NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1654132688|gb|QCR47367|]
View 

sugar ABC transporter substrate-binding protein [Streptomyces sp. SGAir0924]

Protein Classification

sugar-binding protein( domain architecture ID 14448371)

sugar-binding protein is a type 1 periplasmic binding protein, similar to Agrobacterium fabrum multiple sugar-binding periplasmic receptor ChvE that binds diverse plant sugars as virulence signals

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ChvE super family cl46169
sugar ABC transporter substrate-binding protein;
44-363 0e+00

sugar ABC transporter substrate-binding protein;


The actual alignment was detected with superfamily member NF040907:

Pssm-ID: 468842  Cd Length: 319  Bit Score: 629.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  44 IGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADI 123
Cdd:NF040907    1 VGIAMPTKSSERWIADGNNMVKQLEAAGYKTDLQYAEDDVPTQVSQIENMITKGAKVLVIAAIDGTALTDVLQQAADAGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 124 PVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLGLKAGKkGPFNIELFAGSNDDNNTKYFFNGAMNVLKPYMDKG 203
Cdd:NF040907   81 PVIAYDRLIRGSENVDYYATFDNFKVGVLQGTYIVDGLGLKDGK-GPFNIELFAGSPDDNNAYFFFDGAMSVLQPYIDSG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 204 QLVVRSKQTALNQVTTLRWDGGTAQKRMDDLLTSSYRSARVDAVLSPYDGISIGILSALKSDGYGSGSKPMPVVTGQDAE 283
Cdd:NF040907  160 KLVVRSGQTDFDQVATLRWDGATAQARMDNLLSAFYTDKKVDAVLSPYDGISIGIISALKGVGYGSGDKPLPVVTGQDAE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 284 VASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTKSYDNGAKVVPAYLLQPVSVDKDNYKKVLVDGGYY 363
Cdd:NF040907  240 VASVKSIIAGEQTSTIFKDTRELAKVTVKMVDAVLKGEEPEVNDTKTYDNGVKVVPSYLLEPVSVDKDNYKEVLVDSGYY 319
 
Name Accession Description Interval E-value
ChvE NF040907
sugar ABC transporter substrate-binding protein;
44-363 0e+00

sugar ABC transporter substrate-binding protein;


Pssm-ID: 468842  Cd Length: 319  Bit Score: 629.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  44 IGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADI 123
Cdd:NF040907    1 VGIAMPTKSSERWIADGNNMVKQLEAAGYKTDLQYAEDDVPTQVSQIENMITKGAKVLVIAAIDGTALTDVLQQAADAGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 124 PVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLGLKAGKkGPFNIELFAGSNDDNNTKYFFNGAMNVLKPYMDKG 203
Cdd:NF040907   81 PVIAYDRLIRGSENVDYYATFDNFKVGVLQGTYIVDGLGLKDGK-GPFNIELFAGSPDDNNAYFFFDGAMSVLQPYIDSG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 204 QLVVRSKQTALNQVTTLRWDGGTAQKRMDDLLTSSYRSARVDAVLSPYDGISIGILSALKSDGYGSGSKPMPVVTGQDAE 283
Cdd:NF040907  160 KLVVRSGQTDFDQVATLRWDGATAQARMDNLLSAFYTDKKVDAVLSPYDGISIGIISALKGVGYGSGDKPLPVVTGQDAE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 284 VASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTKSYDNGAKVVPAYLLQPVSVDKDNYKKVLVDGGYY 363
Cdd:NF040907  240 VASVKSIIAGEQTSTIFKDTRELAKVTVKMVDAVLKGEEPEVNDTKTYDNGVKVVPSYLLEPVSVDKDNYKEVLVDSGYY 319
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
40-368 1.35e-169

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 475.01  E-value: 1.35e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  40 EGATIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAK 119
Cdd:COG4213     1 GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 120 DADIPVVSYDRLILGSeNVDYYASFDNEKVGELQGSYIVDKLGLKAGKkgpfNIELFAGSNDDNNTKYFFNGAMNVLKPY 199
Cdd:COG4213    81 AAGIPVIAYDRLILNS-DVDYYVSFDNVKVGELQGQYLVDGLPLKGKG----NIELFGGSPTDNNATLFFEGAMSVLQPY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 200 MDKGQLVVRSKQtalnqvTTLRWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYGsgskPMPVVTG 279
Cdd:COG4213   156 IDSGKLVVVSGQ------WTLGWDPETAQKRMENLLTAN--GNKVDAVLAPNDGLAGGIIQALKAQGLA----GKVVVTG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 280 QDAEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTksYDNGAKVVPAYLLQPVSVDKDNYKKVLVD 359
Cdd:COG4213   224 QDAELAAVQRILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPEVNGT--YDNGKKDVPSYLLEPVAVTKDNVKETLID 301

                  ....*....
gi 1654132688 360 GGYYTENDL 368
Cdd:COG4213   302 SGYYTAEQV 310
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
43-348 7.96e-159

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


Pssm-ID: 380649 [Multi-domain]  Cd Length: 304  Bit Score: 447.46  E-value: 7.96e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd19994     1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLGLKAGkKGPFNIELFAGSNDDNNTKYFFNGAMNVLKPYMDK 202
Cdd:cd19994    81 IPVIAYDRLIMNTDAVDYYVTFDNEKVGELQGQYLVDKLGLKDG-KGPFNIELFAGSPDDNNAQLFFKGAMEVLQPYIDD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 GQLVVRSKQTALNQVTTLRWDGGTAQKRMDDLLTSSYR-SARVDAVLSPYDGISIGILSALKSDGYGSGskPMPVVTGQD 281
Cdd:cd19994   160 GTLVVRSGQTTFEQVATPDWDTETAQARMETLLSAYYTgGKKLDAVLSPNDGIARGVIEALKAAGYDTG--PWPVVTGQD 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654132688 282 AEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTKSYDNGAKVVPAYLLQPVSV 348
Cdd:cd19994   238 AEDASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVEVNDTKTYDNGVKVVPSYLLDPVIV 304
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
37-368 3.42e-64

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 207.29  E-value: 3.42e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  37 GGAEGATIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQ 116
Cdd:PRK10355   21 AHAKEVKIGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 117 QAKDADIPVVSYDRLIlGSENVDYYASFDNEKVGELQGSYIVDklglkagKKGPFNIELFAGSNDDNNTKYFFNGAMNVL 196
Cdd:PRK10355  101 EAKQEGIKVLAYDRMI-NNADIDFYISFDNEKVGELQAKALVD-------KVPQGNYFLMGGSPVDNNAKLFRAGQMKVL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 197 KPYMDKGQLVVRSKQTALNqvttlrWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYgSGSKpmpV 276
Cdd:PRK10355  173 KPYIDSGKIKVVGDQWVDG------WLPENALKIMENALTAN--NNKIDAVVASNDATAGGAIQALSAQGL-SGKV---A 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 277 VTGQDAEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTksYDNGAKVVPAYLLQPVSVDKDNYKKV 356
Cdd:PRK10355  241 ISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKANTT--LNNGLKDVPSRLLTPIDVNKNNIDST 318
                         330
                  ....*....|..
gi 1654132688 357 LVDGGYYTENDL 368
Cdd:PRK10355  319 VIKDGFHKKSEL 330
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
44-322 3.47e-61

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: 197.15  E-value: 3.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  44 IGIAMPTKSSERWIADGANVEKELKAKGYETKLV-YGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVgPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILgSENVDYYASFDNEKVGELQGSYIVDKLGlkagkkGPFNIELFAGSNDDNNTKYFFNGAMNVLKPYMDK 202
Cdd:pfam13407  81 IPVVTFDSDAP-SSPRLAYVGFDNEAAGEAAGELLAEALG------GKGKVAILSGSPGDPNANERIDGFKKVLKEKYPG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 GQLVvrskqtalNQVTTLRWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYgsgsKPMPVVTGQDA 282
Cdd:pfam13407 154 IKVV--------AEVEGTNWDPEKAQQQMEALLTAY--PNPLDGIISPNDGMAGGAAQALEAAGL----AGKVVVTGFDA 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1654132688 283 EVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKK 322
Cdd:pfam13407 220 TPEALEAIKDGTIDATVLQDPYGQGYAAVELAAALLKGKK 259
 
Name Accession Description Interval E-value
ChvE NF040907
sugar ABC transporter substrate-binding protein;
44-363 0e+00

sugar ABC transporter substrate-binding protein;


Pssm-ID: 468842  Cd Length: 319  Bit Score: 629.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  44 IGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADI 123
Cdd:NF040907    1 VGIAMPTKSSERWIADGNNMVKQLEAAGYKTDLQYAEDDVPTQVSQIENMITKGAKVLVIAAIDGTALTDVLQQAADAGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 124 PVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLGLKAGKkGPFNIELFAGSNDDNNTKYFFNGAMNVLKPYMDKG 203
Cdd:NF040907   81 PVIAYDRLIRGSENVDYYATFDNFKVGVLQGTYIVDGLGLKDGK-GPFNIELFAGSPDDNNAYFFFDGAMSVLQPYIDSG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 204 QLVVRSKQTALNQVTTLRWDGGTAQKRMDDLLTSSYRSARVDAVLSPYDGISIGILSALKSDGYGSGSKPMPVVTGQDAE 283
Cdd:NF040907  160 KLVVRSGQTDFDQVATLRWDGATAQARMDNLLSAFYTDKKVDAVLSPYDGISIGIISALKGVGYGSGDKPLPVVTGQDAE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 284 VASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTKSYDNGAKVVPAYLLQPVSVDKDNYKKVLVDGGYY 363
Cdd:NF040907  240 VASVKSIIAGEQTSTIFKDTRELAKVTVKMVDAVLKGEEPEVNDTKTYDNGVKVVPSYLLEPVSVDKDNYKEVLVDSGYY 319
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
40-368 1.35e-169

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 475.01  E-value: 1.35e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  40 EGATIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAK 119
Cdd:COG4213     1 GKIKIGVSLPTKTSERWIRDGDNFKAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 120 DADIPVVSYDRLILGSeNVDYYASFDNEKVGELQGSYIVDKLGLKAGKkgpfNIELFAGSNDDNNTKYFFNGAMNVLKPY 199
Cdd:COG4213    81 AAGIPVIAYDRLILNS-DVDYYVSFDNVKVGELQGQYLVDGLPLKGKG----NIELFGGSPTDNNATLFFEGAMSVLQPY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 200 MDKGQLVVRSKQtalnqvTTLRWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYGsgskPMPVVTG 279
Cdd:COG4213   156 IDSGKLVVVSGQ------WTLGWDPETAQKRMENLLTAN--GNKVDAVLAPNDGLAGGIIQALKAQGLA----GKVVVTG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 280 QDAEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTksYDNGAKVVPAYLLQPVSVDKDNYKKVLVD 359
Cdd:COG4213   224 QDAELAAVQRILAGTQYMTVYKDTRELAEAAAELAVALAKGEKPEVNGT--YDNGKKDVPSYLLEPVAVTKDNVKETLID 301

                  ....*....
gi 1654132688 360 GGYYTENDL 368
Cdd:COG4213   302 SGYYTAEQV 310
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
43-348 7.96e-159

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


Pssm-ID: 380649 [Multi-domain]  Cd Length: 304  Bit Score: 447.46  E-value: 7.96e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd19994     1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLGLKAGkKGPFNIELFAGSNDDNNTKYFFNGAMNVLKPYMDK 202
Cdd:cd19994    81 IPVIAYDRLIMNTDAVDYYVTFDNEKVGELQGQYLVDKLGLKDG-KGPFNIELFAGSPDDNNAQLFFKGAMEVLQPYIDD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 GQLVVRSKQTALNQVTTLRWDGGTAQKRMDDLLTSSYR-SARVDAVLSPYDGISIGILSALKSDGYGSGskPMPVVTGQD 281
Cdd:cd19994   160 GTLVVRSGQTTFEQVATPDWDTETAQARMETLLSAYYTgGKKLDAVLSPNDGIARGVIEALKAAGYDTG--PWPVVTGQD 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654132688 282 AEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTKSYDNGAKVVPAYLLQPVSV 348
Cdd:cd19994   238 AEDASVKSILDGEQSMTVFKDTRLLAKATVELVDALLEGEEVEVNDTKTYDNGVKVVPSYLLDPVIV 304
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
43-346 1.72e-103

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


Pssm-ID: 380480 [Multi-domain]  Cd Length: 283  Bit Score: 306.27  E-value: 1.72e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd01538     1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSEnVDYYASFDNEKVGELQGSYIVDklglkagKKGPFNIELFAGSNDDNNTKYFFNGAMNVLKPYMDK 202
Cdd:cd01538    81 IKVIAYDRLILNAD-VDYYISFDNEKVGELQAQALLD-------AKPEGNYVLIGGSPTDNNAKLFRDGQMKVLQPAIDS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 GQLVVRSKQtalnqvTTLRWDGGTAQKRMDDLLTSSYrsARVDAVLSPYDGISIGILSALKSDGYGSGskpmPVVTGQDA 282
Cdd:cd01538   153 GKIKVVGDQ------WVDDWLPANAQQIMENALTANG--NNVDAVVASNDGTAGGAIAALKAQGLSGG----VPVSGQDA 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654132688 283 EVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTksYDNGAKVVPAYLLQPV 346
Cdd:cd01538   221 DLAAIKRILAGTQTMTVYKDIRLLADAAAEVAVALMRGEKPPINGT--TNNGLKDVPSYLLEPV 282
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
44-346 2.73e-78

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


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 242.10  E-value: 2.73e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  44 IGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADI 123
Cdd:cd19992     2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 124 PVVSYDRLILGSeNVDYYASFDNEKVGELQGSYIVdklglKAGKKGpfNIELFAGSNDDNNTKYFFNGAMNVLKPYMDKG 203
Cdd:cd19992    82 PVISYDRLILNA-DVDLYVGRDNYKVGQLQAEYAL-----EAVPKG--NYVILSGDPGDNNAQLITAGAMDVLQPAIDSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 204 QLVVRSKQTALNqvttlrWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKsdGYGSGSKpmPVVTGQDAE 283
Cdd:cd19992   154 DIKIVLDQYVKG------WSPDEAMKLVENALTAN--NNNIDAVLAPNDGMAGGAIQALK--AQGLAGK--VFVTGQDAE 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654132688 284 VASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTkSYDNGAKVVPAYLLQPV 346
Cdd:cd19992   222 LAALKRIVEGTQTMTVWKDLKELARAAADAAVKLAKGEKPQTTDE-TINNGGKDVPAILIPGV 283
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
43-348 1.29e-77

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


Pssm-ID: 380646 [Multi-domain]  Cd Length: 284  Bit Score: 240.22  E-value: 1.29e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd19991     1 KIGFSMDSLRVERWQRDRDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSeNVDYYASFDNEKVGELQGSYIVdklglKAGKKGpfNIELFAGSNDDNNTKYFFNGAMNVLKPYMDK 202
Cdd:cd19991    81 VPVLAYDRLILNA-DVDLYVSFDNEKVGELQAEALV-----KAKPKG--NYVLLGGSPTDNNAKLFREGQMKVLQPLIDS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 GQLVVRSKQTALNqvttlrWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYGSGSkpmpVVTGQDA 282
Cdd:cd19991   153 GDIKVVGDQWVDD------WDPEEALKIMENALTAN--NNKIDAVIASNDGTAGGAIQALAEQGLAGKV----AVSGQDA 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654132688 283 EVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNdtKSYDNGAKVVPAYLLQPVSV 348
Cdd:cd19991   221 DLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKNEAN--RTINNGKKEVPSILLDPIAV 284
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
43-347 7.23e-73

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: 228.33  E-value: 7.23e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIA-DGANVEKELKAKGYETKLVY--GEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAK 119
Cdd:cd19995     1 KVAFLLPDTTSARWEQqDAPGFEKAMKKLCPDCKVIYqnANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 120 DADIPVVSYDRLILGsENVDYYASFDNEKVGELQGSYIVDKlgLKAGKKGPFNIELFAGSNDDNNTKYFFNGAMNVLKPY 199
Cdd:cd19995    81 QAGVPVIAYDRLILG-GPADYYVSFDNVAVGEAQAQSLVDH--LKAIGKKGVNIVMINGSPTDNNAGLFKKGAHEVLDPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 200 MDKGQLVVrskqtaLNQVTTLRWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYgsgsKPMPVVTG 279
Cdd:cd19995   158 GDSGELKL------VCEYDTPDWDPANAQTAMEQALTKL--GNNIDGVLSANDGLAGGAIAALKAQGL----AGKVPVTG 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654132688 280 QDAEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVN-DTKSYDNGAKVVPAYLLQPVS 347
Cdd:cd19995   226 QDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGETPPSDlVTGTVTNGGDKVPAVLLPPVV 294
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
37-368 3.42e-64

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 207.29  E-value: 3.42e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  37 GGAEGATIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQ 116
Cdd:PRK10355   21 AHAKEVKIGMAIDDLRLERWQKDRDIFVKKAESLGAKVFVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 117 QAKDADIPVVSYDRLIlGSENVDYYASFDNEKVGELQGSYIVDklglkagKKGPFNIELFAGSNDDNNTKYFFNGAMNVL 196
Cdd:PRK10355  101 EAKQEGIKVLAYDRMI-NNADIDFYISFDNEKVGELQAKALVD-------KVPQGNYFLMGGSPVDNNAKLFRAGQMKVL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 197 KPYMDKGQLVVRSKQTALNqvttlrWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYgSGSKpmpV 276
Cdd:PRK10355  173 KPYIDSGKIKVVGDQWVDG------WLPENALKIMENALTAN--NNKIDAVVASNDATAGGAIQALSAQGL-SGKV---A 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 277 VTGQDAEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTksYDNGAKVVPAYLLQPVSVDKDNYKKV 356
Cdd:PRK10355  241 ISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVELGNGEEPKANTT--LNNGLKDVPSRLLTPIDVNKNNIDST 318
                         330
                  ....*....|..
gi 1654132688 357 LVDGGYYTENDL 368
Cdd:PRK10355  319 VIKDGFHKKSEL 330
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
44-322 3.47e-61

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: 197.15  E-value: 3.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  44 IGIAMPTKSSERWIADGANVEKELKAKGYETKLV-YGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVgPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILgSENVDYYASFDNEKVGELQGSYIVDKLGlkagkkGPFNIELFAGSNDDNNTKYFFNGAMNVLKPYMDK 202
Cdd:pfam13407  81 IPVVTFDSDAP-SSPRLAYVGFDNEAAGEAAGELLAEALG------GKGKVAILSGSPGDPNANERIDGFKKVLKEKYPG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 GQLVvrskqtalNQVTTLRWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYgsgsKPMPVVTGQDA 282
Cdd:pfam13407 154 IKVV--------AEVEGTNWDPEKAQQQMEALLTAY--PNPLDGIISPNDGMAGGAAQALEAAGL----AGKVVVTGFDA 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1654132688 283 EVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKK 322
Cdd:pfam13407 220 TPEALEAIKDGTIDATVLQDPYGQGYAAVELAAALLKGKK 259
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
43-346 3.98e-58

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


Pssm-ID: 380648 [Multi-domain]  Cd Length: 287  Bit Score: 190.38  E-value: 3.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd19993     1 VVGVSWSNFQEERWKTDEAAMKKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLIlgsENVD-YYASFDNEKVGELQGSYIvdklgLKAGKKGpfNIELFAGSNDDNNTKYFFNGAMNVLKPYMD 201
Cdd:cd19993    81 IPVIAYDRLI---ENPIaFYISFDNVEVGRMQARGV-----LKAKPEG--NYVFIKGSPTDPNADFLRAGQMEVLQPAID 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 202 KGQLVVRSKQTALNqvttlrWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYgSGSKPmpvVTGQD 281
Cdd:cd19993   151 SGKIKIVGEQYTDG------WKPANAQKNMEQILTAN--NNKVDAVVASNDGTAGGAVAALAAQGL-AGKVP---VSGQD 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654132688 282 AEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPE--VNDTKSYDNGAKV-VPAYLLQPV 346
Cdd:cd19993   219 ADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKGTKIEaiKGAALTNDGPKKVaVPSIFLKPI 286
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
43-324 7.79e-47

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: 160.42  E-value: 7.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd01536     1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLglkaGKKGpfNIELFAGSNDDNNTKYFFNGAMNVLKpymDK 202
Cdd:cd01536    81 IPVVAVDTDIDGGGDVVAFVGTDNYEAGKLAGEYLAEAL----GGKG--KVAILEGPPGSSTAIDRTKGFKEALK---KY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 GQLVVRSKQTAlnqvttlRWDGGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKSDGYgsgSKPMPVVtGQDA 282
Cdd:cd01536   152 PDIEIVAEQPA-------NWDRAKALTVTENLLQ---ANPDIDAVFAANDDMALGAAEALKAAGR---TGDIKIV-GVDG 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1654132688 283 EVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPE 324
Cdd:cd01536   218 TPEALKAIKDGELDATVAQDPYLQGYLAVEAAVKLLNGEKVP 259
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
20-352 1.03e-44

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


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 155.85  E-value: 1.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  20 TLTACGQNSEGGSeedKGGAEGATIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVD 99
Cdd:COG1879    15 ALAACGSAAAEAA---AAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 100 ALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLILGSeNVDYYASFDNEKVGELQGSYIVDKLglkaGKKGpfNIELFAGS 179
Cdd:COG1879    92 AIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGS-DRVAYVGSDNYAAGRLAAEYLAKAL----GGKG--KVAILTGS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 180 NDDNNTKYFFNGAMNVLKPYmdkGQLVVRSKQTAlnqvttlRWDGGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGIL 259
Cdd:COG1879   165 PGAPAANERTDGFKEALKEY---PGIKVVAEQYA-------DWDREKALEVMEDLLQ---AHPDIDGIFAANDGMALGAA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 260 SALKSdgygSGSKPMPVVTGQDAEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEvndtksydngakvvP 339
Cdd:COG1879   232 QALKA----AGRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVP--------------K 293
                         330
                  ....*....|...
gi 1654132688 340 AYLLQPVSVDKDN 352
Cdd:COG1879   294 EILTPPVLVTKEN 306
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
43-332 6.60e-32

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: 121.56  E-value: 6.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd06309     1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGsENVDYYASF---DNEKVGELQGSYIVDKLGLKAGKKgpfnIELF--AGSNDDNNTKyffNGAMNVLK 197
Cdd:cd06309    81 IPVILVDRTIDG-EDGSLYVTFigsDFVEEGRRAAEWLVKNYKGGKGNV----VELQgtAGSSVAIDRS---KGFREVIK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 198 PYMDkgqLVVRSKQTALnqvttlrWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYGSGSKpmPVV 277
Cdd:cd06309   153 KHPN---IKIVASQSGN-------FTREKGQKVMENLLQAG--PGDIDVIYAHNDDMALGAIQALKEAGLKPGKD--VLV 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1654132688 278 TGQDAEVASVKSIISGQQTQTVYKDLReLAKVASNMVDAVLNDKKPE---VNDTKSYD 332
Cdd:cd06309   219 VGIDGQKDALEAIKAGELNATVECNPL-FGPTAFDTIAKLLAGEKVPkliIVEERLFD 275
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
62-341 1.01e-27

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


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 110.37  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  62 NVEKELKA-KGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDR-----LILGS 135
Cdd:cd01539    21 ALEKAAKAgGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVIFFNRepsreDLKSY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 136 ENVdYYASFDNEKVGELQGSYIVDKLglkagkKGPFNIELfagsNDDNNTKY-FFNGAMN----------VLKPYMDKG- 203
Cdd:cd01539   101 DKA-YYVGTDAEESGIMQGEIIADYW------KANPEIDK----NGDGKIQYvMLKGEPGhqdaiartkySVKTLNDAGi 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 204 QLVVRSKQTALnqvttlrWDGGTAQKRMDDLLtSSYrSARVDAVLSPYDGISIGILSALKSDGY--GSGSKPMPVVtGQD 281
Cdd:cd01539   170 KTEQLAEDTAN-------WDRAQAKDKMDAWL-SKY-GDKIELVIANNDDMALGAIEALKAAGYntGDGDKYIPVF-GVD 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 282 AEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEVNDTKSYDNGAKVVPAY 341
Cdd:cd01539   240 ATPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLETGYKFLVEGKYVRIPY 299
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
43-324 2.20e-27

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: 108.79  E-value: 2.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKaKGYETKLVY--GEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKD 120
Cdd:cd06308     1 VIGFSQCSLNDPWRAAMNEEIKAEAA-KYPNVELIVtdAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 121 ADIPVVSYDRLIlgseNVDYYASF---DNEKVGELQGSYIVDKLglkaGKKGpfNIELFAGSNDDNNTKYFFNGAMNVLK 197
Cdd:cd06308    80 AGIPVIVLDRKV----SGDDYTAFigaDNVEIGRQAGEYIAELL----NGKG--NVVEIQGLPGSSPAIDRHKGFLEAIA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 198 PYMDkgqLVVRSKQTAlnqvttlRWDGGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKSdgygSGSKPMPVV 277
Cdd:cd06308   150 KYPG---IKIVASQDG-------DWLRDKAIKVMEDLLQ---AHPDIDAVYAHNDEMALGAYQALKK----AGREKEIKI 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1654132688 278 TGQDAE-VASVKSIISGQQTQTVYKDLRelAKVASNMVDAVLNDKKPE 324
Cdd:cd06308   213 IGVDGLpEAGEKAVKDGILAATFLYPTG--GKEAIEAALKILNGEKVP 258
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
43-302 8.41e-27

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: 107.32  E-value: 8.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSE--RWIADGanVEKELKAK-GYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAK 119
Cdd:cd06301     2 KIGVSMQNFSDEflTYLRDA--IEAYAKEYpGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 120 DADIPVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLGLKAgkkgpfNIELFAGSNDDNNTKYFFNGAMNVLKPY 199
Cdd:cd06301    80 DAGIPLVYVNREPDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKG------NIAILDGVLGHEAQILRTEGNKDVLAKY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 200 mDKGQLVVrsKQTAlnqvttlRWDGGTAQKRMDDLLTSsyrSARVDAVLSPYDGISIGILSALKSdgygSGSKPMPVVTG 279
Cdd:cd06301   154 -PGMKIVA--EQTA-------NWSREKAMDIVENWLQS---GDKIDAIVANNDEMAIGAILALEA----AGKKDDILVAG 216
                         250       260
                  ....*....|....*....|...
gi 1654132688 280 QDAEVASVKSIISGQQTQTVYKD 302
Cdd:cd06301   217 IDATPDALKAMKAGRLDATVFQD 239
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
43-325 3.26e-26

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: 105.82  E-value: 3.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSErWIADGAN-VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDA 121
Cdd:cd06313     1 KIGFTVYGLSSE-FITNLVEaMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 122 DIPVVSYDRLIlGSENVDYYASFDNEKVGELQGSYIVDKLGlkaGKKGPFNIELFAG-SNDDNNTKyffnGAMNVLKPYM 200
Cdd:cd06313    80 GIPLVGVNALI-ENEDLTAYVGSDDVVAGELEGQAVADRLG---GKGNVVILEGPIGqSAQIDRGK----GIENVLKKYP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 201 DkgqLVVRSKQTAlnqvttlRWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGygsgsKPMPVVTGQ 280
Cdd:cd06313   152 D---IKVLAEQTA-------NWSRDEAMSLMENWLQAY--GDEIDGIIAQNDDMALGALQAVKAAG-----RDDIPVVGI 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1654132688 281 DAEVASVKSIISGQQTQTVYKD----LRELAKVASNMVDAVLNDKKPEV 325
Cdd:cd06313   215 DGIEDALQAVKSGELIATVLQDaeaqGKGAVEVAVDAVKGEGVEKKYYI 263
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
65-281 1.03e-24

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: 102.32  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  65 KELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLIlGSENVDYYASF 144
Cdd:cd19996    26 AKLKKLIKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSGV-GSDKYTAFVGV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 145 DNEKVGELQGSYIVDKLglkaGKKGpfNIELFAG--SNDDNNTKYffNGAMNVLKPYMDKGQLVvrskqtalNQVTTlrW 222
Cdd:cd19996   105 DDAAFGRVGAEWLVKQL----GGKG--NIIALRGiaGVSVSEDRW--AGAKEVFKEYPGIKIVG--------EVYAD--W 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1654132688 223 DGGTAQKRMDDLLTSsyrSARVDAVLSPYDGISIGILSALKSDGygsgsKPMPVVTGQD 281
Cdd:cd19996   167 DYAKAKQAVESLLAA---YPDIDGVWSDGGAMTLGAIEAFEEAG-----RPLVPMTGED 217
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
43-352 2.74e-24

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: 100.56  E-value: 2.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd06318     1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLGLKAGKkgpfnIELFAGSNDDNNTKYFFNGAMNVLkpymDK 202
Cdd:cd06318    81 IPVITVDSALDPSANVATQVGRDNKQNGVLVGKEAAKALGGDPGK-----IIELSGDKGNEVSRDRRDGFLAGV----NE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 GQLVVRSKqTALNQVTTL--RWDGGTAQKRMDDLLTSsyrSARVDAVLSPYDGISIGILSALKSDGYGSGSKpmpvVTGQ 280
Cdd:cd06318   152 YQLRKYGK-SNIKVVAQPygNWIRSGAVAAMEDLLQA---HPDINVVYAENDDMALGAMKALKAAGMLDKVK----VAGA 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654132688 281 DAEVASVKSIISGQQTQTVYKDLRELAKVAsnmvdavlndkkpeVNDTKSYDNGAKVVPAYLLQPVS-VDKDN 352
Cdd:cd06318   224 DGQKEALKLIKDGKYVATGLNDPDLLGKTA--------------VDTAAKVVKGEESFPEFTYTPTAlITKDN 282
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
43-324 4.09e-24

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: 99.68  E-value: 4.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIA--DGAnvEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKD 120
Cdd:cd06323     1 TIGLSVSTLNNPFFVSlkDGA--QAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 121 ADIPVVSYDRLILGSENVDYYASfDNEKVGELQGSYIVDKLGlkagkkGPFNI-EL--FAGSNDDNNTKYFFNgamNVLK 197
Cdd:cd06323    79 AGIPVITVDRSVTGGKVVSHIAS-DNVAGGEMAAEYIAKKLG------GKGKVvELqgIPGTSAARERGKGFH---NAIA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 198 PYmdkGQLVVRSKQTAlnqvttlRWDGGTAQKRMDDLLTSsyrSARVDAVLSPYDGISIGILSALKSDGygsgsKPMPVV 277
Cdd:cd06323   149 KY---PKINVVASQTA-------DFDRTKGLNVMENLLQA---HPDIDAVFAHNDEMALGAIQALKAAG-----RKDVIV 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1654132688 278 TGQDAEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPE 324
Cdd:cd06323   211 VGFDGTPDAVKAVKDGKLAATVAQQPEEMGAKAVETADKYLKGEKVP 257
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
43-294 1.22e-23

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: 98.59  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTkSSERWIAdGANVEKELKAKGYE--TKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKD 120
Cdd:cd06311     1 TIGISIPS-ADHGWTA-GVAYYAEKQAKELAdlEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 121 ADIPVVSYDRlILGSENVDYYASFDNEKVGELQGSYIVDKLGlkaGKKGPFNIELFAGSNDDNNTKyffNGAMNVLKPYM 200
Cdd:cd06311    79 AGIPVVNFDR-GLNVLIYDLYVAGDNPGMGVVSAEYIGKKLG---GKGNVVVLEVPSSGSVNEERV---AGFKEVIKGNP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 201 dkGQLVVRSKQTALNQVTTLrwdggtaqKRMDDLLTSsyrSARVDAVLSPYDGISIGILSALKSdgygSGSKPMPVVTGQ 280
Cdd:cd06311   152 --GIKILAMQAGDWTREDGL--------KVAQDILTK---NKKIDAVWAADDDMAIGVLQAIKE----AGRTDIKVMTGG 214
                         250
                  ....*....|....
gi 1654132688 281 DAEVASVKSIISGQ 294
Cdd:cd06311   215 GGSQEYFKRIMDGD 228
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
43-325 1.25e-23

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


Pssm-ID: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 98.61  E-value: 1.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd19968     1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSENVDYYASfDNEKVGELQGSYIVDKLGLKA------GKKGpfnielfAGSNDDnNTKYFFNGamnvL 196
Cdd:cd19968    81 IPVVTVDRRAEGAAPVPHVGA-DNVAGGREVAKFVVDKLPNGAkvieltGTPG-------SSPAID-RTKGFHEE----L 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 197 KPYmDKGQLVVrsKQTAlnqvttlRWDGGTAQKRMDDLLTSSyrSARVDAVLSPYDGISIGILSALKSDGYGSGSKpmpV 276
Cdd:cd19968   148 AAG-PKIKVVF--EQTG-------NFERDEGLTVMENILTSL--PGPPDAIICANDDMALGAIEAMRAAGLDLKKV---K 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1654132688 277 VTGQDAEVASVKSIISGQQTQTV-YKDLRELAKVASNMVDAVLNDKKPEV 325
Cdd:cd19968   213 VIGFDAVPDALQAIKDGELYATVeQPPGGQARTALRILVDYLKDKKAPKK 262
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
69-281 2.60e-22

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: 95.43  E-value: 2.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  69 AKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLIlgSENVDYYASFDNEK 148
Cdd:cd19998    31 ADKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVV--DEPCAYNVNTDQAK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 149 VGELQGSYIVDKLGlkaGKKGPFNIELFAGSNDDnNTKYffNGAMNVLKPYMDKgqLVVRSKQTalnqvttlRWDGGTAQ 228
Cdd:cd19998   109 AGEQTAQWLVDKLG---GKGNILMVRGVPGTSVD-RDRY--EGAKEVFKKYPDI--KVVAEYYG--------NWDDGTAQ 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1654132688 229 KRMDDLLtssyrsarvdAVLSPYDGI-----SIGILSALKSDGygsgsKPMPVVTGQD 281
Cdd:cd19998   173 KAVADAL----------AAHPDVDGVwtqggETGVIKALQAAG-----HPLVPVGGEA 215
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
82-279 1.94e-21

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: 93.16  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  82 DPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLIlgSENVDYYASFDNEKVGELQGSYIVDKL 161
Cdd:cd06300    45 DATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGAV--TSPDAYNVSNDQVEWGRLGAKWLFEAL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 162 GlkaGKKGPFNIELFAGS--NDDnntkyFFNGAMNVLKPYMDKgqlvvrskqTALNQVTTlRWDGGTAQKRMDDLLTSsy 239
Cdd:cd06300   123 G---GKGNVLVVRGIAGApaSAD-----RHAGVKEALAEYPGI---------KVVGEVFG-GWDEATAQTAMLDFLAT-- 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1654132688 240 rSARVDAVLSpYDGISIGILSALKSdgygSGSKPMPVVTG 279
Cdd:cd06300   183 -HPQVDGVWT-QGGEDTGVLQAFQQ----AGRPPVPIVGG 216
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
43-324 5.54e-21

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: 91.11  E-value: 5.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd19971     1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLGLKAgkkgpfNIELFAgSNDDNNTKYFFNGAMNVLKpymDK 202
Cdd:cd19971    81 IPVINVDTPVKDTDLVDSTIASDNYNAGKLCGEDMVKKLPEGA------KIAVLD-HPTAESCVDRIDGFLDAIK---KN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 GQLVVRSKQTALNQVttlrwdgGTAQKRMDDLLTSsyrSARVDAVLSPYDGISIGILSALKSDGYGSGSKpmpvVTGQDA 282
Cdd:cd19971   151 PKFEVVAQQDGKGQL-------EVAMPIMEDILQA---HPDLDAVFALNDPSALGALAALKAAGKLGDIL----VYGVDG 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1654132688 283 EVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPE 324
Cdd:cd19971   217 SPDAKAAIKDGKMTATAAQSPIEIGKKAVETAYKILNGEKVE 258
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
43-266 9.64e-20

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 87.72  E-value: 9.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd06322     1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSENVDYYASfDNEKVGELQGSYIVDKLGLKAGKKGpfnielFAGSNDDNNTKYFFNGAMNVLKPYMDk 202
Cdd:cd06322    81 IPVFTVDVKADGAKVVTHVGT-DNYAGGKLAGEYALKALLGGGGKIA------IIDYPEVESVVLRVNGFKEAIKKYPN- 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654132688 203 gqlvvrskqtaLNQVTTLRWDGG--TAQKRMDDLLTSsyrSARVDAVLSPYDGISIGILSALKSDG 266
Cdd:cd06322   153 -----------IEIVAEQPGDGRreEALAATEDMLQA---NPDLDGIFAIGDPAALGALTAIESAG 204
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
62-279 1.97e-19

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


Pssm-ID: 380652 [Multi-domain]  Cd Length: 305  Bit Score: 87.34  E-value: 1.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  62 NVEKELKAKGY--ETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLIlgSENVD 139
Cdd:cd19997    23 EAAKKAKADGLiaDYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGV--TEPCA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 140 YYASFDNEKVGELQGSYIVDKLGlkaGKKGPFNIELFAGSNDDNNtkyFFNGAMNVLKPYMDkgqlvvrskqtaLNQVTT 219
Cdd:cd19997   101 YILNNDFEDYGAASVEYVADRLG---GKGNVLEVRGVAGTSPDEE---IYAGQVEALKKYPD------------LKVVAE 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654132688 220 L--RWDGGTAQKRMDDLLTSsyrSARVDAVLSpYDGISIGILSALKSDGygsgsKPMPVVTG 279
Cdd:cd19997   163 VygNWTQSVAQKAVTGILPS---LPEVDAVIT-QGGDGYGAAQAFEAAG-----RPLPIIIG 215
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
43-323 7.74e-19

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: 85.07  E-value: 7.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAID-NKSLDNVlQQAKDA 121
Cdd:cd19967     1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADaDASIAAV-KKAKDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 122 DIPVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLglkaGKKGPFnIELFaGSNDDNNTKYFFNGAMNVLKPYMD 201
Cdd:cd19967    80 GIPVFLIDREINAEGVAVAQIVSDNYQGAVLLAQYFVKLM----GEKGLY-VELL-GKESDTNAQLRSQGFHSVIDQYPE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 202 kgqLVVRSKQTAlnqvttlRWDGGTAQKRMDDLLTSsyrSARVDAVLSPYDGISIGILSALKSDGYGSGSKpmpvVTGQD 281
Cdd:cd19967   154 ---LKMVAQQSA-------DWDRTEAFEKMESILQA---NPDIKGVICGNDEMALGAIAALKAAGRAGDVI----IVGFD 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1654132688 282 AEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKP 323
Cdd:cd19967   217 GSNDVRDAIKEGKISATVLQPAKLIARLAVEQADQYLKGGST 258
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
43-279 2.01e-17

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


Pssm-ID: 380654 [Multi-domain]  Cd Length: 313  Bit Score: 81.97  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSErW----IADGANVEKELKAKGYETKLVYGEDDPD--QQVSQIENMITQGVDALIIAAIDNKSLDNVLQ 116
Cdd:cd19999     1 VIGVSNGYVGNE-WraqmIADFEEVAAEYKEEGVISDLIVQNADADatGQISQIRNMINEGVDAILIDPVSATALNPVIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 117 QAKDADIPVVSYDRLIlGSENVdYYASFDNEKVGELQGSYIVDKLGlkaGKKGPFNIELFAGSNDDNNTKyffNGAMNVL 196
Cdd:cd19999    80 KAQAAGILVVSFDQPV-SSPDA-INVVIDQYKWAAIQAQWLAEQLG---GKGNIVAINGVAGNPANEARV---KAADDVF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 197 KPYMDkGQLvvrskqtaLNQVTTlRWDGGTAQKRMDDLLtSSYrsARVDAVLSPyDGISIGILSALKSDGygsgsKPMPV 276
Cdd:cd19999   152 AKYPG-IKV--------LASVPG-GWDQATAQQVMATLL-ATY--PDIDGVLTQ-DGMAEGVLRAFQAAG-----KDPPV 212

                  ...
gi 1654132688 277 VTG 279
Cdd:cd19999   213 MTG 215
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
43-297 2.42e-17

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: 80.95  E-value: 2.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd19972     1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSENVDYYASFDNEKVGELqGSYIVDKLGLKAgkkgpfNIELFAGSNDDNNTKYFFNGAMNVLKPYMDk 202
Cdd:cd19972    81 IPVIAVDRNPEDAPGDTFIATDSVAAAKEL-GEWVIKQTGGKG------EIAILHGQLGTTPEVDRTKGFQEALAEAPG- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 gqLVVRSKQTAlnqvttlRWDGGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKsdgyGSGSKPMPVVTGQDA 282
Cdd:cd19972   153 --IKVVAEQTA-------DWDQDEGFKVAQDMLQ---ANPNITVFFGQSDAMALGAAQAVK----VAGLDHKIWVVGFDG 216
                         250       260
                  ....*....|....*....|..
gi 1654132688 283 EVASVKSIISG-------QQTQ 297
Cdd:cd19972   217 DVAGLKAVKDGvldatmtQQTQ 238
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
43-319 3.15e-17

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: 80.87  E-value: 3.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDAD 122
Cdd:cd06319     1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSENVDYYASfDNEKVGELQGSYIVDKL---GLKAGKKGPFNIELFAgSNDDNNTKYFFNGamnvlkpy 199
Cdd:cd06319    81 IPVVIADIGTGGGDYVSYIIS-DNYDGGYQAGEYLAEALkenGWGGGSVGIIAIPQSR-VNGQARTAGFEDA-------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 200 MDKGQLVVrskqTALNQVTTLRWDGGTaqKRMDDLLTSsyrSARVDAVLSPYDGISIGILSALKSDGYGSGSkpmpVVTG 279
Cdd:cd06319   151 LEEAGVEE----VALRQTPNSTVEETY--SAAQDLLAA---NPDIKGIFAQNDQMAQGALQAIEEAGRTGDI----LVVG 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1654132688 280 QDAEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLN 319
Cdd:cd06319   218 FDGDPEALDLIKDGKLDGTVAQQPFGMGARAVELAIQALN 257
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
43-299 1.43e-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: 76.13  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWI--ADGAnVEKELKAKGYETkLVYG---EDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQ 117
Cdd:cd19970     1 KVALVMKSLANEFFIemEKGA-RKHAKEANGYEL-LVKGikqETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 118 AKDADIPVVSYD-RL---ILGSENVDY-YASFDNEKVGELQGSYIVDKLGlKAGKKGPfnIELFAGSNDDNNTKYFFNGA 192
Cdd:cd19970    79 AVDAGIAVINIDnRLdadALKEGGINVpFVGPDNRQGAYLAGDYLAKKLG-KGGKVAI--IEGIPGADNAQQRKAGFLKA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 193 mnvlkpyMDKGQLVVRSKQTALnqvttlrWDGGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKSdgygSGSK 272
Cdd:cd19970   156 -------FEEAGMKIVASQSAN-------WEIDEANTVAANLLT---AHPDIRGILCANDNMALGAIKAVDA----AGKA 214
                         250       260
                  ....*....|....*....|....*..
gi 1654132688 273 PMPVVTGQDAEVASVKSIISGQQTQTV 299
Cdd:cd19970   215 GKVLVVGFDNIPAVRPLLKDGKMLATI 241
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
44-352 5.78e-15

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: 74.22  E-value: 5.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  44 IGIAMPTKSSERWIADGANVEKELKAKG--YETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDA 121
Cdd:cd06320     2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGvkVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 122 DIPVVSYDRLILGSE------NVDYYASFDNEKVGELQGSYIVDKLGlKAGKKGpfNIELFAGS-NDDNNTKyffnGAMN 194
Cdd:cd06320    82 GIPVINLDDAVDADAlkkaggKVTSFIGTDNVAAGALAAEYIAEKLP-GGGKVA--IIEGLPGNaAAEARTK----GFKE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 195 VLKPYmDKGQLVvrskqtalnQVTTLRWDGGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKSdgygSGSKPM 274
Cdd:cd06320   155 TFKKA-PGLKLV---------ASQPADWDRTKALDAATAILQ---AHPDLKGIYAANDTMALGAVEAVKA----AGKTGK 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654132688 275 PVVTGQDAEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKK-PEVndtksydngaKVVPAYLlqpvsVDKDN 352
Cdd:cd06320   218 VLVVGTDGIPEAKKSIKAGELTATVAQYPYLEGAMAVEAALRLLQGQKvPAV----------VATPQAL-----ITKDN 281
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
43-338 8.88e-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: 73.53  E-value: 8.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVY--GEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKD 120
Cdd:cd06310     1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGpeSEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 121 ADIPVVSYDRLILGSENVDYYASfDNEKVGELQGSYIVDKLGlKAGKKGPFNIELFAGSNDDNNTkyffnGAMNVLKPym 200
Cdd:cd06310    81 KGIPVIVIDSGIKGDAYLSYIAT-DNYAAGRLAAQKLAEALG-GKGKVAVLSLTAGNSTTDQREE-----GFKEYLKK-- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 201 DKGQLVVRSKQTALNQVttlrwdgGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKSDGYgsgSKPMPVVtGQ 280
Cdd:cd06310   152 HPGGIKVLASQYAGSDY-------AKAANETEDLLG---KYPDIDGIFATNEITALGAAVAIKSRKL---SGQIKIV-GF 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1654132688 281 DAEVASVKSIISGQQTQTVYKDLRELAKVASNMVDAVLNDKKPEvndtKSYDNGAKVV 338
Cdd:cd06310   218 DSQEELLDALKNGKIDALVVQNPYEIGYEGIKLALKLLKGEEVP----KNIDTGAELI 271
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
43-323 9.07e-15

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: 73.48  E-value: 9.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKL--VYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKD 120
Cdd:cd06321     1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGAKVtvVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 121 ADIPVVSYDrliLGSENVDYYASFDNEKVGELQGSYIVDKLGLKaGK----KGPFN---IELFAGSNddnntkyffngam 193
Cdd:cd06321    81 AGIIVVAVD---VAAEGADATVTTDNVQAGYLACEYLVEQLGGK-GKvaiiDGPPVsavIDRVNGCK------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 194 NVLKPYMDkgqlvvrskqtaLNQVTTLRWDGGTAQKR--MDDLLTssyRSARVDAVLSPYDGISIGILSALKsdgyGSGS 271
Cdd:cd06321   144 EALAEYPG------------IKLVDDQNGKGSRAGGLsvMTRMLT---AHPDVDGVFAINDPGAIGALLAAQ----QAGR 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1654132688 272 KPMpVVTGQD------AEVASVKSIISGQQTQtvykDLRELAKVASNMVDAVLNDKKP 323
Cdd:cd06321   205 DDI-VITSVDgspeavAALKREGSPFIATAAQ----DPYDMARKAVELALKILNGQEP 257
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
43-266 9.20e-15

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: 73.48  E-value: 9.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKS---SERWIaDGAnvEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAK 119
Cdd:cd06305     1 TIAVVRNGTSgdwDQQAL-QGA--VAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 120 DADIPVVSYDRLILGSENVdyYASFDNEKVGELQGSYIVDKLGLKAgkkgpfNIELFAGSN----DDNNTKYffngaMNV 195
Cdd:cd06305    78 DAGIPVVTFDTDSQVPGVN--NITQDDYALGTLSLGQLVKDLNGEG------NIAVFNVFGvpplDKRYDIY-----KAV 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654132688 196 LKPYMDkGQLVVRSKQTALNQVTtlrwdgGTAQKRMDDLLTsSYRSARVDAVLSPYDGISIGILSALKSDG 266
Cdd:cd06305   145 LKANPG-IKKIVAELGDVTPNTA------ADAQTQVEALLK-KYPEGGIDAIWAAWDEPAKGAVQALEEAG 207
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
43-167 8.45e-14

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: 70.69  E-value: 8.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLV----YGEDDpdQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQA 118
Cdd:cd06306     1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYeaggYTNLS--KQISQLEDCVASGADAILLGAISFDGLDPKVAEA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1654132688 119 KDADIPVVSYDRLILgSENVDYYASFDNEKVGELQGSYIVDKLGLKAGK 167
Cdd:cd06306    79 AAAGIPVIDLVNGID-SPKVAARVLVDFYDMGYLAGEYLVEHHPGKPVK 126
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
82-220 8.46e-14

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


Pssm-ID: 380525 [Multi-domain]  Cd Length: 296  Bit Score: 71.12  E-value: 8.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  82 DPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLIlGSENVDYYAS-FDNEKVGELqgsyIVDK 160
Cdd:cd06302    41 DAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSDA-PPSARDYFVNqADDEGLGEA----LVDS 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654132688 161 LGLKAGKKGpfNIELFAGSNDDNNTKYFFNGAMNVLKPYMDKGQLVVR-----SKQTALNQVTTL 220
Cdd:cd06302   116 LAKEIGGKG--KVAILSGSLTATNLNAWIKAMKEYLKSKYPDIELVDTyytddDQQKAYTQAQNL 178
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
80-169 1.15e-13

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


Pssm-ID: 380656  Cd Length: 296  Bit Score: 70.77  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  80 EDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLILgsENVDY-YASFDNEKVGElqgsYIV 158
Cdd:cd20001    39 TADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDAGIVVITHEASNL--KNVDYdVEAFDNAAYGA----FIM 112
                          90
                  ....*....|.
gi 1654132688 159 DKLGLKAGKKG 169
Cdd:cd20001   113 DKLAEAMGGKG 123
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
59-324 1.93e-13

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 70.12  E-value: 1.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  59 DGAnvEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLILGSENV 138
Cdd:PRK10653   46 DGA--QKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 139 DYYASfDNEKVGELQGSYIVDKLGLKAGKkgpFNIELFAGSNDDNNTKYFFNGAmnvlkpyMDKGQLVVRSKQTAlnqvt 218
Cdd:PRK10653  124 SHIAS-DNVAGGKMAGDFIAKKLGEGAKV---IQLEGIAGTSAARERGEGFKQA-------VAAHKFNVLASQPA----- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 219 tlRWDGGTAQKRMDDLLTSsyrSARVDAVLSPYDGISIGILSALKSDGygsgsKPMPVVTGQDAEVASVKSIISGQQTQT 298
Cdd:PRK10653  188 --DFDRTKGLNVMQNLLTA---HPDVQAVFAQNDEMALGALRALQTAG-----KSDVMVVGFDGTPDGIKAVNRGKLAAT 257
                         250       260
                  ....*....|....*....|....*.
gi 1654132688 299 VYKDLRELAKVASNMVDAVLNDKKPE 324
Cdd:PRK10653  258 IAQQPDQIGAIGVETADKVLKGEKVE 283
PRK15395 PRK15395
galactose/glucose ABC transporter substrate-binding protein MglB;
63-352 3.87e-13

galactose/glucose ABC transporter substrate-binding protein MglB;


Pssm-ID: 185293 [Multi-domain]  Cd Length: 330  Bit Score: 69.37  E-value: 3.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  63 VEKELKAKGyETKLVYGEDDPDQ--QVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYD----RLILGSE 136
Cdd:PRK15395   46 IEKDAKAAP-DVQLLMNDSQNDQskQNDQIDVLLAKGVKALAINLVDPAAAPTVIEKARGQDVPVVFFNkepsRKALDSY 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 137 NVDYYASFDNEKVGELQGSYIVDKL----GLKAGKKGPFNIELFAGS----NDDNNTKYffngamnVLKPYMDKGqlvVR 208
Cdd:PRK15395  125 DKAYYVGTDSKESGIIQGDLIAKHWkanpAWDLNKDGKIQYVLLKGEpghpDAEARTTY-------VIKELNDKG---IK 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 209 SKQTALNqvtTLRWDGGTAQKRMDDLLTSSyRSARVDAVLSPYDGISIGILSALKSDGYGSgskpMPVVtGQDAEVASVK 288
Cdd:PRK15395  195 TEQLQLD---TAMWDTAQAKDKMDAWLSGP-NANKIEVVIANNDAMAMGAVEALKAHNKSS----IPVF-GVDALPEALA 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654132688 289 SIISGQQTQTVYKDLRELAKVASNMVDAvLNDKKPEVNDTKsYDNGAKVVP-AYllqpVSVDKDN 352
Cdd:PRK15395  266 LVKSGAMAGTVLNDANNQAKATFDLAKN-LADGKGAAEGTN-WKIENKVVRvPY----VGVDKDN 324
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
80-328 4.97e-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: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 68.41  E-value: 4.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  80 EDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLILGSENVDYYASfDNEKVGELQGSYIVD 159
Cdd:cd20004    40 EDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDSDLGGDAVISFVAT-DNYAAGRLAAKRMAK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 160 KLglkaGKKGpfNIELFAGSNDDNNTKYFFNGAMNVLKPYMDkgQLVVRSKQTALNQVttlrwdgGTAQKRMDDLLTSSY 239
Cdd:cd20004   119 LL----NGKG--KVALLRLAKGSASTTDRERGFLEALKKLAP--GLKVVDDQYAGGTV-------GEARSSAENLLNQYP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 240 rsaRVDAVLSPYDGISIGILSALKSDGYGSGskpmPVVTGQDAEVASVKSIISGQQTQTVYKDLRELAKVA-SNMVDAVL 318
Cdd:cd20004   184 ---DVDGIFTPNESTTIGALRALRRLGLAGK----VKFIGFDASDLLLDALRAGEISALVVQDPYRMGYLGvKTAVAALR 256
                         250
                  ....*....|
gi 1654132688 319 NDKKPEVNDT 328
Cdd:cd20004   257 GKPVPKRIDT 266
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
43-285 1.53e-12

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: 67.15  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSlDNVLQQAKDAD 122
Cdd:pfam00532   3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSG-DDITAKAEGYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVSYDRLILGSENVDYYAsFDNEKVGELQGSYIVdklglKAGKKGPfnIELFAGSNDDNNTKYFFNGAMNVLKpymdK 202
Cdd:pfam00532  82 IPVIAADDAFDNPDGVPCVM-PDDTQAGYESTQYLI-----AEGHKRP--IAVMAGPASALTARERVQGFMAALA----A 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 203 GQLVVRSKQTALnqvttlrwdGGTAQKRMDDLLTSSYRSA-RVDAVLSPYDGISIGILSALKSDGYGSGskPMPVVTGQD 281
Cdd:pfam00532 150 AGREVKIYHVAT---------GDNDIPDAALAANAMLVSHpTIDAIVAMNDEAAMGAVRALLKQGRVKI--PDIVGIGIN 218

                  ....
gi 1654132688 282 AEVA 285
Cdd:pfam00532 219 SVVG 222
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
80-169 1.76e-12

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


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 66.88  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  80 EDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLIlGSENVDYYASFDNEKVGELQGsyivD 159
Cdd:cd20005    40 ESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGV-PSDLPLATVATDNYAAGALAA----D 114
                          90
                  ....*....|
gi 1654132688 160 KLGLKAGKKG 169
Cdd:cd20005   115 HLAELIGGKG 124
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
56-199 2.10e-12

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: 66.45  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  56 WIADGANVEKELKAKGYETKLVYGED-DPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLILG 134
Cdd:cd06314    14 WDLAEAGAEKAAKELGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFDSDAPD 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654132688 135 SENVDYYASfDNEKVGELQGSYIVDKLGlKAGKkgpfnIELFAGSNDDNNTKYFFNGAMNVLKPY 199
Cdd:cd06314    94 SKRLAYIGT-DNYEAGREAGELMKKALP-GGGK-----VAIITGGLGADNLNERIQGFKDALKGS 151
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
63-159 3.32e-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: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 66.25  E-value: 3.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  63 VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRlILGSENVDYYA 142
Cdd:cd06317    21 AQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDA-VIPSDFQAAQV 99
                          90
                  ....*....|....*..
gi 1654132688 143 SFDNEKVGELQGSYIVD 159
Cdd:cd06317   100 GVDNLEGGKEIGKYAAD 116
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
43-267 5.32e-12

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: 65.23  E-value: 5.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKS----SErwIADGanVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKslDNVLQQA 118
Cdd:cd06267     1 TIGLIVPDISnpffAE--LLRG--IEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLD--DELLEEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 119 KDADIPVVSYDRLILGsENVDyYASFDNEkvgelQGSY-IVDKLgLKAGKKgpfNIELFAGSNDDNNTKYFFNGAMNVLK 197
Cdd:cd06267    75 LAAGIPVVLIDRRLDG-LGVD-SVVVDNY-----AGAYlATEHL-IELGHR---RIAFIGGPLDLSTSRERLEGYRDALA 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654132688 198 ----PYMDkgQLVVRSkqtalnqvttlRWDGGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKSDGY 267
Cdd:cd06267   144 eaglPVDP--ELVVEG-----------DFSEESGYEAARELLA---LPPRPTAIFAANDLMAIGALRALRELGL 201
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
43-324 8.67e-12

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 65.61  E-value: 8.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKS----SErwIADGanVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKslDNVLQQA 118
Cdd:COG1609    63 TIGVVVPDLSnpffAE--LLRG--IEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLD--DARLERL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 119 KDADIPVVSYDRLIlGSENVDyYASFDNEKVGELqgsyIVDKLgLKAGKKgpfNIELFAGSNDDNNTKYFFNGAMNVLKp 198
Cdd:COG1609   137 AEAGIPVVLIDRPL-PDPGVP-SVGVDNRAGARL----ATEHL-IELGHR---RIAFIGGPADSSSARERLAGYREALA- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 199 ymDKG-----QLVVRSKQTAlnqvttlrwDGGtaQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKSDGygsgskp 273
Cdd:COG1609   206 --EAGlppdpELVVEGDFSA---------ESG--YEAARRLLA---RGPRPTAIFCANDLMALGALRALREAG------- 262
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1654132688 274 mpVVTGQDAEVASVKSIISGQQTQ----TVYKDLRELAKVASNMVDAVLNDKKPE 324
Cdd:COG1609   263 --LRVPEDVSVVGFDDIPLARYLTppltTVRQPIEEMGRRAAELLLDRIEGPDAP 315
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
46-169 9.53e-12

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


Pssm-ID: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 64.94  E-value: 9.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  46 IAMPTKS--SERWIADGANVEKELKAKGYETKLVYG--EDDPDQQVSQIENMITQGVDALIIAAIDNKSLdNVLQQAKDA 121
Cdd:cd20008     2 IAVIVKDtdSEYWQTVLKGAEKAAKELGVEVTFLGPatEADIAGQVNLVENAISRKPDAIVLAPNDTAAL-VPAVEAADA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1654132688 122 DIPVVSYDRLIlgseNVDYYASF---DNEKVGELQGSYIVDKLGLKAGKKG 169
Cdd:cd20008    81 GIPVVLVDSGA----NTDDYDAFlatDNVAAGALAADELAELLKASGGGKG 127
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
43-357 1.74e-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: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 64.18  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSErWIA---DGAnvEKELKAKGYE-TKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQA 118
Cdd:cd06316     1 KVAIAMHTTGSD-WSRlqvAGI--KDTFEELGIEvVAVTDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 119 KDADIPVVSYDRLILGSENVDYYA---SFDNEKVGELQGSYIVDKLGLKaGKKG--PFNIELFAgsnddNNTKYffNGAM 193
Cdd:cd06316    78 ADAGIKLVFMDNVPDGLEAGKDYVsvvSSDNRGNGQIAAELLAEAIGGK-GKVGiiYHDADFYA-----TNQRD--KAFK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 194 NVLKPYMDKGQLVVRSKQTALNQVttlrwdGGTAQkrmdDLLTssyRSARVDAVLSPYDGISIGILSALKSDGYgsgsKP 273
Cdd:cd06316   150 DTLKEKYPDIKIVAEQGFADPNDA------EEVAS----AMLT---ANPDIDGIYVSWDTPALGVISALRAAGR----SD 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 274 MPVVTGQ-DAEVASV---KSIISGQQTQTVYKDLRELAKVASNmvdAVLNdkkpevndtksydngaKVVPAYL-LQPVSV 348
Cdd:cd06316   213 IKITTVDlGTEIALDmakGGNVKGIGAQRPYDQGVAEALAAAL---ALLG----------------KEVPPFIgVPPLAV 273
                         330
                  ....*....|...
gi 1654132688 349 DKDN----YKKVL 357
Cdd:cd06316   274 TKDNlleaWKQIF 286
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
61-324 2.43e-11

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


Pssm-ID: 380479 [Multi-domain]  Cd Length: 265  Bit Score: 63.42  E-value: 2.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  61 ANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSlDNVLQQAKDADIPVVSYDRlilGSENVD- 139
Cdd:cd01537    19 KAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAA-AGVAEKARGQNVPVVFFDK---EPSRYDk 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 140 -YYASFDNEKVGELQGSYIVdklglkagKKGPFNIELFAGSNDDNNTKYFFNGAMNVLKPYMDKGQLVvrskqtalnQVT 218
Cdd:cd01537    95 aYYVITDSKEGGIIQGDLLA--------KHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQL---------QLD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 219 TLRWDGGTAQKRMDDLLTSSYrsaRVDAVLSPYDGISIGILSALKSDGYGSGSKpMPVVTGQDAEVASVksiiSGQQTQT 298
Cdd:cd01537   158 TGDWDTASGKDKMDQWLSGPN---KPTAVIANNDAMAMGAVEALKEHGLRVPSD-ISVFGYDALPEALK----SGPLLTT 229
                         250       260
                  ....*....|....*....|....*.
gi 1654132688 299 VYKDLRELAKVASNMVDAVLNDKKPE 324
Cdd:cd01537   230 ILQDANNLGKTTFDLLLNLADNWKID 255
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
82-202 6.73e-11

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: 62.29  E-value: 6.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  82 DPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLILGSENVDyyASF---DNEKVGELQGSYIv 158
Cdd:cd19965    41 DVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAFNVDAPGGENAR--LAFvgqDLYPAGYVLGKRI- 117
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1654132688 159 dklgLKAGKKGPFNIELFAGSNDDNNTKYFFNGAMNVLKPYMDK 202
Cdd:cd19965   118 ----AEKFKPGGGHVLLGISTPGQSALEQRLDGIKQALKEYGRG 157
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
53-161 2.41e-10

periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380482 [Multi-domain]  Cd Length: 294  Bit Score: 60.77  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  53 SERWIADGAN-VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRL 131
Cdd:cd01540    10 DQPWFQDEWKgAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAGIPVIAVDDQ 89
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1654132688 132 ILGSENVDY--YASFDNEKVGELQGSYIVDKL 161
Cdd:cd01540    90 LVDADPMKIvpFVGIDAYKIGEAVGEWLAKEM 121
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
43-167 3.72e-10

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: 60.17  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQ--QVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKD 120
Cdd:cd19973     1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKIDGDNatQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1654132688 121 ADIPVVSYDRLILGSENVDYYASFDNEKVGELQGSYIVDKLGLKAGK 167
Cdd:cd19973    81 AGVLVIALDTPTDPIDAADATFATDNFKAGVLIGEWAKAALGAKDAK 127
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
82-179 4.83e-10

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


Pssm-ID: 380657  Cd Length: 295  Bit Score: 60.02  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  82 DPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRliLGSENVDYYASF-DNEKVGELQgsyiVDK 160
Cdd:cd20002    41 DPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVITHES--PGQKGADWDVELiDNEKFGEAQ----MEL 114
                          90
                  ....*....|....*....
gi 1654132688 161 LGLKAGKKGPFNIelFAGS 179
Cdd:cd20002   115 LAKEMGGKGEYAI--FVGS 131
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
37-317 5.53e-10

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 59.89  E-value: 5.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  37 GGAEG-ATIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYG--EDDPDQQVSQIENMITQGVDALIIAAIDNKSLDN 113
Cdd:PRK09701   19 TSAFAaAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASpsEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVM 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 114 VLQQAKDADIPVVSYDR------LILGSENVDYYASFDNEKVGELQGSYIVDKLGLKAGKKGPfnIELFAGSNDDNNTKy 187
Cdd:PRK09701   99 PVARAWKKGIYLVNLDEkidmdnLKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAI--IEGKAGNASGEARR- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 188 ffNGAMNVLKpymdkgqlvvRSKQTALNQVTTLRWDGGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKSdgy 267
Cdd:PRK09701  176 --NGATEAFK----------KASQIKLVASQPADWDRIKALDVATNVLQ---RNPNIKAIYCANDTMAMGVAQAVAN--- 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1654132688 268 gSGSKPMPVVTGQDAEVASVKSIISGQQTQTVYKDLREL-AKVASNMVDAV 317
Cdd:PRK09701  238 -AGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIgATGLKLMVDAE 287
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
61-160 2.72e-09

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: 57.19  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  61 ANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDnVLQQAKDADIPVVSYDRLILGSEnVDY 140
Cdd:cd06289    19 AGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTTAE-LLRRLKAWGIPVVLALRDVPGSD-LDY 96
                          90       100
                  ....*....|....*....|
gi 1654132688 141 YASfDNEKVGELQGSYIVDK 160
Cdd:cd06289    97 VGI-DNRLGAQLATEHLIAL 115
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
80-173 2.10e-08

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


Pssm-ID: 380658  Cd Length: 298  Bit Score: 54.98  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  80 EDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDrlilGSENVDYYASFDNEKVGELQGSYIVD 159
Cdd:cd20003    39 EASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVTWD----SDVNPDARDFFVNQATPEGIGKTLVD 114
                          90
                  ....*....|....
gi 1654132688 160 KLGLKAGKKGPFNI 173
Cdd:cd20003   115 MVAEQTGEKGKVAI 128
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
77-299 5.07e-08

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 53.76  E-value: 5.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  77 VYGEDDPDQQVSQIENMITQ--GVDALIIAAIDNkSLDNVLQQAKDADIPVVSYDRLILGSENVDYYA------------ 142
Cdd:cd06324    36 LYANRNRFKMLELAEELLARppKPDYLILVNEKG-VAPELLELAEQAKIPVFLINNDLTDEERALLGKprekfkywlgsi 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 143 SFDNEKVGELQGSYIVDKLGlKAGKKGPFNIELFAGSNDDNNTKYFFNGAMNVLKpymdkgqlvvRSKQTALNQVTTLRW 222
Cdd:cd06324   115 VPDNEQAGYLLAKALIKAAR-KKSDDGKIRVLAISGDKSTPASILREQGLRDALA----------EHPDVTLLQIVYANW 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654132688 223 DGGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKSdgygSGSKPMP--VVTGQDAEVASVKSIISGQQTQTV 299
Cdd:cd06324   184 SEDEAYQKTEKLLQ---RYPDIDIVWAANDAMALGAIDALEE----AGLKPGKdvLVGGIDWSPEALQAVKDGELTASV 255
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
46-162 9.95e-08

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 52.60  E-value: 9.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  46 IAMPTKS----SERW--IADGAnvekELKAKGYETKLVY----GEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVL 115
Cdd:cd20006     2 IALILKSsdpnSDFWqtVKSGA----EAAAKEYGVDLEFlgpeSEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAV 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1654132688 116 QQAKDADIPVVSYDRLIlGSENVDYYASFDNEKVGELQGSYIVDKLG 162
Cdd:cd20006    78 ERAKKAGIPVITIDSPV-NSKKADSFVATDNYEAGKKAGEKLASLLG 123
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
86-129 1.37e-07

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


Pssm-ID: 380655  Cd Length: 298  Bit Score: 52.26  E-value: 1.37e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1654132688  86 QVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYD 129
Cdd:cd20000    45 QIPFINTLIQQGVDAIAISANDPDALAPALKKARAAGIKVVTFD 88
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
66-169 1.87e-07

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


Pssm-ID: 380662 [Multi-domain]  Cd Length: 271  Bit Score: 51.86  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  66 ELKAKGYETKLVYGED---DPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYD-RLILGSENVDYY 141
Cdd:cd20007    22 EAAAKELGVELDVQGPptfDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVDtTLGDPSFVLSQI 101
                          90       100
                  ....*....|....*....|....*...
gi 1654132688 142 ASfDNEKVGELQGsyivDKLGLKAGKKG 169
Cdd:cd20007   102 AS-DNVAGGALAA----EALAELIGGKG 124
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
63-264 2.35e-07

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


Pssm-ID: 380632 [Multi-domain]  Cd Length: 264  Bit Score: 51.38  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  63 VEKELKAKGYetKLVYG--EDDPDQQVSQIENMITQGVDALIIAAIDNKslDNVLQQAKDADIPVVSYDRLILGSEnVDY 140
Cdd:cd19977    21 IEDEAYKNGY--HVILCntDEDPEKEKKYIEMLRAKQVDGIIIAPTGGN--EDLIEKLVKSGIPVVFVDRYIPGLD-VDT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 141 YASfDNEKvgelqGSY-IVDKLgLKAGKKgpfNIELFAGSNDDNNTKYFFNGAMNVLKPY-MDKGQLVVRSKQtalnqvt 218
Cdd:cd19977    96 VVV-DNFK-----GAYqATEHL-IELGHK---RIAFITYPLELSTRQERLEGYKAALADHgLPVDEELIKHVD------- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1654132688 219 tlRWDGGTAQkrMDDLLTSsyrSARVDAVLSPYDGISIGILSALKS 264
Cdd:cd19977   159 --RQDDVRKA--ISELLKL---EKPPDAIFAANNLITLEVLKAIKE 197
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
71-180 4.41e-07

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: 50.79  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  71 GYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAID-NKSLDNVLQQAKDADIPVVSYDRLILGSENVD---YYASFDN 146
Cdd:cd19966    30 GVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPgDGAYTPLIEAAKKAGIIVTSFNTDLPKLEYGDcglGYVGADL 109
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1654132688 147 EKVGELQGSYIVDKLGLKAGKKGpFNIELFAGSN 180
Cdd:cd19966   110 YAAGYTLAKELVKRGGLKTGDRV-FVPGLLPGQP 142
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
63-160 6.71e-07

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


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 50.25  E-value: 6.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  63 VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIA----AIDNKSLDnVLQQAKDADIPVVSYDRLIlgsENV 138
Cdd:cd01541    21 IESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEptksALPNPNLD-LYEELQKKGIPVVFINSYY---PEL 96
                          90       100
                  ....*....|....*....|...
gi 1654132688 139 DY-YASFDNEKVGELQGSYIVDK 160
Cdd:cd01541    97 DApSVSLDDEKGGYLATKHLIDL 119
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
63-344 8.90e-07

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


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 49.83  E-value: 8.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  63 VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNvlqqaKDADIPVVSYDRLIlgSENVDYYA 142
Cdd:cd06291    21 IEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEY-----KKLNIPIVSIDRYL--SEGIPSVS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 143 SfDNEKVGELqgsyIVDKLgLKAGKKgpfNIELFAGSNDDNNTKYFFNGAMNVLKpymdKGQLVVRSKQTALNQVTTlrw 222
Cdd:cd06291    94 S-DNYQGGRL----AAEHL-IEKGCK---KILHIGGPSNNSPANERYRGFEDALK----EAGIEYEIIEIDENDFSE--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 223 dgGTAQKRMDDLLTssyRSARVDAVLSPYDGISIGILSALKSDGYgsgSKP--MPVVTGQDAEVAS-VKSIISgqqtqTV 299
Cdd:cd06291   158 --EDAYELAKELLE---KYPDIDGIFASNDLLAIGVLKALQKLGI---RVPedVQIIGFDGIEISElLYPELT-----TI 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1654132688 300 YKDLRELAKVASNMVDAVLNDKKPEVNDtksydngaKVVPAYLLQ 344
Cdd:cd06291   225 RQPIEEMAKEAVELLLKLIEGEEIEESR--------IVLPVELIE 261
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
63-152 1.25e-06

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


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 49.15  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  63 VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAaiDNKSLDNVLQQAKDADIPVVSYDRLIlGSENVDyYA 142
Cdd:cd06285    21 IEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIIT--PARDDAPDLQELAARGVPVVLVDRRI-GDTALP-SV 96
                          90
                  ....*....|
gi 1654132688 143 SFDNEKVGEL 152
Cdd:cd06285    97 TVDNELGGRL 106
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
56-178 5.70e-06

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 47.64  E-value: 5.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  56 WIADGANVEKELKAKGYETKLVY--GEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKdADIPVVSY----- 128
Cdd:PRK10936   61 WLSVNYGMVEEAKRLGVDLKVLEagGYYNLAKQQQQLEQCVAWGADAILLGAVTPDGLNPDLELQA-ANIPVIALvngid 139
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1654132688 129 DRLILGSENVDYYasfdneKVGELQGSYIVDKLglkAGKKGPFNIELFAG 178
Cdd:PRK10936  140 SPQVTTRVGVSWY------QMGYQAGRYLAQWH---PKGSKPLNVALLPG 180
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
57-148 6.59e-06

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


Pssm-ID: 380522 [Multi-domain]  Cd Length: 268  Bit Score: 47.27  E-value: 6.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  57 IADGanVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIA-AIDNKSLdnvLQQAKDADIPVVSYDRLILGS 135
Cdd:cd06299    17 LASG--IEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVpTGENSEG---LQALIAQGLPVVFVDREVEGL 91
                          90
                  ....*....|...
gi 1654132688 136 ENVDYYASfDNEK 148
Cdd:cd06299    92 GGVPVVTS-DNRP 103
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
68-130 7.62e-06

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


Pssm-ID: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 46.82  E-value: 7.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654132688  68 KAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIA-AIDNkslDNVLQQAKDADIPVVSYDR 130
Cdd:cd06274    26 RERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVApSTPP---DDIYYLCQAAGLPVVFLDR 86
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
56-167 9.50e-06

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


Pssm-ID: 380624 [Multi-domain]  Cd Length: 278  Bit Score: 46.56  E-value: 9.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  56 WIADGANVEKELKAKGYETKLVyGEDDPD--QQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYDRLIL 133
Cdd:cd19969    14 WDDVKEGFEDAGAELGVKTEYT-GPATADvnEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSDAP 92
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1654132688 134 GSENVDYYASfDNEKVGELQGSYIVDKLGLKaGK 167
Cdd:cd19969    93 ESKRISYVGT-DNYEAGYAAAEKLAELLGGK-GK 124
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
63-160 2.67e-05

ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380499 [Multi-domain]  Cd Length: 269  Bit Score: 45.32  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  63 VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALI-IAAIDNKSLDNVLQQakDADIPVVSYDRLILGSeNVDyY 141
Cdd:cd06275    21 VEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLlMCSEMTDDDAELLAA--LRSIPVVVLDREIAGD-NAD-A 96
                          90
                  ....*....|....*....
gi 1654132688 142 ASFDNEKVGELQGSYIVDK 160
Cdd:cd06275    97 VLDDSFQGGYLATRHLIEL 115
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
61-126 2.80e-05

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 45.47  E-value: 2.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654132688  61 ANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNvLQQAKDADIPVV 126
Cdd:PRK10014   84 AGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDL-REMAEEKGIPVV 148
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
57-149 3.04e-05

ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380506 [Multi-domain]  Cd Length: 266  Bit Score: 45.23  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  57 IADGAN---------VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKslDNVLQQAKDADIPVVS 127
Cdd:cd06283     6 VADITNpfsslllkgIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNN--NDAYLELAQKGLPVVL 83
                          90       100
                  ....*....|....*....|..
gi 1654132688 128 YDRLILGSeNVDYYASfDNEKV 149
Cdd:cd06283    84 VDRQIEPL-NWDTVVT-DNYDA 103
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
63-197 3.29e-05

ligand-binding domain of putative DNA transcription regulators highly similar to that of the transcription regulator DegA; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the transcription regulator DegA, which is involved in the control of degradation of Bacillus subtilis amidophosphoribosyltransferase (purF). This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380631 [Multi-domain]  Cd Length: 268  Bit Score: 44.93  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  63 VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIA--AIDNKSLDNVLQQAKdadIPVVSYDRLIlgSENVDY 140
Cdd:cd19976    21 IEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIAssNISDEAIIKLLKEEK---IPVVVLDRYI--EDNDSD 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1654132688 141 YASFDNEKvgelqGSYIVDKLGLKAGKKgpfNIELFAGSNDDNNTKYFFNGAMNVLK 197
Cdd:cd19976    96 SVGVDDYR-----GGYEATKYLIELGHT---RIGCIVGPPSTYNEHERIEGYKNALQ 144
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
43-329 5.31e-05

ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380521 [Multi-domain]  Cd Length: 268  Bit Score: 44.20  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSE------RWIADGANVEKelkakgYETKLVYGEDDPDQQVSQIENMITQGVDALIIaaIDNKSLDNVLQ 116
Cdd:cd06298     1 TVGVIIPDISNLyyaelaRGIDDIATMYK------YNIILSNSDNNVDKELDLLNTMLSKQVDGIIF--MGDELTEEIRE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 117 QAKDADIPVV----SYDRLILGSENVDYYASFDNekvgelqgsyIVDKLgLKAGKKgpfNIELFAGS-NDDNNTKYFFNG 191
Cdd:cd06298    73 EFKRSPVPVVlagtVDSDHEIPSVNIDYEQAAYD----------ATKSL-IDKGHK---KIAFVSGPlKEYINNDKKLQG 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 192 AMNVLKP--YMDKGQLVVRSKQTalnqvttlrWDGGTAQkrMDDLLTSSYrsarVDAVLSPYDGISIGILSALKSDGYgs 269
Cdd:cd06298   139 YKRALEEagLEFNEPLIFEGDYD---------YDSGYEL--YEELLESGE----PDAAIVVRDEIAVGLLNAAQDRGL-- 201
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654132688 270 gSKP--MPVVTGQDAEVAsvksIISGQQTQTVYKDLRELAKVASNMVDAVLNDKkpEVNDTK 329
Cdd:cd06298   202 -KVPedLEIIGFDNTRYA----TMSRPQLTSINQPLYDIGAVAMRLLTKLMNKE--EVEETI 256
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
43-267 7.68e-05

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


Pssm-ID: 380484 [Multi-domain]  Cd Length: 259  Bit Score: 43.64  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNksLDNVLQQAKDAD 122
Cdd:cd01542     1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEI--TDEHRKALKKLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 123 IPVVsydrlILGSEnVDYYAS--FDNEKVGELQGSYIVDKlglkaGKKgpfNIeLFAGSNDDNNT--KYFFNGAMNVLKp 198
Cdd:cd01542    79 IPVV-----VLGQE-HEGFSCvyHDDYGAGKLLGEYLLKK-----GHK---NI-AYIGVDEEDIAvgVARKQGYLDALK- 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654132688 199 ymDKGQLVVRSKQTALNQVttlrwdggTAQKRMDDLLTSSyrsaRVDAVLSPYDGISIGILSALKSDGY 267
Cdd:cd01542   143 --EHGIDEVEIVETDFSME--------SGYEAAKELLKEN----KPDAIICATDNIALGAIKALRELGI 197
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
63-160 3.61e-04

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: 41.71  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  63 VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDnkSLDNVLQQAKDADIPVVS-YDrliLGSENVDYY 141
Cdd:cd01575    21 LSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTE--HTPATRKLLRAAGIPVVEtWD---LPDDPIDMA 95
                          90
                  ....*....|....*....
gi 1654132688 142 ASFDNEKVGELQGSYIVDK 160
Cdd:cd01575    96 VGFSNFAAGRAMARHLIER 114
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
81-160 6.25e-04

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


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 41.06  E-value: 6.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  81 DDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKDADIPVVSYD-RLILGSENVDY--YASFDNEKVGELQGSYI 157
Cdd:cd06312    41 NDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAINsGDDRSKERLGAltYVGQDEYLAGQAAGERA 120

                  ...
gi 1654132688 158 VDK 160
Cdd:cd06312   121 LEA 123
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
57-136 6.44e-04

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


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 41.09  E-value: 6.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  57 IADGanVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDNVLQQAKdaDIPVVSYDRLILGSE 136
Cdd:cd06280    17 IARG--IEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKH--GIPIVLIDREVEGLE 92
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
43-152 8.27e-04

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


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 40.72  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKSLDnvLQQAKDAD 122
Cdd:cd06293     1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSH--LARLRARG 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1654132688 123 IPVVSYDRLILGSE--NVdyyaSFDNEKVGEL 152
Cdd:cd06293    79 TAVVLLDRPAPGPAgcSV----SVDDVQGGAL 106
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
43-160 8.71e-04

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


Pssm-ID: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 40.73  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSE--RWIADGanVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIaAIDNKSLDNVLQQAKD 120
Cdd:cd06282     1 TIGVLIPSLNNPvfAEAAQG--IQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLIL-TVGDAQGSEALELLEE 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1654132688 121 ADIPVVsydrLILGSENVDYYA--SFDNEKVGELQGSYIVDK 160
Cdd:cd06282    78 EGVPYV----LLFNQTENSSHPfvSVDNRLASYDVAEYLIAL 115
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
43-267 2.64e-03

ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380630 [Multi-domain]  Cd Length: 269  Bit Score: 39.08  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMP----TKSSErwIADGanVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAI-DNKSLDNVLQQ 117
Cdd:cd19975     1 TIGVIIPdisnSFFAE--ILKG--IEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGtLTEENKQLLKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688 118 akdADIPVVsydrLILGSENVDYYASF--DNEkvgelQGSYIVDKLGLKAGKKgpfNIELFAGSNDDNNTKYF-FNGAMN 194
Cdd:cd19975    77 ---MNIPVV----LVSTESEDPDIPSVkiDDY-----QAAYDATNYLIKKGHR---KIAMISGPLDDPNAGYPrYEGYKK 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654132688 195 VLKpymDKGqLVVRSKQTALNqvtTLRWDGGTaqKRMDDLLTSSYrsaRVDAVLSPYDGISIGILSALKSDGY 267
Cdd:cd19975   142 ALK---DAG-LPIKENLIVEG---DFSFKSGY--QAMKRLLKNKK---LPTAVFAASDEMALGVISAAYDHGI 202
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
63-197 5.07e-03

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


Pssm-ID: 380507 [Multi-domain]  Cd Length: 267  Bit Score: 38.29  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  63 VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAaidNKSLDNVLQQAKDADIPVVsydrliLGSENVD--- 139
Cdd:cd06284    21 IEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILL---SGRLDAELLSELSKRYPIV------QCCEYIPdsg 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1654132688 140 -YYASFDNEKVGELQGSYIvdklgLKAGKKgpfNIELFAGSNDDNNTKYFFNGAMNVLK 197
Cdd:cd06284    92 vPSVSIDNEAAAYDATEYL-----ISLGHR---RIAHINGPLDNVYARERLEGYRRALA 142
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
43-162 5.89e-03

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


Pssm-ID: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 37.87  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654132688  43 TIGIAMPTKSSERWIADGANVEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIaaIDNKSLDNVLQQAKDAD 122
Cdd:cd06273     1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLIL--VGSDHDPELFELLEQRQ 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1654132688 123 IPVV---SYDRlilgsenVDYYAS--FDNEKVGELQGSYIVDkLG 162
Cdd:cd06273    79 VPYVltwSYDE-------DSPHPSigFDNRAAAARAAQHLLD-LG 115
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
63-130 8.13e-03

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: 380504 [Multi-domain]  Cd Length: 270  Bit Score: 37.60  E-value: 8.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654132688  63 VEKELKAKGYETKLVYGEDDPDQQVSQIENMITQGVDALIIAAIDNKslDNVLQQA-KDADIPVVSYDR 130
Cdd:cd06281    21 AEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDED--DPELAAAlARLDIPVVLIDR 87
 
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