHLKDSYWLSVNYGMVEEAKRLGVDLKVLEAGGYYNLAKQQQQ 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  95 IDQCKQWGAEAILLGSSTTSF--PDLQKQVASLPVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQW--AHGKPLNVL 170
Cdd:PRK10936   97 LEQCVAWGADAILLGAVTPDGlnPDLELQAANIPVIALVNGIDSPQVTTRVGVSWYQMGYQAGRYLAQWhpKGSKPLNVA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 171 LMPGPDNAGGSKEMVEGFRAAIAGSPVRIVDIALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGE--GRNLKT 248
Cdd:PRK10936  177 LLPGPEGAGGSKAVEQGFRAAIAGSDVRIVDIAYGDNDKELQRNLLQELLERHPDIDYIAGSAVAAEAAIGElrGRNLTD 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 249 PLTVVSFYLSHQVYRGLKRGRVIMAASDQMVWQGELAVEQAIRQLQGQSVSDNVSPPILVLTPKNADREHIRRSLSPGGF 328
Cdd:PRK10936  257 KIKLVSFYLSHQVYRGLKRGKVLAAPSDQMVLQGRLAIDQAVRQLEGAPVPGDVGPKILVLTPKNLDSEDLRRSLSPAGF 336

                  ....*..
gi 1487551699 329 RPVYFYQ 335
Cdd:PRK10936  337 RPVYRVQ 343
 
Name Accession Description Interval E-value
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
15-335 2.56e-168

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 472.13  E-value: 2.56e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  15 PAFSADNLLRWHDAQHFTVQASTPLKAKRAWKLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQ 94
Cdd:PRK10936   17 TAFAAANLLTWHLAQRTSLQYSPLLKAKKAWKLCALYPHLKDSYWLSVNYGMVEEAKRLGVDLKVLEAGGYYNLAKQQQQ 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  95 IDQCKQWGAEAILLGSSTTSF--PDLQKQVASLPVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQW--AHGKPLNVL 170
Cdd:PRK10936   97 LEQCVAWGADAILLGAVTPDGlnPDLELQAANIPVIALVNGIDSPQVTTRVGVSWYQMGYQAGRYLAQWhpKGSKPLNVA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 171 LMPGPDNAGGSKEMVEGFRAAIAGSPVRIVDIALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGE--GRNLKT 248
Cdd:PRK10936  177 LLPGPEGAGGSKAVEQGFRAAIAGSDVRIVDIAYGDNDKELQRNLLQELLERHPDIDYIAGSAVAAEAAIGElrGRNLTD 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 249 PLTVVSFYLSHQVYRGLKRGRVIMAASDQMVWQGELAVEQAIRQLQGQSVSDNVSPPILVLTPKNADREHIRRSLSPGGF 328
Cdd:PRK10936  257 KIKLVSFYLSHQVYRGLKRGKVLAAPSDQMVLQGRLAIDQAVRQLEGAPVPGDVGPKILVLTPKNLDSEDLRRSLSPAGF 336

                  ....*..
gi 1487551699 329 RPVYFYQ 335
Cdd:PRK10936  337 RPVYRVQ 343
TMAO_TorT TIGR02955
TMAO reductase system periplasmic protein TorT; Members of this family are the periplasmic ...
46-334 9.65e-167

TMAO reductase system periplasmic protein TorT; Members of this family are the periplasmic protein TorT which, together with the the TorS/TorR histidine kinase/response regulator system, regulates expression of the torCAD operon for trimethylamine N-oxide reductase (TMAO reductase). It appears to bind an inducer for TMAO reductase, and shows homology to a periplasmic D-ribose binding protein.


Pssm-ID: 132000 [Multi-domain]  Cd Length: 295  Bit Score: 466.17  E-value: 9.65e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  46 KLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLGSSTTSF--PDLQKQVA 123
Cdd:TIGR02955   1 KLCALYPHLKDSYWLSINYGMVEQAKHLGVELKVLEAGGYPNLDKQLAQIEQCKSWGADAILLGTVSPEAlnHDLAQLTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 124 SLPVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQwAHGK---PLNVLLMPGPDNAGGSKEMVEGFRAAIAGSPVRIV 200
Cdd:TIGR02955  81 SIPVFALVNQIDSNQVKGRVGVDWYQMGYQAGEYLAQ-RHPKgsgPTTLAWLPGPKNRGGTKPVTQGFRAALEGSDVEIS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 201 DIALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGE--GRNLKTPLTVVSFYLSHQVYRGLKRGRVIMAASDQM 278
Cdd:TIGR02955 160 AILWADNDKELQRNLLQDLLKKHPDIDYLVGSAVAAEAAISElrSLHMTQQIKLVSTYLSHGVYRGLKRGKVLFAPTDQM 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1487551699 279 VWQGELAVEQAIRQLQGQSVSDNVSPPILVLTPKNADREHIRRSLSPGGFRPVYFY 334
Cdd:TIGR02955 240 VLQGKLAIDQAVRYLEGKPVSFDQAPKIEALTPQHLPREVIEDSLSPAEFRPVYQV 295
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
46-309 3.74e-112

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: 326.85  E-value: 3.74e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  46 KLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQKQVA 123
Cdd:cd06306     1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGGYTNLSKQISQLEDCVASGADAILLGaiSFDGLDPKVAEAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 124 S-LPVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPLNVLLMPGPDNAGGSKEMVEGFRAAIAGSPVRIVDI 202
Cdd:cd06306    81 AgIPVIDLVNGIDSPKVAARVLVDFYDMGYLAGEYLVEHHPGKPVKVAWFPGPAGAGWAEDREKGFKEALAGSNVEIVAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 203 ALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGEGR--NLKTPLTVVSFYLSHQVYRGLKRGRVIMAASDQMVW 280
Cdd:cd06306   161 KYGDTGKAVQLNLVEDALQAHPDIDYIVGNAVAAEAAVGALReaGLTGKVKVVSTYLTPGVYRGIKRGKILAAPSDQPVL 240
                         250       260
                  ....*....|....*....|....*....
gi 1487551699 281 QGELAVEQAIRQLQGQSVSDNVSPPILVL 309
Cdd:cd06306   241 QGRIAVDQAVRALEGKPVPKHVGPPILVV 269
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
44-337 9.48e-98

Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 290.57  E-value: 9.48e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  44 AWKLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQqaQIDQCKQWGAEAILLGSSTTSFPDLQKQVA 123
Cdd:pfam00532   1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTN--AIDLLLASGADGIIITTPAPSGDDITAKAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 124 S--LPVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPlnVLLMPGPDNAGGSKEMVEGFRAAI--AGSPVRI 199
Cdd:pfam00532  79 GygIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRP--IAVMAGPASALTARERVQGFMAALaaAGREVKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 200 VDIALGDNDIEIQRNLLQEMLERHPEIDVV-----AGTAIAAEAAMGEGRnLKTPLTVVSFYLSHQVYRGLKRgrvimaA 274
Cdd:pfam00532 157 YHVATGDNDIPDAALAANAMLVSHPTIDAIvamndEAAMGAVRALLKQGR-VKIPDIVGIGINSVVGFDGLSK------A 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487551699 275 SDQMVWQGELAVEQAIRQLQGQSVSDNVSPPIlvltpkNADREHIRRSLSpggfrPVYFYQHT 337
Cdd:pfam00532 230 QDTGLYLSPLTVIQLPRQLLGIKASDMVYQWI------PKFREHPRVLLI-----PRDFFKET 281
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
35-314 5.31e-50

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: 168.95  E-value: 5.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  35 ASTPLKAKRAWKLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGysQLATQQAQIDQCKQWGAEAILLgsSTTS 114
Cdd:COG1879    24 AEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEG--DAAKQISQIEDLIAQGVDAIIV--SPVD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 115 FPDLQKQVASL-----PVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFR 189
Cdd:COG1879   100 PDALAPALKKAkaagiPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKG-KVAILTGSPGAPAANERTDGFK 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 190 AAIAGSP-VRIVDIALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAaeaaMGEG-------RNLKTPLTVVSFYLSHQV 261
Cdd:COG1879   179 EALKEYPgIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDG----MALGaaqalkaAGRKGDVKVVGFDGSPEA 254
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1487551699 262 YRGLKRGRVIMAASDQMVWQGELAVEQAIRQLQGQSVSDNVSPPILVLTPKNA 314
Cdd:COG1879   255 LQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
 
Name Accession Description Interval E-value
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
15-335 2.56e-168

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 472.13  E-value: 2.56e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  15 PAFSADNLLRWHDAQHFTVQASTPLKAKRAWKLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQ 94
Cdd:PRK10936   17 TAFAAANLLTWHLAQRTSLQYSPLLKAKKAWKLCALYPHLKDSYWLSVNYGMVEEAKRLGVDLKVLEAGGYYNLAKQQQQ 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  95 IDQCKQWGAEAILLGSSTTSF--PDLQKQVASLPVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQW--AHGKPLNVL 170
Cdd:PRK10936   97 LEQCVAWGADAILLGAVTPDGlnPDLELQAANIPVIALVNGIDSPQVTTRVGVSWYQMGYQAGRYLAQWhpKGSKPLNVA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 171 LMPGPDNAGGSKEMVEGFRAAIAGSPVRIVDIALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGE--GRNLKT 248
Cdd:PRK10936  177 LLPGPEGAGGSKAVEQGFRAAIAGSDVRIVDIAYGDNDKELQRNLLQELLERHPDIDYIAGSAVAAEAAIGElrGRNLTD 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 249 PLTVVSFYLSHQVYRGLKRGRVIMAASDQMVWQGELAVEQAIRQLQGQSVSDNVSPPILVLTPKNADREHIRRSLSPGGF 328
Cdd:PRK10936  257 KIKLVSFYLSHQVYRGLKRGKVLAAPSDQMVLQGRLAIDQAVRQLEGAPVPGDVGPKILVLTPKNLDSEDLRRSLSPAGF 336

                  ....*..
gi 1487551699 329 RPVYFYQ 335
Cdd:PRK10936  337 RPVYRVQ 343
TMAO_TorT TIGR02955
TMAO reductase system periplasmic protein TorT; Members of this family are the periplasmic ...
46-334 9.65e-167

TMAO reductase system periplasmic protein TorT; Members of this family are the periplasmic protein TorT which, together with the the TorS/TorR histidine kinase/response regulator system, regulates expression of the torCAD operon for trimethylamine N-oxide reductase (TMAO reductase). It appears to bind an inducer for TMAO reductase, and shows homology to a periplasmic D-ribose binding protein.


Pssm-ID: 132000 [Multi-domain]  Cd Length: 295  Bit Score: 466.17  E-value: 9.65e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  46 KLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLGSSTTSF--PDLQKQVA 123
Cdd:TIGR02955   1 KLCALYPHLKDSYWLSINYGMVEQAKHLGVELKVLEAGGYPNLDKQLAQIEQCKSWGADAILLGTVSPEAlnHDLAQLTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 124 SLPVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQwAHGK---PLNVLLMPGPDNAGGSKEMVEGFRAAIAGSPVRIV 200
Cdd:TIGR02955  81 SIPVFALVNQIDSNQVKGRVGVDWYQMGYQAGEYLAQ-RHPKgsgPTTLAWLPGPKNRGGTKPVTQGFRAALEGSDVEIS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 201 DIALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGE--GRNLKTPLTVVSFYLSHQVYRGLKRGRVIMAASDQM 278
Cdd:TIGR02955 160 AILWADNDKELQRNLLQDLLKKHPDIDYLVGSAVAAEAAISElrSLHMTQQIKLVSTYLSHGVYRGLKRGKVLFAPTDQM 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1487551699 279 VWQGELAVEQAIRQLQGQSVSDNVSPPILVLTPKNADREHIRRSLSPGGFRPVYFY 334
Cdd:TIGR02955 240 VLQGKLAIDQAVRYLEGKPVSFDQAPKIEALTPQHLPREVIEDSLSPAEFRPVYQV 295
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
46-309 3.74e-112

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: 326.85  E-value: 3.74e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  46 KLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQKQVA 123
Cdd:cd06306     1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGGYTNLSKQISQLEDCVASGADAILLGaiSFDGLDPKVAEAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 124 S-LPVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPLNVLLMPGPDNAGGSKEMVEGFRAAIAGSPVRIVDI 202
Cdd:cd06306    81 AgIPVIDLVNGIDSPKVAARVLVDFYDMGYLAGEYLVEHHPGKPVKVAWFPGPAGAGWAEDREKGFKEALAGSNVEIVAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 203 ALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGEGR--NLKTPLTVVSFYLSHQVYRGLKRGRVIMAASDQMVW 280
Cdd:cd06306   161 KYGDTGKAVQLNLVEDALQAHPDIDYIVGNAVAAEAAVGALReaGLTGKVKVVSTYLTPGVYRGIKRGKILAAPSDQPVL 240
                         250       260
                  ....*....|....*....|....*....
gi 1487551699 281 QGELAVEQAIRQLQGQSVSDNVSPPILVL 309
Cdd:cd06306   241 QGRIAVDQAVRALEGKPVPKHVGPPILVV 269
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
44-337 9.48e-98

Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 290.57  E-value: 9.48e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  44 AWKLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQqaQIDQCKQWGAEAILLGSSTTSFPDLQKQVA 123
Cdd:pfam00532   1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTN--AIDLLLASGADGIIITTPAPSGDDITAKAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 124 S--LPVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPlnVLLMPGPDNAGGSKEMVEGFRAAI--AGSPVRI 199
Cdd:pfam00532  79 GygIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRP--IAVMAGPASALTARERVQGFMAALaaAGREVKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 200 VDIALGDNDIEIQRNLLQEMLERHPEIDVV-----AGTAIAAEAAMGEGRnLKTPLTVVSFYLSHQVYRGLKRgrvimaA 274
Cdd:pfam00532 157 YHVATGDNDIPDAALAANAMLVSHPTIDAIvamndEAAMGAVRALLKQGR-VKIPDIVGIGINSVVGFDGLSK------A 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487551699 275 SDQMVWQGELAVEQAIRQLQGQSVSDNVSPPIlvltpkNADREHIRRSLSpggfrPVYFYQHT 337
Cdd:pfam00532 230 QDTGLYLSPLTVIQLPRQLLGIKASDMVYQWI------PKFREHPRVLLI-----PRDFFKET 281
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
35-314 5.31e-50

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: 168.95  E-value: 5.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  35 ASTPLKAKRAWKLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGysQLATQQAQIDQCKQWGAEAILLgsSTTS 114
Cdd:COG1879    24 AEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEG--DAAKQISQIEDLIAQGVDAIIV--SPVD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 115 FPDLQKQVASL-----PVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFR 189
Cdd:COG1879   100 PDALAPALKKAkaagiPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKG-KVAILTGSPGAPAANERTDGFK 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 190 AAIAGSP-VRIVDIALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAaeaaMGEG-------RNLKTPLTVVSFYLSHQV 261
Cdd:COG1879   179 EALKEYPgIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDG----MALGaaqalkaAGRKGDVKVVGFDGSPEA 254
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1487551699 262 YRGLKRGRVIMAASDQMVWQGELAVEQAIRQLQGQSVSDNVSPPILVLTPKNA 314
Cdd:COG1879   255 LQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
46-308 5.54e-32

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: 120.36  E-value: 5.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  46 KLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGysQLATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQKQVA 123
Cdd:cd01536     1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQG--DVAKQISQIEDLIAQGVDAIIIApvDSEALVPAVKKANA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 124 S-LPVIELVNAIDAP-QVKSRVGVPWFQMGYQPGRYLVQwAHGKPLNVLLMPGPDNAGGSKEMVEGFRAAIAGSP-VRIV 200
Cdd:cd01536    79 AgIPVVAVDTDIDGGgDVVAFVGTDNYEAGKLAGEYLAE-ALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYPdIEIV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 201 DIALGDNDIEIQRNLLQEMLERHPEIDVVagtaIAAEAAMGEG-------RNLKTPLTVVSFYLSHQVYRGLKRGRVIMA 273
Cdd:cd01536   158 AEQPANWDRAKALTVTENLLQANPDIDAV----FAANDDMALGaaealkaAGRTGDIKIVGVDGTPEALKAIKDGELDAT 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1487551699 274 ASDQMVWQGELAVEQAIRQLQGQSVSDNVSPPILV 308
Cdd:cd01536   234 VAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPVTL 268
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
50-297 1.04e-16

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: 78.51  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  50 LYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQlATQQAQIDQCKQWGAEAILLgsSTTSFPDLQKQVASL---- 125
Cdd:pfam13407   4 VPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADA-AEQVAQIEDAIAQGVDAIIV--APVDPTALAPVLKKAkdag 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 126 -PVIelvnAIDAPQVKSR----VGVPWFQMGYQPGRYLVQWAHGKpLNVLLMPGPDNAGGSKEMVEGFRAAIAGSP--VR 198
Cdd:pfam13407  81 iPVV----TFDSDAPSSPrlayVGFDNEAAGEAAGELLAEALGGK-GKVAILSGSPGDPNANERIDGFKKVLKEKYpgIK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 199 IVDIALGDN-DIEIQRNLLQEMLERHP-EIDVVAGTAIAAEAAMG---EGRNLKTPLTVVSFYLSHQVYRGLKRGRVIMA 273
Cdd:pfam13407 156 VVAEVEGTNwDPEKAQQQMEALLTAYPnPLDGIISPNDGMAGGAAqalEAAGLAGKVVVTGFDATPEALEAIKDGTIDAT 235
                         250       260
                  ....*....|....*....|....
gi 1487551699 274 ASDQMVWQGELAVEQAIRQLQGQS 297
Cdd:pfam13407 236 VLQDPYGQGYAAVELAAALLKGKK 259
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
46-315 3.14e-16

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: 77.69  E-value: 3.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  46 KLCALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYS----QLATQQAQIDQckqwGAEAILLG--SSTTSFPDLQ 119
Cdd:cd06320     1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAAPSETdtqgQLNLLETMLNK----GYDAILVSpiSDTNLIPPIE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 120 K-QVASLPVIELVNAIDAPQVK-------SRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFRAA 191
Cdd:cd06320    77 KaNKKGIPVINLDDAVDADALKkaggkvtSFIGTDNVAAGALAAEYIAEKLPGGG-KVAIIEGLPGNAAAEARTKGFKET 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 192 IAGSP-VRIVDIALGDNDIEIQRNLLQEMLERHPEI-------DVvagtaiaaeaaMGEG-------RNLKTPLTVVSFY 256
Cdd:cd06320   156 FKKAPgLKLVASQPADWDRTKALDAATAILQAHPDLkgiyaanDT-----------MALGaveavkaAGKTGKVLVVGTD 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1487551699 257 LSHQVYRGLKRGRviMAAS-DQM-VWQGELAVEQAIRQLQGQSVSDNVSPPILVLTPKNAD 315
Cdd:cd06320   225 GIPEAKKSIKAGE--LTATvAQYpYLEGAMAVEAALRLLQGQKVPAVVATPQALITKDNVD 283
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
52-308 5.13e-16

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: 76.94  E-value: 5.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILL--GSSTTSFPDLQK-QVASLPVI 128
Cdd:cd06321     7 QDLGNPFFVAMVRGAEEAAAEINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLnaADSAGIEPAIKRaKDAGIIVV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 129 elvnAIDAPQ--VKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAgGSKEMVEGFRAAIAGSP-VRIVDIALG 205
Cdd:cd06321    87 ----AVDVAAegADATVTTDNVQAGYLACEYLVEQLGGKG-KVAIIDGPPVS-AVIDRVNGCKEALAEYPgIKLVDDQNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 206 DNDIEIQRNLLQEMLERHPEIDVVagtaIAAEAAMGEGRNL------KTPLTVVSFYLSHQVYRGLKRGR---VIMAASD 276
Cdd:cd06321   161 KGSRAGGLSVMTRMLTAHPDVDGV----FAINDPGAIGALLaaqqagRDDIVITSVDGSPEAVAALKREGspfIATAAQD 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1487551699 277 QMVwQGELAVEQAIRQLQGQSVSDNV--SPPILV 308
Cdd:cd06321   237 PYD-MARKAVELALKILNGQEPAPELvlIPSTLV 269
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
52-310 5.32e-16

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: 76.57  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSqlATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQK-QVASLPVI 128
Cdd:cd06323     7 STLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDP--AKQLSQVEDLIVRKVDALLINptDSDAVSPAVEEaNEAGIPVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 129 ELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFRAAIAGSP-VRIVDIALGDN 207
Cdd:cd06323    85 TVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKG-KVVELQGIPGTSAARERGKGFHNAIAKYPkINVVASQTADF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 208 DIEIQRNLLQEMLERHPEIDVVagtaIAAEAAMGEG-------RNLKTPLtVVSFYLSHQVYRGLKRGRVIMAASDQMVW 280
Cdd:cd06323   164 DRTKGLNVMENLLQAHPDIDAV----FAHNDEMALGaiqalkaAGRKDVI-VVGFDGTPDAVKAVKDGKLAATVAQQPEE 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 1487551699 281 QGELAVEQAIRQLQGQSVSDNVSPPILVLT 310
Cdd:cd06323   239 MGAKAVETADKYLKGEKVPKKIPVPLKLVT 268
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
56-310 3.95e-15

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: 74.30  E-value: 3.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  56 DSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLgsSTTSFPDLQKQV-----ASLPVIEL 130
Cdd:cd06310    11 SAFWRTVREGAEAAAKDLGVKIIFVGPESEEDVAGQNSLLEELINKKPDAIVV--APLDSEDLVDPLkdakdKGIPVIVI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 131 VNAIDAPQVKSRVGVPWFQMGYQPGRYLVQwAHGKPLNVLLMPGPDNAGGSKEMVEGFRAAIAGSP--VRIVDIALGDND 208
Cdd:cd06310    89 DSGIKGDAYLSYIATDNYAAGRLAAQKLAE-ALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPggIKVLASQYAGSD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 209 IEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGEG---RNLKTPLTVVSFYLSHQVYRGLKRGRVimaasDQMVWQ---- 281
Cdd:cd06310   168 YAKAANETEDLLGKYPDIDGIFATNEITALGAAVAiksRKLSGQIKIVGFDSQEELLDALKNGKI-----DALVVQnpye 242
                         250       260       270
                  ....*....|....*....|....*....|
gi 1487551699 282 -GELAVEQAIRQLQGQSVSDNVSPPILVLT 310
Cdd:cd06310   243 iGYEGIKLALKLLKGEEVPKNIDTGAELIT 272
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
66-308 9.25e-15

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: 73.44  E-value: 9.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  66 MQEAARRY-----GVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILL--GSSTTSFPDLQKQV-ASLPVIELVNAIDAP 137
Cdd:cd19970    17 MEKGARKHakeanGYELLVKGIKQETDIEQQIAIVENLIAQKVDAIVIapADSKALVPVLKKAVdAGIAVINIDNRLDAD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 138 QVKSR------VGVPWFQMGYQPGRYLVQwAHGKPLNVLLMPGPDNAGGSKEMVEGFRAAIAGSPVRIVDIALGDNDIEI 211
Cdd:cd19970    97 ALKEGginvpfVGPDNRQGAYLAGDYLAK-KLGKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAGMKIVASQSANWEIDE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 212 QRNLLQEMLERHPEIDVVagtaIAAEAAMGEG-------RNLKTPLTVVSFYLSHQVYRGLKRGRVIMAASDQMVWQGEL 284
Cdd:cd19970   176 ANTVAANLLTAHPDIRGI----LCANDNMALGaikavdaAGKAGKVLVVGFDNIPAVRPLLKDGKMLATIDQHPAKQAVY 251
                         250       260
                  ....*....|....*....|....
gi 1487551699 285 AVEQAIRQLQGQSVSDNVSPPILV 308
Cdd:cd19970   252 GIEYALKMLNGEEVPGWVKTPVEL 275
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
48-316 3.78e-14

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: 71.64  E-value: 3.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  48 CALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGysQLATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQK-QVAS 124
Cdd:cd06317     3 ALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNAND--DPSKQNTAVDNYIARGVDAIILDaiDVNGSIPAIKRaSEAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 125 LPVIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWA----HGKPLNVLLmpGPDNAGGSKEMVEGFRAAIAGSP-VRI 199
Cdd:cd06317    81 IPVIAYDAVIPSDFQAAQVGVDNLEGGKEIGKYAADYIkaelGGQAKIGVV--GALSSLIQNQRQKGFEEALKANPgVEI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 200 VDIALGDNDIEIQRNLLQEMLERHPEIDVVAGT---AIAAEAAMGEGRNLKTPLTVVSFYLSHQ-VYRGLKRGRVIMAAS 275
Cdd:cd06317   159 VATVDGQNVQEKALSAAENLLTANPDLDAIYATgepALLGAVAAVRSQGRQGKIKVFGWDLTKQaIFLGIDEGVLQAVVQ 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1487551699 276 DQMVWQGELAVEQAIRQLQGQSVSDNVSPPILVLTPKNADR 316
Cdd:cd06317   239 QDPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTKENVDQ 279
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
56-311 9.55e-14

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: 70.34  E-value: 9.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  56 DSYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLGSSTTSF--PDLQKQVASLPVIELVNA 133
Cdd:cd20008    11 SEYWQTVLKGAEKAAKELGVEVTFLGPATEADIAGQVNLVENAISRKPDAIVLAPNDTAAlvPAVEAADAGIPVVLVDSG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 134 IDAPQVKSRVGVPWFQMGYQPGRYLV---QWAHGKPLNVLLMPGPDNAGGSKEMVEGFRAAIAGSP--VRIVDIALGDND 208
Cdd:cd20008    91 ANTDDYDAFLATDNVAAGALAADELAellKASGGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKYpdIEIVDVQYSDGD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 209 IEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGEG---RNLKTPLTVVSFYLSHQVYRGLKRGrVIMAASDQMVWQ-GEL 284
Cdd:cd20008   171 IAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQAlaeAGKAGKIVLVGFDSSPDEVALLKSG-VIKALVVQDPYQmGYE 249
                         250       260
                  ....*....|....*....|....*...
gi 1487551699 285 AVEQAIRQLQGQS-VSDNVSPPILVLTP 311
Cdd:cd20008   250 GVKTAVKALKGEEiVEKNVDTGVTVVTK 277
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
53-229 2.37e-13

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: 69.11  E-value: 2.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  53 SLKDSYWLSLNYGMQEAARRY-GVDLKVLEAGGYSqlATQQAQIDQCKQWGAEAILLgSSTTSFPdLQKQV-----ASLP 126
Cdd:cd06308     8 SLNDPWRAAMNEEIKAEAAKYpNVELIVTDAQGDA--AKQIADIEDLIAQGVDLLIV-SPNEADA-LTPVVkkaydAGIP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 127 VIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFRAAIAGSP-VRIVDIALG 205
Cdd:cd06308    84 VIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKG-NVVEIQGLPGSSPAIDRHKGFLEAIAKYPgIKIVASQDG 162
                         170       180
                  ....*....|....*....|....
gi 1487551699 206 DNDIEIQRNLLQEMLERHPEIDVV 229
Cdd:cd06308   163 DWLRDKAIKVMEDLLQAHPDIDAV 186
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
52-310 2.95e-13

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: 68.84  E-value: 2.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGysQLATQQAQIDQCKQWGAEAILL-----GSSTTSFPDLQKqvASLP 126
Cdd:cd06322     7 LTLQHPFFVDIKDAMKKEAAELGVKVVVADANG--DLAKQLSQIEDFIQQGVDAIILapvdsGGIVPAIEAANE--AGIP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 127 VIELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPLNVLLMPGPDnAGGSKEMVEGFRAAIAGSP-VRIVDIALG 205
Cdd:cd06322    83 VFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKALLGGGGKIAIIDYPE-VESVVLRVNGFKEAIKKYPnIEIVAEQPG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 206 DNDIEIQRNLLQEMLERHPEIDVVagTAIAAEAAMG-----EGRNLKTPLTVVSFYLSHQVYRGLKRGRVIMAasdqMVW 280
Cdd:cd06322   162 DGRREEALAATEDMLQANPDLDGI--FAIGDPAALGaltaiESAGKEDKIKVIGFDGNPEAIKAIAKGGKIKA----DIA 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1487551699 281 Q-----GELAVEQAIRQLQGQSVSDNVSPPILVLT 310
Cdd:cd06322   236 QqpdkiGQETVEAIVKYLAGETVEKEILIPPKLYT 270
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
58-302 4.08e-13

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 68.39  E-value: 4.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  58 YWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLgsSTTSFPDLQKQV-----ASLPVIELVN 132
Cdd:cd20006    15 FWQTVKSGAEAAAKEYGVDLEFLGPESEEDIDGQIELIEEAIAQKPDAIVL--AASDYDRLVEAVerakkAGIPVITIDS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 133 AIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFRAAIAGSP-VRIVDIALGDNDIEI 211
Cdd:cd20006    93 PVNSKKADSFVATDNYEAGKKAGEKLASLLGEKG-KVAIVSFVKGSSTAIEREEGFKQALAEYPnIKIVETEYCDSDEEK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 212 QRNLLQEMLERHPEIDVVagTAIAAEAAMGEGRNLK-TPLT----VVSFYLSHQVYRGLKRGRVimaasDQMVWQ----- 281
Cdd:cd20006   172 AYEITKELLSKYPDINGI--VALNEQSTLGAARALKeLGLGgkvkVVGFDSSVEEIQLLEEGII-----DALVVQnpfnm 244
                         250       260
                  ....*....|....*....|.
gi 1487551699 282 GELAVEQAIRQLQGQSVSDNV 302
Cdd:cd20006   245 GYLSVQAAVDLLNGKKIPKRI 265
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
50-313 7.81e-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: 64.69  E-value: 7.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  50 LYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEA--GGYSQLATQQAQIDQckqwGAEAILLgSSTTSfpdlqkqVASLPV 127
Cdd:cd06319     5 SVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQknSANEQVTNANDLIAQ----GVDGIII-SPTNS-------SAAPTV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 128 IELVNAIDAPQVKSRVGVPW-----------FQMGYQPGRYLVQ------WAHGKPLNVLLMPGPDNAggsKEMVEGFRA 190
Cdd:cd06319    73 LDLANEAKIPVVIADIGTGGgdyvsyiisdnYDGGYQAGEYLAEalkengWGGGSVGIIAIPQSRVNG---QARTAGFED 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 191 AIAGSPVRIVDIAL-GDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEAamGEGRNLKTP-----LTVVSFYLSHQVYRG 264
Cdd:cd06319   150 ALEEAGVEEVALRQtPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQ--GALQAIEEAgrtgdILVVGFDGDPEALDL 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1487551699 265 LKRGRVIMAASDQMVWQGELAVEQAIRQLQG-QSVSDNVSPPILVLTPKN 313
Cdd:cd06319   228 IKDGKLDGTVAQQPFGMGARAVELAIQALNGdNTVEKEIYLPVLLVTSEN 277
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
57-311 1.71e-11

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: 63.79  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  57 SYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLgsSTTSFPDLQKQVASL-----PVIELV 131
Cdd:cd20004    12 DFWKSVKAGAEKAAQELGVEIYWRGPSREDDVEAQIQIIEYFIDQGVDGIVL--APLDRKALVAPVERAraqgiPVVIID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 132 NAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFR-AAIAGSP-VRIVDIALGDNDI 209
Cdd:cd20004    90 SDLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKG-KVALLRLAKGSASTTDRERGFLeALKKLAPgLKVVDDQYAGGTV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 210 EIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGEG---RNLKTPLTVVSFYLSHQVYRGLKRGrVIMAASDQMVWQ-GELA 285
Cdd:cd20004   169 GEARSSAENLLNQYPDVDGIFTPNESTTIGALRAlrrLGLAGKVKFIGFDASDLLLDALRAG-EISALVVQDPYRmGYLG 247
                         250       260
                  ....*....|....*....|....*.
gi 1487551699 286 VEQAIRQLQGQSVSDNVSPPILVLTP 311
Cdd:cd20004   248 VKTAVAALRGKPVPKRIDTGVVLVTK 273
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
52-310 9.12e-11

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: 61.44  E-value: 9.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGVDLkVLEAGGYSQLATQQAQIDQCKQWGAEAILL-GSSTTSFPDLQKQVAS--LPVI 128
Cdd:cd06314     7 KGLNNPFWDLAEAGAEKAAKELGVNV-EFVGPQKSDAAEQVQLIEDLIARGVDGIAIsPNDPEAVTPVINKAADkgIPVI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 129 eLVNAiDAPQVKsR---VGVPWFQMGYQPGRYLVQwAHGKPLNVLLM---PGPDNAggsKEMVEGFRAAIAGSP-VRIVD 201
Cdd:cd06314    86 -TFDS-DAPDSK-RlayIGTDNYEAGREAGELMKK-ALPGGGKVAIItggLGADNL---NERIQGFKDALKGSPgIEIVD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 202 IaLGDNDIEIQ-RNLLQEMLERHPEIDV---VAGTAIAAEAAMGEGRNLKTPLTVVSFYLSHQVYRGLKRGRVimaasDQ 277
Cdd:cd06314   159 P-LSDNDDIAKaVQNVEDILKANPDLDAifgVGAYNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVI-----AA 232
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1487551699 278 MVWQ-----GELAVEQAIRQLQ-GQSVSDNVSPPILVLT 310
Cdd:cd06314   233 TVGQrpyemGYLSVKLLYKLLKgGKPVPDVIDTGVDVVT 271
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
52-289 9.50e-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: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 61.48  E-value: 9.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSqlATQQAQ-IDQCKQWGAEAILlgsSTTSFPD-----LQKQVAS- 124
Cdd:cd06312     8 GSPSDPFWSVVKKGAKDAAKDLGVTVQYLGPQNND--IADQARlIEQAIAAKPDGII---VTIPDPDalepaLKRAVAAg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 125 LPVIeLVNAIDaPQVKSR------VGVPWFQMGYQPGRYLVQwahGKPLNVL-LMPGPDNAgGSKEMVEGFRAAIAGSPV 197
Cdd:cd06312    83 IPVI-AINSGD-DRSKERlgaltyVGQDEYLAGQAAGERALE---AGPKNALcVNHEPGNP-GLEARCKGFADAFKGAGI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 198 RIVDIALGDNDIEIQrNLLQEMLERHPEIDVVAGTAIAAEAAMGEGRN---LKTPLTVVSFYLSHQVYRGLKRGRvIMAA 274
Cdd:cd06312   157 LVELLDVGGDPTEAQ-EAIKAYLQADPDTDAVLTLGPVGADPALKAVKeagLKGKVKIGTFDLSPETLEAIKDGK-ILFA 234
                         250
                  ....*....|....*.
gi 1487551699 275 SDQMVW-QGELAVEQA 289
Cdd:cd06312   235 IDQQPYlQGYLAVVFL 250
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
49-229 3.25e-10

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: 59.91  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  49 ALYPSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGgYSQlATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQK-QVASL 125
Cdd:cd19971     4 FSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQ-LDQ-NKQNEQIEDMINQGVDAIFLNpvDSEGIRPALEAaKEAGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 126 PVIelvnAIDAP-----QVKSRVGVPWFQMGYQPGRYLVQwAHGKPLNVLLMPGPdNAGGSKEMVEGFRAAIAGSP-VRI 199
Cdd:cd19971    82 PVI----NVDTPvkdtdLVDSTIASDNYNAGKLCGEDMVK-KLPEGAKIAVLDHP-TAESCVDRIDGFLDAIKKNPkFEV 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 1487551699 200 VDIALGDNDIEIQRNLLQEMLERHPEIDVV 229
Cdd:cd19971   156 VAQQDGKGQLEVAMPIMEDILQAHPDLDAV 185
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
50-229 1.04e-09

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: 58.77  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  50 LYPSLKD-SYWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQ--IDQCKqwGAEAILL----GSSTTSFPDLQKqv 122
Cdd:cd06324     5 INPGKEDePFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEelLARPP--KPDYLILvnekGVAPELLELAEQ-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 123 ASLPVIELVNAIDAPQvKSRVGVP------W--------FQMGYQPGRYLV----QWAHGKPLNVLLMPGPDNAGGSKEM 184
Cdd:cd06324    81 AKIPVFLINNDLTDEE-RALLGKPrekfkyWlgsivpdnEQAGYLLAKALIkaarKKSDDGKIRVLAISGDKSTPASILR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1487551699 185 VEGFRAAIAGSP-VRIVDIALGDNDIEIQRNLLQEMLERHPEIDVV 229
Cdd:cd06324   160 EQGLRDALAEHPdVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIV 205
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
49-310 3.40e-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: 380662 [Multi-domain]  Cd Length: 271  Bit Score: 56.86  E-value: 3.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  49 ALYPSLK-DSYWLSLNYGMQEAARRYGVDLKVLEAGGYSqLATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQKQVAS- 124
Cdd:cd20007     3 ALVPGVTgDPFYITMQCGAEAAAKELGVELDVQGPPTFD-PTLQTPIVNAVIAKKPDALLIAptDPQALIAPLKRAADAg 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 125 LPVIELVNAIDAPQVK-SRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFRAAIAGSP-VRIVDI 202
Cdd:cd20007    82 IKVVTVDTTLGDPSFVlSQIASDNVAGGALAAEALAELIGGKG-KVLVINSTPGVSTTDARVKGFAEEMKKYPgIKVLGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 203 ALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAeaamGEG-----RN--LKTPLTVVSFYLSHQVYRGLKRGRVIMAAS 275
Cdd:cd20007   161 QYSENDPAKAASIVAAALQANPDLAGIFGTNTFS----AEGaaaalRNagKTGKVKVVGFDASPAQVEQLKAGTIDALIA 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1487551699 276 DQMVWQGELAVEQAIRQLQGQSVSDNVSPPILVLT 310
Cdd:cd20007   237 QKPAEIGYLAVEQAVAALTGKPVPKDILTPFVVIT 271
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
65-229 1.39e-08

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: 55.30  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  65 GMQEAARRYGVDLKVLEAGGYS--QLATQQAQIDQckqwGAEAILLGSSTTSFPD--LQK-QVASLPVIEL---VNAIDA 136
Cdd:cd06309    20 SIKEAAKKRGYELVYTDANQDQekQINDIRDLIAQ----GVDAILISPIDATGWDpvLKEaKDAGIPVILVdrtIDGEDG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 137 PQVKSRVGVPWFQMGYQPGRYLVQWAHGKPLNVLLMPGPDNAGGSKEMVEGFRAAIAGSP-VRIVDIALGDNDIEIQRNL 215
Cdd:cd06309    96 SLYVTFIGSDFVEEGRRAAEWLVKNYKGGKGNVVELQGTAGSSVAIDRSKGFREVIKKHPnIKIVASQSGNFTREKGQKV 175
                         170
                  ....*....|....*
gi 1487551699 216 LQEMLERHP-EIDVV 229
Cdd:cd06309   176 MENLLQAGPgDIDVI 190
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
66-315 4.21e-08

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


Pssm-ID: 380651 [Multi-domain]  Cd Length: 302  Bit Score: 53.78  E-value: 4.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  66 MQEAARRYGVDLK---VLEAGGYSQlaTQQAQI-DQCKQwGAEAILL--GSSTTSFPDLQKQVAS-LPVIELVNAIDAPQ 138
Cdd:cd19996    21 FEAEAAKLKKLIKeliYTDAQGDTQ--KQIADIqDLIAQ-GVDAIIVspNSPTALLPAIEKAAAAgIPVVLFDSGVGSDK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 139 VKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFRAAIAGSP-VRIVDIALGDNDIEIQRNLLQ 217
Cdd:cd19996    98 YTAFVGVDDAAFGRVGAEWLVKQLGGKG-NIIALRGIAGVSVSEDRWAGAKEVFKEYPgIKIVGEVYADWDYAKAKQAVE 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 218 EMLERHPEIDVVAGTAIAAEA---------------AMGEGRNlktpltvvSFYLSHQVYRGLKrgrviMAASDQMVWQG 282
Cdd:cd19996   177 SLLAAYPDIDGVWSDGGAMTLgaieafeeagrplvpMTGEDNN--------GFLKAWKELPGFK-----SIAPSYPPWLG 243
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1487551699 283 ELAVEQAIRQLQGQSVSDNVSPPILVLTPKNAD 315
Cdd:cd19996   244 ATALDAALAALEGEPVPKYVYIPLPVITDENLD 276
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
66-315 6.10e-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: 53.48  E-value: 6.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  66 MQEAARRYGVD-----LKVLEAGGYsqlATQQ-AQIDQCKQWGAEAILLG-SSTTSFPDLQKQV--ASLPVIELVNAIDA 136
Cdd:cd06300    21 LKADAAQSGQKglvkeLIVANSNGD---ATEQiAQIRNLIDQGVDAIIINpSSPTALNAVIEQAadAGIPVVAFDGAVTS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 137 PQVKSrVGVPWFQMGYQPGRYLVQwAHGKPLNVLLMPGPDNAGGSKEMVEGFRAAIAGSP-VRIVDIALGDNDIEIQRNL 215
Cdd:cd06300    98 PDAYN-VSNDQVEWGRLGAKWLFE-ALGGKGNVLVVRGIAGAPASADRHAGVKEALAEYPgIKVVGEVFGGWDEATAQTA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 216 LQEMLERHPEIDVVAGTAIAAE---AAMGEGRNLKTPLTV------VSFYLSHqVYRGLKRGRVIMAAsdqmvWQGELAV 286
Cdd:cd06300   176 MLDFLATHPQVDGVWTQGGEDTgvlQAFQQAGRPPVPIVGgdengfAKQWWKH-PKKGLTGAAVWPPP-----AIGAAGL 249
                         250       260       270
                  ....*....|....*....|....*....|
gi 1487551699 287 EQAIRQLQGQS-VSDNVSPPILVLTPKNAD 315
Cdd:cd06300   250 EVALRLLEGQGpKPQSVLLPPPLITNDDAK 279
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
52-229 1.77e-07

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: 51.75  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGysQLATQQAQIDQCKQWGAEAILLGSSTTSFPDLQKQVAS-LPVIEL 130
Cdd:cd06267     7 PDISNPFFAELLRGIEDAARERGYSLLLCNTDE--DPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAgIPVVLI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 131 VNAIDAPQVkSRVGVPWFQMGYQPGRYLVQwaHG-KplNVLLMPGPDNAGGSKEMVEGFRAAI--AGSPVRIVDIALGDN 207
Cdd:cd06267    85 DRRLDGLGV-DSVVVDNYAGAYLATEHLIE--LGhR--RIAFIGGPLDLSTSRERLEGYRDALaeAGLPVDPELVVEGDF 159
                         170       180
                  ....*....|....*....|..
gi 1487551699 208 DIEIQRNLLQEMLERHPEIDVV 229
Cdd:cd06267   160 SEESGYEAARELLALPPRPTAI 181
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
53-315 2.36e-07

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: 51.50  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  53 SLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGysQLATQQAQIDQCKQWGAEAILLgsSTTSFPDLQKQV-----ASLPV 127
Cdd:cd06313     8 GLSSEFITNLVEAMKAVAKELNVDLVVLDGNG--DVSTQINQVDTLIAQGVDAIIV--VPVDADALAPAVekakeAGIPL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 128 IELVNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPdnAGGSKEM--VEGFRAAIAGSP-VRIVDIAL 204
Cdd:cd06313    84 VGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKG-NVVILEGP--IGQSAQIdrGKGIENVLKKYPdIKVLAEQT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 205 GDNDIEIQRNLLQEMLERHP-EIDVVAGTAIAaeaaMGEG-------RNlKTPLTVVSFYLSHQVYRGLKRGRVIMAASD 276
Cdd:cd06313   161 ANWSRDEAMSLMENWLQAYGdEIDGIIAQNDD----MALGalqavkaAG-RDDIPVVGIDGIEDALQAVKSGELIATVLQ 235
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1487551699 277 QMVWQGELAVEQAIRQLQGQSVSDNVSPPILVLTPKNAD 315
Cdd:cd06313   236 DAEAQGKGAVEVAVDAVKGEGVEKKYYIPFVLVTKDNVD 274
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
52-310 3.90e-07

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: 50.52  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSqlATQQAQIDQCKQWGAEAILL---GSSTTSFPDLQKQVASLPVI 128
Cdd:cd19972     7 ANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDS--ATQVNQIQDLITQNIDALIYipaGATAAAVPVKAARAAGIPVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 129 EL-VNAIDAP--------QVKSrvgvpwfqmGYQPGRYLVQWAHGKPlNVLLMPGpdNAGGSKEM--VEGFRAAIAGSP- 196
Cdd:cd19972    85 AVdRNPEDAPgdtfiatdSVAA---------AKELGEWVIKQTGGKG-EIAILHG--QLGTTPEVdrTKGFQEALAEAPg 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 197 VRIVDIALGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEaaMGEGR-----NLKTPLTVVSFYLSHQVYRGLKRGRVI 271
Cdd:cd19972   153 IKVVAEQTADWDQDEGFKVAQDMLQANPNITVFFGQSDAMA--LGAAQavkvaGLDHKIWVVGFDGDVAGLKAVKDGVLD 230
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1487551699 272 MAASDQMVWQGELAVEQAIRQLQGQSVSDNVSPPILVLT 310
Cdd:cd19972   231 ATMTQQTQKMGRLAVDSAIDLLNGKAVPKEQLQDAVLTT 269
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
58-312 4.57e-07

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


Pssm-ID: 380541 [Multi-domain]  Cd Length: 282  Bit Score: 50.49  E-value: 4.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  58 YWLSLNYGMQEAARRYGVDLKVLEAGGysQLATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQK-QVASLPVIELVNAI 134
Cdd:cd06318    13 YYAALVAAAKAEAKKLGVELVVTDAQN--DLTKQISDVEDLITRGVDVLILNpvDPEGLTPAVKAaKAAGIPVITVDSAL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 135 D-APQVKSRVGVPWFQMGYQPGRYLVQWAHGKPLNVLLMPGpdNAGG--SKEMVEGFRAAIAGSPVR--------IVDIA 203
Cdd:cd06318    91 DpSANVATQVGRDNKQNGVLVGKEAAKALGGDPGKIIELSG--DKGNevSRDRRDGFLAGVNEYQLRkygksnikVVAQP 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 204 LGDNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMG---EGRNLKTPLTVVSFYLSHQVYRGLKRGRVIMAASDQMVW 280
Cdd:cd06318   169 YGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMkalKAAGMLDKVKVAGADGQKEALKLIKDGKYVATGLNDPDL 248
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1487551699 281 QGELAVEQAIRQLQGQSVSdnvspPILVLTPK 312
Cdd:cd06318   249 LGKTAVDTAAKVVKGEESF-----PEFTYTPT 275
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
62-229 1.47e-06

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: 48.90  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  62 LNYGMQEAARRY-GVDLKVLEAGGYSQlatQQAQIDQCKQWGAEAILLGS--STTSFPDLQKQV-ASLPVIELVNAIDAP 137
Cdd:cd06311    17 VAYYAEKQAKELaDLEYKLVTSSNANE---QVSQLEDLIAQKVDAIVILPqdSEELTVAAQKAKdAGIPVVNFDRGLNVL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 138 QVKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFRAAIAGSP-VRIVDIALGDNDIEIQRNLL 216
Cdd:cd06311    94 IYDLYVAGDNPGMGVVSAEYIGKKLGGKG-NVVVLEVPSSGSVNEERVAGFKEVIKGNPgIKILAMQAGDWTREDGLKVA 172
                         170
                  ....*....|...
gi 1487551699 217 QEMLERHPEIDVV 229
Cdd:cd06311   173 QDILTKNKKIDAV 185
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
52-222 2.24e-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: 48.38  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGYSqlATQQAQIDQCKQWGAEAILLGSSTTSFPDLQKQVAS-LPVIEL 130
Cdd:cd06285     7 SDLSNPFYAELVEGIEDAARERGYTVLLADTGDDP--ERELAALDSLLSRRVDGLIITPARDDAPDLQELAARgVPVVLV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 131 VNAIDAPQVKSrVGVPWFQMGYQPGRYLVQWAHGKPLNVllmPGPDNAGGSKEMVEGFRAAI--AGSPVRIVDIALGDND 208
Cdd:cd06285    85 DRRIGDTALPS-VTVDNELGGRLATRHLLELGHRRIAVV---AGPLNASTGRDRLRGYRRALaeAGLPVPDERIVPGGFT 160
                         170
                  ....*....|....
gi 1487551699 209 IEIQRNLLQEMLER 222
Cdd:cd06285   161 IEAGREAAYRLLSR 174
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
65-229 2.83e-06

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


Pssm-ID: 380489 [Multi-domain]  Cd Length: 269  Bit Score: 47.87  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  65 GMQEAARRYGVDLkVLEAGGYSQlATQQAQIDQCKQWGAEAILLgSSTTSFPDLQK--QVASLPVIELVNaIDAPQVKSR 142
Cdd:cd01575    20 GLSDVLEPAGYQL-LLGNTGYSP-EREEELIRALLSRRPAGLIL-TGTEHTPATRKllRAAGIPVVETWD-LPDDPIDMA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 143 VGVPWFQMGYQPGRYLVQWAHGKPlnVLLMPGPDNAGGSKEMVEGFRAAI--AGSPVRIVDIALGDNDIEIQRNLLQEML 220
Cdd:cd01575    96 VGFSNFAAGRAMARHLIERGYRRI--AFVGARLDGDSRARQRLEGFRDALaeAGLPLPLVLLVELPSSFALGREALAELL 173

                  ....*....
gi 1487551699 221 ERHPEIDVV 229
Cdd:cd01575   174 ARHPDLDAI 182
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
52-229 3.53e-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: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 47.65  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGvdLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLGSSTTSFPDLQKQVA-SLPVIeL 130
Cdd:cd06293     7 PDVSNPFFAEVARGVEDAARERG--YAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRArGTAVV-L 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 131 VNAIDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKplnVLLMPGPDNAGGSKEMVEGFRAAIAGSPV----RIVDIALGD 206
Cdd:cd06293    84 LDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRR---IAFVSGPLRTRQVAERLAGARAAVAEAGLdpdeVVRELSAPD 160
                         170       180
                  ....*....|....*....|...
gi 1487551699 207 NDIEIQRNLLQEMLERHPEIDVV 229
Cdd:cd06293   161 ANAELGRAAAAQLLAMPPRPTAV 183
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
52-289 5.09e-06

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: 47.27  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGVDLKVLeAGGYSQLATQQAQIDQCKQWGAEAILLG-SSTTSFPDLQKQV--ASLPVI 128
Cdd:cd19965     7 HVTTNPFFQPVKKGMDDACELLGAECQFT-GPQTFDVAEQVSLLEAAIASGPDGIATTiVDPEAFDEVIKRAldAGIPVV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 129 eLVNaIDAPQVKSR----VGVPWFQMGYQPGRYLVQWAHGKPLNVLLM---PGPDN----AGGSKEMVEGFraaiaGSPV 197
Cdd:cd19965    86 -AFN-VDAPGGENArlafVGQDLYPAGYVLGKRIAEKFKPGGGHVLLGistPGQSAleqrLDGIKQALKEY-----GRGI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 198 RIVDIALGdNDIEIQRNLLQEMLERHPEIDVVAGTAIAAEAAMGE---GRNLKTPLTVVSFYLSHQVYRGLKRGrVIMAA 274
Cdd:cd19965   159 TYDVIDTG-TDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQaikDLGLKGKVLVGGFDLVPEVLQGIKAG-YIDFT 236
                         250
                  ....*....|....*.
gi 1487551699 275 SDQMVW-QGELAVEQA 289
Cdd:cd19965   237 IDQQPYlQGFYPVMQL 252
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
75-313 8.19e-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: 46.90  E-value: 8.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  75 VDLKVLEAGGYSQlaTQQAQIDQCKQWGAEAILL-GSSTTSFPDLQKQV--ASLPVIELVNAIDAPQVKSrVGVPWFQMG 151
Cdd:cd19998    34 VELKVVSSGTDVQ--AQISAIDNMIAAGYDAILIyAISPTALNPVIKRAcdAGIVVVAFDNVVDEPCAYN-VNTDQAKAG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 152 YQPGRYLVQWAHGKPlNVLLMPGPDNAGGSKEMVEGFRAAIAGSP-VRIVDIALGDNDIEIQRNLLQEMLERHPEIDVVA 230
Cdd:cd19998   111 EQTAQWLVDKLGGKG-NILMVRGVPGTSVDRDRYEGAKEVFKKYPdIKVVAEYYGNWDDGTAQKAVADALAAHPDVDGVW 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 231 GTAIAAEAA-------------MGEGRNLktpltVVSFYLSHQVYrGLKrgrVIMAAsdQMVWQGELAVEQAIRQLQGQS 297
Cdd:cd19998   190 TQGGETGVIkalqaaghplvpvGGEAENG-----FRKAMLEPLAN-GLP---GISAG--SPPALSAVALKLAVAVLEGEK 258
                         250
                  ....*....|....*.
gi 1487551699 298 VSDNVSPPILVLTPKN 313
Cdd:cd19998   259 EPKTIELPLPWVTTDD 274
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
56-288 1.28e-05

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


Pssm-ID: 380621 [Multi-domain]  Cd Length: 278  Bit Score: 46.16  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  56 DSYWLSLNYGMQEAARRYGVDLKVLEAGGysqlaTQQAQIDQCKQWGAeAILLGSSTTSFPDL--------QKQVASLPV 127
Cdd:cd19966    12 DPFWTVVYNGAKDAAADLGVDLDYVFSSW-----DPEKMVEQFKEAIA-AKPDGIAIMGHPGDgaytplieAAKKAGIIV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 128 IELVNAIDAPQVKSR----VGVPWFQMGYQPGRYLVQWAHGKPLNVLLMPG--PDNAGGSKE---MVEGFRAaiAGSPVR 198
Cdd:cd19966    86 TSFNTDLPKLEYGDCglgyVGADLYAAGYTLAKELVKRGGLKTGDRVFVPGllPGQPYRVLRtkgVIDALKE--AGIKVD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 199 IVDIALGDNDIEIQRNLLQEMLERHPEIDVVagtaiaaeaaMGEGRNLKTPLT--------------VVSFYLSHQVYRG 264
Cdd:cd19966   164 YLEISLEPNKPAEGIPVMTGYLAANPDVKAI----------VGDGGGLTANVAkylkaagkkpgeipVAGFDLSPATVQA 233
                         250       260
                  ....*....|....*....|....
gi 1487551699 265 LKRGRVIMAASDQMVWQGELAVEQ 288
Cdd:cd19966   234 IKSGYVNATIDQQPYLQGYLPVLQ 257
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
126-311 3.52e-05

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: 44.86  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 126 PVIELVNaiDAPQVKSR--VGVPWFQMGYQPGRYLVQWAHGKPLNVLLMPGPDNAGGSKEMVEGFRAAIA--GSPVRIVD 201
Cdd:cd06307    85 PVVTLVS--DLPGSRRLayVGIDNRAAGRTAAWLMGRFLGRRPGKVLVILGSHRFRGHEEREAGFRSVLRerFPDLTVLE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 202 IALGDNDIEIQRNLLQEMLERHPEIDVVagtaiaaeAAMGEG----------RNLKTPLTVVSFYLSHQVYRGLKRGRVI 271
Cdd:cd06307   163 VLEGLDDDELAYELLRELLARHPDLVGI--------YNAGGGnegiaralreAGRARRVVFIGHELTPETRRLLRDGTID 234
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1487551699 272 MAASDQMVWQGELAVEQAIRQLQG-QSVSDNVSPPILVLTP 311
Cdd:cd06307   235 AVIDQDPELQARRAIEVLLAHLGGkGPAPPQPPIPIEIITR 275
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
58-227 3.75e-05

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


Pssm-ID: 380624 [Multi-domain]  Cd Length: 278  Bit Score: 44.64  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  58 YWLSLNYGMQEAARRYGVDLKVLEAGGYSqLATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQKQV-ASLPVIelVNAI 134
Cdd:cd19969    13 YWDDVKEGFEDAGAELGVKTEYTGPATAD-VNEQITAIEQAIAKNPDGIAVSaiDPEALTPTINKAVdAGIPVV--TFDS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 135 DAPQVK--SRVGVPWFQMGYQPGRYLVQWAHGK-PLNVLLMPGPDNaggSKEMVEGFRAAIAGSP-VRIVDIALGDNDIE 210
Cdd:cd19969    90 DAPESKriSYVGTDNYEAGYAAAEKLAELLGGKgKVAVLTGPGQPN---HEERVEGFKEAFAEYPgIEVVAVGDDNDDPE 166
                         170
                  ....*....|....*..
gi 1487551699 211 IQRNLLQEMLERHPEID 227
Cdd:cd19969   167 KAAQNTSALLQAHPDLV 183
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
53-305 1.18e-04

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: 42.99  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  53 SLKDSYWLSLNYGMQEAARRY-GVDLKVLEAGgySQLATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQKQVAS-LPVI 128
Cdd:cd06301     9 NFSDEFLTYLRDAIEAYAKEYpGVKLVIVDAQ--SDAAKQLSQVENFIAQGVDAIIVNpvDTDASAPAVDAAADAgIPLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 129 ElVNA--IDAPQVKSRVGVPWFQMGYQPGRYLVQWAHGKPlNVLLMPGPdnAGGSKEMV--EGFRAAIAGSP-VRIVDIA 203
Cdd:cd06301    87 Y-VNRepDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKG-NIAILDGV--LGHEAQILrtEGNKDVLAKYPgMKIVAEQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 204 LGDND----IEIQRNLLQEmlerHPEIDVVAGTAIAAEaaMG-----EGRNLKTPLTVVSFYLSHQVYRGLKRGRVimaa 274
Cdd:cd06301   163 TANWSrekaMDIVENWLQS----GDKIDAIVANNDEMA--IGailalEAAGKKDDILVAGIDATPDALKAMKAGRL---- 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1487551699 275 sDQMVWQ-----GELAVEQAIRQLQGQSVSDNVSPP 305
Cdd:cd06301   233 -DATVFQdaagqGETAVDVAVKAAKGEEVESDIWIP 267
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
52-297 8.18e-04

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: 40.38  E-value: 8.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  52 PSLKDSYWLSLNYGMQEAARRYGVDLKVLEAGGysQLATQQAQIDQCKQWGAEAILL--GSSTTSFPDLQKQV-ASLPVI 128
Cdd:cd19967     7 STPNNPFFVVEAEGAKEKAKELGYEVTVFDHQN--DTAKEAELFDTAIASGAKAIILdpADADASIAAVKKAKdAGIPVF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 129 ---ELVNAIDApqVKSRVGVPWFQMGYQPGRYLVQWAHGKPLNVLLMpGPDNAGGSKEMVEGFRAAIAGSP--VRIV-DI 202
Cdd:cd19967    85 lidREINAEGV--AVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELL-GKESDTNAQLRSQGFHSVIDQYPelKMVAqQS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 203 ALGDNDIEIqrNLLQEMLERHPEIDVVagTAIAAEAAMG-----EGRNLKTPLTVVSFYLSHQVYRGLKRGRVIMAASDQ 277
Cdd:cd19967   162 ADWDRTEAF--EKMESILQANPDIKGV--ICGNDEMALGaiaalKAAGRAGDVIIVGFDGSNDVRDAIKEGKISATVLQP 237
                         250       260
                  ....*....|....*....|
gi 1487551699 278 MVWQGELAVEQAIRQLQGQS 297
Cdd:cd19967   238 AKLIARLAVEQADQYLKGGS 257
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
58-302 8.32e-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: 40.69  E-value: 8.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  58 YWLSLNYGMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLG--SSTTSFPDLQK-QVASLPVIELVNAI 134
Cdd:cd20005    13 FWKAVKKGAEQAAKELGVKITFEGPDTESDVDKQIEMLDNAIAKKPDAIALAalDTNALLPQLEKaKEKGIPVVTFDSGV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 135 DAPQVKSRVGVPWFQMGYQPGRYLVQwAHGKPLNVLLMPGPDNAGGSKEMVEGFRAAIAGSP--VRIVDIALGDNDIEIQ 212
Cdd:cd20005    93 PSDLPLATVATDNYAAGALAADHLAE-LIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYpdIKVVNVQYGVGDHAKA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 213 RNLLQEMLERHPEI-------DVVAGTAIAAEAAMGEGRNLKtpltVVSFYLSHQVYRGLKRGRviMAASdqmVWQ---- 281
Cdd:cd20005   172 ADIAKAILQANPDLkgiyatnEGAAIGVANALKEMGKLGKIK----VVGFDSGEAQIDAIKNGV--IAGS---VTQnpyg 242
                         250       260
                  ....*....|....*....|..
gi 1487551699 282 -GELAVEQAIRQLQGQSVSDNV 302
Cdd:cd20005   243 mGYKTVKAAVKALKGEEVEKLI 264
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
65-229 9.86e-04

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


Pssm-ID: 380628 [Multi-domain]  Cd Length: 285  Bit Score: 40.53  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  65 GMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILLG-SSTTSFPDLQKQVASLPVieLVNAIDAPQVKSRV 143
Cdd:cd19973    20 GAQKAAKALGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITpSDTKAIVPAVKKARDAGV--LVIALDTPTDPIDA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 144 GVPWFQM-GYQPGRYLVQWAH----GKP-----LNVLLMPGPDnAGGSKEMVEGFRAAIA-------GSPVRIVDIALGD 206
Cdd:cd19973    98 ADATFATdNFKAGVLIGEWAKaalgAKDakiatLDLTPGHTVG-VLRHQGFLKGFGIDEKdpesnedEDDSQVVGSADTN 176
                         170       180
                  ....*....|....*....|...
gi 1487551699 207 NDIEIQRNLLQEMLERHPEIDVV 229
Cdd:cd19973   177 GDQAKGQTAMENLLQKDPDINLV 199
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
65-229 1.43e-03

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: 39.86  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  65 GMQEAARRYGvdLKVLEAGGYSQLATQQAQIDQCKQWGAEAILL----GSSTTSFPDLQKqvASLPVIELVNAIDAPQVk 140
Cdd:cd06289    20 GIEEALEEAG--YLVFLANTGEDPERQRRFLRRMLEQGVDGLILspaaGTTAELLRRLKA--WGIPVVLALRDVPGSDL- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699 141 SRVGVPWFQMGYQPGRYLVQWAHGKplnVLLMPGPDNAGGSKEMVEGFRAAIAGSPVRI--VDIALGDNDIEIQRNLLQE 218
Cdd:cd06289    95 DYVGIDNRLGAQLATEHLIALGHRR---IAFLGGLSDSSTRRERLAGFRAALAEAGLPLdeSLIVPGPATREAGAEAARE 171
                         170
                  ....*....|.
gi 1487551699 219 MLERHPEIDVV 229
Cdd:cd06289   172 LLDAAPPPTAV 182
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
65-165 1.91e-03

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: 39.59  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  65 GMQEAARRYGVDLKVLEAGGysQLATQQAQIDQCKQWGAEAIL--LGSSTTSFPDLQKQV-ASLPVIELVNAIDAPQVKS 141
Cdd:cd06305    20 GAVAEAEKLGGTVIVFDANG--DDARMADQIQQAITQKVDAIIisHGDADALDPKLKKALdAGIPVVTFDTDSQVPGVNN 97
                          90       100
                  ....*....|....*....|....
gi 1487551699 142 rVGVPWFQMGYQPGRYLVQWAHGK 165
Cdd:cd06305    98 -ITQDDYALGTLSLGQLVKDLNGE 120
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
65-187 7.99e-03

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


Pssm-ID: 380650 [Multi-domain]  Cd Length: 294  Bit Score: 37.65  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551699  65 GMQEAARRYGVDLKVLEAGGYSQLATQQAQIDQCKQWGAEAILL----GSSTTSFPDLQKQvASLPVIELVNAIDAPQVK 140
Cdd:cd19995    21 GFEKAMKKLCPDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVdpvdSNAAAGIVAKAAQ-AGVPVIAYDRLILGGPAD 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1487551699 141 SRVGVPWFQMGYQPGRYLVQ---WAHGKPLNVLLMPG--PDNAGGskEMVEG 187
Cdd:cd19995   100 YYVSFDNVAVGEAQAQSLVDhlkAIGKKGVNIVMINGspTDNNAG--LFKKG 149
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH