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Conserved domains on  [gi|282586574|gb|EFB91827|]
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hypothetical protein HMPREF7215_1425 [Pyramidobacter piscolens W5455]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 39-318 1.46e-131

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: 376.28  E-value: 1.46e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  39 TVWFDAGGSVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMGHPGDDAYEPLIDEAFA 118
Cdd:cd19966    1 KIYFIPGGAPGDPFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTPLIEAAKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 119 KGMIVTCVDTALPRLQgkYQARGFGYVGTDNWRQGAEMAREILRRGGLKQGDRAFVWGLK-RLEGRGRRARALLEEFGKA 197
Cdd:cd19966   81 AGIIVTSFNTDLPKLE--YGDCGLGYVGADLYAAGYTLAKELVKRGGLKTGDRVFVPGLLpGQPYRVLRTKGVIDALKEA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 198 GLTVDYLEISDEINKdAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGVKPGEIYATGFSLTPATVGAIEAG 277
Cdd:cd19966  159 GIKVDYLEISLEPNK-PAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKKPGEIPVAGFDLSPATVQAIKSG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 282586574 278 YLNLTSEAQPYLMGYLSVLQIVNTAKYKFGGLNVDTGGGYI 318
Cdd:cd19966  238 YVNATIDQQPYLQGYLPVLQIYLTKKYGFSGLDIDTGGGYV 278
 
Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 39-318 1.46e-131

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: 376.28  E-value: 1.46e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  39 TVWFDAGGSVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMGHPGDDAYEPLIDEAFA 118
Cdd:cd19966    1 KIYFIPGGAPGDPFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTPLIEAAKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 119 KGMIVTCVDTALPRLQgkYQARGFGYVGTDNWRQGAEMAREILRRGGLKQGDRAFVWGLK-RLEGRGRRARALLEEFGKA 197
Cdd:cd19966   81 AGIIVTSFNTDLPKLE--YGDCGLGYVGADLYAAGYTLAKELVKRGGLKTGDRVFVPGLLpGQPYRVLRTKGVIDALKEA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 198 GLTVDYLEISDEINKdAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGVKPGEIYATGFSLTPATVGAIEAG 277
Cdd:cd19966  159 GIKVDYLEISLEPNK-PAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKKPGEIPVAGFDLSPATVQAIKSG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 282586574 278 YLNLTSEAQPYLMGYLSVLQIVNTAKYKFGGLNVDTGGGYI 318
Cdd:cd19966  238 YVNATIDQQPYLQGYLPVLQIYLTKKYGFSGLDIDTGGGYV 278
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 24-323 9.58e-31

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: 118.10  E-value: 9.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  24 GSAGASEMAQSGKGMTVWFdAGGSVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMgh 103
Cdd:COG1879   20 GSAAAEAAAAAAKGKTIGF-VVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVS-- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 104 PGD-DAYEPLIDEAFAKGMIVTCVDTALPrlqgkyQARGFGYVGTDNWRQGAEMAREILRRGGlKQGDRAFVWGLKRLEG 182
Cdd:COG1879   97 PVDpDALAPALKKAKAAGIPVVTVDSDVD------GSDRVAYVGSDNYAAGRLAAEYLAKALG-GKGKVAILTGSPGAPA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 183 RGRRARALLEEFGKA-GLTVDYLEISDEinkDAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGvKPGEIYA 261
Cdd:COG1879  170 ANERTDGFKEALKEYpGIKVVAEQYADW---DREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAG-RKGDVKV 245

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282586574 262 TGFSLTPATVGAIEAGYLNLTSEAQPYLMGYLSVLQIVNTAKYKFGGLNVDTGGGYISQDNI 323
Cdd:COG1879  246 VGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 47-300 1.66e-20

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: 89.29  E-value: 1.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574   47 SVGEPYATTVVNGAKQAAIDLGVDLKIV-YSDWNPEKMLENFKTGLAANPTGFVVmgHPGD-DAYEPLIDEAFAKGMIVT 124
Cdd:pfam13407   7 STGNPFFQAAEEGAEEAAKELGGEVIVVgPAEADAAEQVAQIEDAIAQGVDAIIV--APVDpTALAPVLKKAKDAGIPVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  125 CVDTALPrlqgkyQARGFGYVGTDNWRQGAEMAREILRRGGlKQGDRAFVWGLKRLEGRGRRARALLEEFGKAGLTVDYL 204
Cdd:pfam13407  85 TFDSDAP------SSPRLAYVGFDNEAAGEAAGELLAEALG-GKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  205 EISDEINKDAALGAPVLSGYLASHPD-CKVIVVDHGGLTGQLGNFLRAAGVKpGEIYATGFSLTPATVGAIEAGYLNLTS 283
Cdd:pfam13407 158 AEVEGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLA-GKVVVTGFDATPEALEAIKDGTIDATV 236

                         250
                  ....*....|....*..
gi 282586574  284 EAQPYLMGYLSVLQIVN 300
Cdd:pfam13407 237 LQDPYGQGYAAVELAAA 253
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
25-295 6.96e-04

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 40.84  E-value: 6.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  25 SAGASEMAQSGKGMTVwfdagGSVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFK-------TGLAANPTG 97
Cdd:PRK10653  18 TVSANAMAKDTIALVV-----STLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQdltvrgtKILLINPTD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  98 FVVMGHP---GDDAYEPLI--DEAFAKGMIVTcvdtalprlqgkyqargfgYVGTDNwRQGAEMAREILRRgglKQGDRA 172
Cdd:PRK10653  93 SDAVGNAvkmANQANIPVItlDRGATKGEVVS-------------------HIASDN-VAGGKMAGDFIAK---KLGEGA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 173 FVWGLKRLEGRGrRARALLEEFGKAGLTVDY-LEISDEINKDAALGAPVLSGYLASHPDCKVIVVDHGGLTgqLGNF--L 249
Cdd:PRK10653 150 KVIQLEGIAGTS-AARERGEGFKQAVAAHKFnVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMA--LGALraL 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 282586574 250 RAAGvkPGEIYATGFSLTPATVGAIEAGYLNLTSEAQPYLMGYLSV 295
Cdd:PRK10653 227 QTAG--KSDVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGV 270
 
Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 39-318 1.46e-131

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: 376.28  E-value: 1.46e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  39 TVWFDAGGSVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMGHPGDDAYEPLIDEAFA 118
Cdd:cd19966    1 KIYFIPGGAPGDPFWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTPLIEAAKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 119 KGMIVTCVDTALPRLQgkYQARGFGYVGTDNWRQGAEMAREILRRGGLKQGDRAFVWGLK-RLEGRGRRARALLEEFGKA 197
Cdd:cd19966   81 AGIIVTSFNTDLPKLE--YGDCGLGYVGADLYAAGYTLAKELVKRGGLKTGDRVFVPGLLpGQPYRVLRTKGVIDALKEA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 198 GLTVDYLEISDEINKdAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGVKPGEIYATGFSLTPATVGAIEAG 277
Cdd:cd19966  159 GIKVDYLEISLEPNK-PAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKKPGEIPVAGFDLSPATVQAIKSG 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 282586574 278 YLNLTSEAQPYLMGYLSVLQIVNTAKYKFGGLNVDTGGGYI 318
Cdd:cd19966  238 YVNATIDQQPYLQGYLPVLQIYLTKKYGFSGLDIDTGGGYV 278
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 24-323 9.58e-31

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: 118.10  E-value: 9.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  24 GSAGASEMAQSGKGMTVWFdAGGSVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMgh 103
Cdd:COG1879   20 GSAAAEAAAAAAKGKTIGF-VVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVS-- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 104 PGD-DAYEPLIDEAFAKGMIVTCVDTALPrlqgkyQARGFGYVGTDNWRQGAEMAREILRRGGlKQGDRAFVWGLKRLEG 182
Cdd:COG1879   97 PVDpDALAPALKKAKAAGIPVVTVDSDVD------GSDRVAYVGSDNYAAGRLAAEYLAKALG-GKGKVAILTGSPGAPA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 183 RGRRARALLEEFGKA-GLTVDYLEISDEinkDAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGvKPGEIYA 261
Cdd:COG1879  170 ANERTDGFKEALKEYpGIKVVAEQYADW---DREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAG-RKGDVKV 245

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282586574 262 TGFSLTPATVGAIEAGYLNLTSEAQPYLMGYLSVLQIVNTAKYKFGGLNVDTGGGYISQDNI 323
Cdd:COG1879  246 VGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 49-318 5.77e-30

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: 115.06  E-value: 5.77e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  49 GEPYATTVVNGAKQAAIDLGVDLKIVYS-DWNPEKMLENFKTGLAANPTGFVVMgHPGDDAYEPLIDEAFAKGMIVTCVD 127
Cdd:cd19965   10 TNPFFQPVKKGMDDACELLGAECQFTGPqTFDVAEQVSLLEAAIASGPDGIATT-IVDPEAFDEVIKRALDAGIPVVAFN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 128 TALPrlqgKYQARGFGYVGTDNWRQGAEMAREILRrgGLKQGDRAFVWGLKR-----LEGRGRRARALLEEFGKaGLTVD 202
Cdd:cd19965   89 VDAP----GGENARLAFVGQDLYPAGYVLGKRIAE--KFKPGGGHVLLGISTpgqsaLEQRLDGIKQALKEYGR-GITYD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 203 YLEISDeinkDAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGVkPGEIYATGFSLTPATVGAIEAGYLNLT 282
Cdd:cd19965  162 VIDTGT----DLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGL-KGKVLVGGFDLVPEVLQGIKAGYIDFT 236

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 282586574 283 SEAQPYLMGYLSVLQIVNTAKYKFGGLNVDTGGGYI 318
Cdd:cd19965  237 IDQQPYLQGFYPVMQLFLYKKFGLSPFDIDTGAAVV 272
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 45-318 1.02e-24

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: 100.77  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  45 GGSVGEPYATTVVNGAKQAAIDLGVDLKIVYS-DWNPEKMLENFKTGLAANPTGFVVmGHPGDDAYEPLIDEAFAKGMIV 123
Cdd:cd06312    7 HGSPSDPFWSVVKKGAKDAAKDLGVTVQYLGPqNNDIADQARLIEQAIAAKPDGIIV-TIPDPDALEPALKRAVAAGIPV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 124 TCVDTALPRLQGKYQArgFGYVGTDNWRQGAEMAREILRRGGlkqgdRAFVW-----GLKRLEgrgRRARALLEEFGKAG 198
Cdd:cd06312   86 IAINSGDDRSKERLGA--LTYVGQDEYLAGQAAGERALEAGP-----KNALCvnhepGNPGLE---ARCKGFADAFKGAG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 199 LTVDYLEISDeiNKDAALGApvLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGVKpGEIYATGFSLTPATVGAIEAGY 278
Cdd:cd06312  156 ILVELLDVGG--DPTEAQEA--IKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLK-GKVKIGTFDLSPETLEAIKDGK 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 282586574 279 LNLTSEAQPYLMGYLSVLQIVNTAKYKF--GGLNVDTGGGYI 318
Cdd:cd06312  231 ILFAIDQQPYLQGYLAVVFLYLYKRYGTlpPPEPILTGPGFV 272
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 47-314 2.02e-24

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: 99.95  E-value: 2.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  47 SVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVmgHPGD-DAYEPLIDEAFAKGMIVTC 125
Cdd:cd01536    8 DLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIII--APVDsEALVPAVKKANAAGIPVVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 126 VDTALPrLQGKYQArgfgYVGTDNWRQGAEMAREILRR--GGLK----QGDRAFVWGLKRLEGrgrrARALLEEFGKagl 199
Cdd:cd01536   86 VDTDID-GGGDVVA----FVGTDNYEAGKLAGEYLAEAlgGKGKvailEGPPGSSTAIDRTKG----FKEALKKYPD--- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 200 tvdyLEISDEI--NKDAALGAPVLSGYLASHPDCKVIVVDHGGLTgqLG--NFLRAAGvKPGEIYATGFSLTPATVGAIE 275
Cdd:cd01536  154 ----IEIVAEQpaNWDRAKALTVTENLLQANPDIDAVFAANDDMA--LGaaEALKAAG-RTGDIKIVGVDGTPEALKAIK 226

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 282586574 276 AGYLNLTSEAQPYLMGYLSVLQIVNTAKYKFGGLNVDTG 314
Cdd:cd01536  227 DGELDATVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTP 265
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 47-300 1.66e-20

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: 89.29  E-value: 1.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574   47 SVGEPYATTVVNGAKQAAIDLGVDLKIV-YSDWNPEKMLENFKTGLAANPTGFVVmgHPGD-DAYEPLIDEAFAKGMIVT 124
Cdd:pfam13407   7 STGNPFFQAAEEGAEEAAKELGGEVIVVgPAEADAAEQVAQIEDAIAQGVDAIIV--APVDpTALAPVLKKAKDAGIPVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  125 CVDTALPrlqgkyQARGFGYVGTDNWRQGAEMAREILRRGGlKQGDRAFVWGLKRLEGRGRRARALLEEFGKAGLTVDYL 204
Cdd:pfam13407  85 TFDSDAP------SSPRLAYVGFDNEAAGEAAGELLAEALG-GKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  205 EISDEINKDAALGAPVLSGYLASHPD-CKVIVVDHGGLTGQLGNFLRAAGVKpGEIYATGFSLTPATVGAIEAGYLNLTS 283
Cdd:pfam13407 158 AEVEGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLA-GKVVVTGFDATPEALEAIKDGTIDATV 236

                         250
                  ....*....|....*..
gi 282586574  284 EAQPYLMGYLSVLQIVN 300
Cdd:pfam13407 237 LQDPYGQGYAAVELAAA 253
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 47-305 1.16e-16

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: 78.39  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  47 SVGEPYATTVVNGAKQAAIDLGVDLKIVYS-DWNPEKMLENFKTGLAANPTGFVVMghPGD-DAYEPLIDEAFAKGMIVT 124
Cdd:cd06314    8 GLNNPFWDLAEAGAEKAAKELGVNVEFVGPqKSDAAEQVQLIEDLIARGVDGIAIS--PNDpEAVTPVINKAADKGIPVI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 125 CVDTALPrlqgkyQARGFGYVGTDNWRQGAEMAREILRRGGlKQGDRAFVWGLKRLEGRGRRARALLEEF-GKAGLTVdy 203
Cdd:cd06314   86 TFDSDAP------DSKRLAYIGTDNYEAGREAGELMKKALP-GGGKVAIITGGLGADNLNERIQGFKDALkGSPGIEI-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 204 LEIsDEINKDAALGAPVLSGYLASHPDCKVIVvdhggLTGQLGNFLRAAGV----KPGEIYATGFSLTPATVGAIEAGYL 279
Cdd:cd06314  157 VDP-LSDNDDIAKAVQNVEDILKANPDLDAIF-----GVGAYNGPAIAAALkdagKVGKVKIVGFDTLPETLQGIKDGVI 230

                        250       260
                 ....*....|....*....|....*.
gi 282586574 280 NLTSEAQPYLMGYLSVLQIVNTAKYK 305
Cdd:cd06314  231 AATVGQRPYEMGYLSVKLLYKLLKGG 256
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
 48-296 8.26e-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: 380624 [Multi-domain]  Cd Length: 278  Bit Score: 73.53  E-value: 8.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  48 VGEPYATTVVNGAKQAAIDLGVdlKIVYS---DWNPEKMLENFKTGLAANPTGFVVmgHPGD-DAYEPLIDEAFAKGMIV 123
Cdd:cd19969    9 SGHPYWDDVKEGFEDAGAELGV--KTEYTgpaTADVNEQITAIEQAIAKNPDGIAV--SAIDpEALTPTINKAVDAGIPV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 124 TCVDTALPrlqgkyQARGFGYVGTDNWRQGAEMAREILRRGGlKQGDRAfVWGLKRLEGRGRRARALLEEF-GKAGLTVd 202
Cdd:cd19969   85 VTFDSDAP------ESKRISYVGTDNYEAGYAAAEKLAELLG-GKGKVA-VLTGPGQPNHEERVEGFKEAFaEYPGIEV- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 203 YLEISDEINKDAAlgAPVLSGYLASHPDCKVIV-VDHGGLTGqLGNFLRAAGvKPGEIYATGFSLTPATVGAIEAGYLNL 281
Cdd:cd19969  156 VAVGDDNDDPEKA--AQNTSALLQAHPDLVGIFgVDASGGVG-AAQAVREAG-KTGKVKIVAFDDDPETLDLIKDGVIDA 231

                        250
                 ....*....|....*
gi 282586574 282 TSEAQPYLMGYLSVL 296
Cdd:cd19969  232 SIAQRPWMMGYWSLQ 246
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 47-314 2.74e-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: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 68.80  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  47 SVGEPYATTVVNGAKQAAIDLGVDLKIV----YSDWNPEK-MLENFktgLAANPTGfVVMGHPGDDAYEPlIDEAFAKGM 121
Cdd:cd20008    8 DTDSEYWQTVLKGAEKAAKELGVEVTFLgpatEADIAGQVnLVENA---ISRKPDA-IVLAPNDTAALVP-AVEAADAGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 122 IVTCVDTALPrlQGKYQArgfgYVGTDNWRQGAEMAREI---LRRGGLKQGDRA---FVWGLKRLEGRgrraralLEEFg 195
Cdd:cd20008   83 PVVLVDSGAN--TDDYDA----FLATDNVAAGALAADELaelLKASGGGKGKVAiisFQAGSQTLVDR-------EEGF- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 196 kagltVDYL-EISDEI--------NKDAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGvKPGEIYATGFSL 266
Cdd:cd20008  149 -----RDYIkEKYPDIeivdvqysDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAG-KAGKIVLVGFDS 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 282586574 267 TPATVGAIEAGYLNLTSEAQPYLMGYLSVLQIVNTAK-YKFGGLNVDTG 314
Cdd:cd20008  223 SPDEVALLKSGVIKALVVQDPYQMGYEGVKTAVKALKgEEIVEKNVDTG 271
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 52-314 7.03e-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: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 67.75  E-value: 7.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  52 YATTVVNGAKQAAIDLGVDLKIVY--SDWNPE---KMLENFktgLAANPTGFVVMGHPGDDAYEPLiDEAFAKGMIVTCV 126
Cdd:cd06310   13 FWRTVREGAEAAAKDLGVKIIFVGpeSEEDVAgqnSLLEEL---INKKPDAIVVAPLDSEDLVDPL-KDAKDKGIPVIVI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 127 DTALprlqgkYQARGFGYVGTDNwRQGAEMAREILRRGGLKQGDRAFVWGLKRLEGRGRRARALLEEFGKAGLTVDYLEi 206
Cdd:cd06310   89 DSGI------KGDAYLSYIATDN-YAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIKVLA- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 207 SDEINKDAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGVKpGEIYATGFSLTPATVGAIEAGYLNLTSEAQ 286
Cdd:cd06310  161 SQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLS-GQIKIVGFDSQEELLDALKNGKIDALVVQN 239

                        250       260
                 ....*....|....*....|....*...
gi 282586574 287 PYLMGYLSVLQIVNTAKYKFGGLNVDTG 314
Cdd:cd06310  240 PYEIGYEGIKLALKLLKGEEVPKNIDTG 267
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 46-300 1.44e-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: 380662 [Multi-domain]  Cd Length: 271  Bit Score: 66.88  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  46 GSVGEPYATTVVNGAKQAAIDLGVDLKIV-YSDWNPEKMLENFKTGLAANPTGFVVMghPGDDA--YEPLiDEAFAKGMI 122
Cdd:cd20007    7 GVTGDPFYITMQCGAEAAAKELGVELDVQgPPTFDPTLQTPIVNAVIAKKPDALLIA--PTDPQalIAPL-KRAADAGIK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 123 VTCVDTALprlqgkyQARGF--GYVGTDNWRQGAEMAREILRRGGlKQGDRAFVWGLKRLEGRGRRARALLEEFGKA-GL 199
Cdd:cd20007   84 VVTVDTTL-------GDPSFvlSQIASDNVAGGALAAEALAELIG-GKGKVLVINSTPGVSTTDARVKGFAEEMKKYpGI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 200 TVDYLEISDEinkDAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGvKPGEIYATGFSLTPATVGAIEAGYL 279
Cdd:cd20007  156 KVLGVQYSEN---DPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAG-KTGKVKVVGFDASPAQVEQLKAGTI 231

                        250       260
                 ....*....|....*....|.
gi 282586574 280 NLTSEAQPYLMGYLSVLQIVN 300
Cdd:cd20007  232 DALIAQKPAEIGYLAVEQAVA 252
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 55-314 9.51e-11

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 61.46  E-value: 9.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  55 TVVNGAKQAAIDLGVDLKIV--YSDWNPEKMLENFKTGLAANPTGFVVMghPGD-DAYEPLIDEAFAKGMIVTCVDTALP 131
Cdd:cd20006   18 TVKSGAEAAAKEYGVDLEFLgpESEEDIDGQIELIEEAIAQKPDAIVLA--ASDyDRLVEAVERAKKAGIPVITIDSPVN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 132 rlqgkyQARGFGYVGTDNWRQGAEMAREILRRGGlKQGDRAFVWGLKRLEGRGRRARALLEEFGKAG-LTVDYLEISDEI 210
Cdd:cd20006   96 ------SKKADSFVATDNYEAGKKAGEKLASLLG-EKGKVAIVSFVKGSSTAIEREEGFKQALAEYPnIKIVETEYCDSD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 211 NKDAALGAPVLsgyLASHPDCKVIVVDHGGLTGQLGNFLRAAGVKpGEIYATGFSLTPATVGAIEAGYLNLTSEAQPYLM 290
Cdd:cd20006  169 EEKAYEITKEL---LSKYPDINGIVALNEQSTLGAARALKELGLG-GKVKVVGFDSSVEEIQLLEEGIIDALVVQNPFNM 244

                        250       260
                 ....*....|....*....|....
gi 282586574 291 GYLSVLQIVNTAKYKFGGLNVDTG 314
Cdd:cd20006  245 GYLSVQAAVDLLNGKKIPKRIDTG 268
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
47-295 3.34e-10

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 60.21  E-value: 3.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  47 SVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMGHPGDDayePLIDEAFAKGMIVTCV 126
Cdd:COG1609   70 DLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDD---ARLERLAEAGIPVVLI 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 127 DTALPRLqgkyqarGFGYVGTDNwRQGAEMAREILrrggLKQGDR--AFVWGLKRLEGRGRRARALLEEFGKAGLTVDYL 204
Cdd:COG1609  147 DRPLPDP-------GVPSVGVDN-RAGARLATEHL----IELGHRriAFIGGPADSSSARERLAGYREALAEAGLPPDPE 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 205 EIsDEINKDAALGAPVLSGYLASHPDCKVIVV--DH---GGLTGqlgnfLRAAGVK-PGEIYATGFSLTPatvgaiEAGY 278
Cdd:COG1609  215 LV-VEGDFSAESGYEAARRLLARGPRPTAIFCanDLmalGALRA-----LREAGLRvPEDVSVVGFDDIP------LARY 282

                        250       260
                 ....*....|....*....|
gi 282586574 279 LN--LTSEAQP-YLMGYLSV 295
Cdd:COG1609  283 LTppLTTVRQPiEEMGRRAA 302
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 51-295 4.80e-10

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: 59.23  E-value: 4.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  51 PYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTgLAANPTGFVVMGHPGDDAYEPLIDEAFAKGMIVTCVDTAL 130
Cdd:cd06323   12 PFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVED-LIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 131 PrlqgkyQARGFGYVGTDNwRQGAEMAREILRRgglKQGDRAFVWGLKRLEG------RGRRARALLEEFGK----AGLT 200
Cdd:cd06323   91 T------GGKVVSHIASDN-VAGGEMAAEYIAK---KLGGKGKVVELQGIPGtsaareRGKGFHNAIAKYPKinvvASQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 201 VDYleisdeinkDAALGAPVLSGYLASHPDCKViVVDHGGLTGqLGNfLRAAG-VKPGEIYATGFSLTPATVGAIEAGYL 279
Cdd:cd06323  161 ADF---------DRTKGLNVMENLLQAHPDIDA-VFAHNDEMA-LGA-IQALKaAGRKDVIVVGFDGTPDAVKAVKDGKL 228

                        250
                 ....*....|....*.
gi 282586574 280 NLTSEAQPYLMGYLSV 295
Cdd:cd06323  229 AATVAQQPEEMGAKAV 244
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 51-297 1.09e-08

D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 55.41  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  51 PYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGfVVMGHPGDDAYEPLIDEAFAKGMIVTCVDTAL 130
Cdd:cd19967   12 PFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKA-IILDPADADASIAAVKKAKDAGIPVFLIDREI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 131 PRlQGKYQARgfgyVGTDNWRQGAEMAREILRRGGlKQGDRAFVWGLKRLEGRGRRARALLEefgkaglTVD-YLEI--- 206
Cdd:cd19967   91 NA-EGVAVAQ----IVSDNYQGAVLLAQYFVKLMG-EKGLYVELLGKESDTNAQLRSQGFHS-------VIDqYPELkmv 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 207 -SDEINKDAALGAPVLSGYLASHPDCKVIVVdhGGLTGQLGNF--LRAAGvKPGEIYATGFSLTPATVGAIEAGYLNLTS 283
Cdd:cd19967  158 aQQSADWDRTEAFEKMESILQANPDIKGVIC--GNDEMALGAIaaLKAAG-RAGDVIIVGFDGSNDVRDAIKEGKISATV 234

                        250
                 ....*....|....
gi 282586574 284 EAQPYLMGYLSVLQ 297
Cdd:cd19967  235 LQPAKLIARLAVEQ 248
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 52-303 2.22e-08

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


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 54.30  E-value: 2.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  52 YATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMghPGD-DAYEPLIDEAFAKGMIVTCVDTAL 130
Cdd:cd06317   13 FFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILD--AIDvNGSIPAIKRASEAGIPVIAYDAVI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 131 PRlqgKYQArgfGYVGTDNWRQGAEMAREILRRGGLKQGDRA--FVWGLKRLEGRGRRARALLEEFgKAGLTVDYLEISD 208
Cdd:cd06317   91 PS---DFQA---AQVGVDNLEGGKEIGKYAADYIKAELGGQAkiGVVGALSSLIQNQRQKGFEEAL-KANPGVEIVATVD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 209 EIN-KDAALGAPvlSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGvKPGEIYATGFSLTP-ATVGAIEAGYLNLTSEAQ 286
Cdd:cd06317  164 GQNvQEKALSAA--ENLLTANPDLDAIYATGEPALLGAVAAVRSQG-RQGKIKVFGWDLTKqAIFLGIDEGVLQAVVQQD 240

                        250
                 ....*....|....*..
gi 282586574 287 PYLMGYLSVLQIVNTAK 303
Cdd:cd06317  241 PEKMGYEAVKAAVKAIK 257
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 51-313 2.75e-08

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


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 54.29  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  51 PYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVmgHPGD-DAYEPLIDEAFAKGMIVTCVDTA 129
Cdd:cd06319   12 PFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIII--SPTNsSAAPTVLDLANEAKIPVVIADIG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 130 LprlQGKYQArgfGYVGTDNW---RQGAEMAREILRRGGLKQGDRAFV-WGLKRLEGRgRRARALLEEFGKAGLTVDYLE 205
Cdd:cd06319   90 T---GGGDYV---SYIISDNYdggYQAGEYLAEALKENGWGGGSVGIIaIPQSRVNGQ-ARTAGFEDALEEAGVEEVALR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 206 ISDEINKDAALGApvLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGVKpGEIYATGFSLTPATVGAIEAGYLNLTSEA 285
Cdd:cd06319  163 QTPNSTVEETYSA--AQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT-GDILVVGFDGDPEALDLIKDGKLDGTVAQ 239

                        250       260
                 ....*....|....*....|....*...
gi 282586574 286 QPYLMGYLSvlqiVNTAKYKFGGLNVDT 313
Cdd:cd06319  240 QPFGMGARA----VELAIQALNGDNTVE 263
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 52-321 6.71e-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: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 53.02  E-value: 6.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  52 YATTVVNGAKQAAIDLGVdlKIVYSdwNPEK---------MLENfktGLAANPTGfVVMGHPGDDAYEPLIDEAFAKGMI 122
Cdd:cd20005   13 FWKAVKKGAEQAAKELGV--KITFE--GPDTesdvdkqieMLDN---AIAKKPDA-IALAALDTNALLPQLEKAKEKGIP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 123 VTCVDTALPrlQGKYQArgfgYVGTDNWRQGAEMAREILRRGGlKQGDRAFV---WGLKRLEGRGRRARALLEEFGKAGL 199
Cdd:cd20005   85 VVTFDSGVP--SDLPLA----TVATDNYAAGALAADHLAELIG-GKGKVAIVahdATSETGIDRRDGFKDEIKEKYPDIK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 200 TVDYLEISDEINKDAAlgapVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGVKpGEIYATGFSLTPATVGAIEAGYL 279
Cdd:cd20005  158 VVNVQYGVGDHAKAAD----IAKAILQANPDLKGIYATNEGAAIGVANALKEMGKL-GKIKVVGFDSGEAQIDAIKNGVI 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 282586574 280 nLTSEAQ-PYLMGYLSVLQIVNTAKYKFGGLNVDTGGGYISQD 321
Cdd:cd20005  233 -AGSVTQnPYGMGYKTVKAAVKALKGEEVEKLIDTGAKWYDKD 274
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
 113-305 7.47e-08

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


Pssm-ID: 380530 [Multi-domain]  Cd Length: 275  Bit Score: 52.95  E-value: 7.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 113 IDEAFAKGMIVTCVDTALPrlqgkyQARGFGYVGTDNWRQG---AE-MAREILRRGglkqGDRAFVWGLKRLEG-RGRRA 187
Cdd:cd06307   76 IDELAARGIPVVTLVSDLP------GSRRLAYVGIDNRAAGrtaAWlMGRFLGRRP----GKVLVILGSHRFRGhEEREA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 188 --RALLEEFGKaGLTVdyLEISdEINKDAALGAPVLSGYLASHPDCKVIVVDHGGLTGqLGNFLRAAGvKPGEIYATGFS 265
Cdd:cd06307  146 gfRSVLRERFP-DLTV--LEVL-EGLDDDELAYELLRELLARHPDLVGIYNAGGGNEG-IARALREAG-RARRVVFIGHE 219

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 282586574 266 LTPATVGAIEAGYLNLTSEAQPYLMGYLSVLQIVNTAKYK 305
Cdd:cd06307  220 LTPETRRLLRDGTIDAVIDQDPELQARRAIEVLLAHLGGK 259
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 51-202 1.43e-06

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: 48.67  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  51 PYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMGHPGDDayePLIDEAFAKGMIVTCVDTAL 130
Cdd:cd06267   12 PFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDD---ELLEELLAAGIPVVLIDRRL 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282586574 131 PRLqgkyqarGFGYVGTDNwRQGAEMAREILrrggLKQGDR--AFVWGLKRLEGRGRRARALLEEFGKAGLTVD 202
Cdd:cd06267   89 DGL-------GVDSVVVDN-YAGAYLATEHL----IELGHRriAFIGGPLDLSTSRERLEGYRDALAEAGLPVD 150
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 46-277 1.80e-06

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


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 48.75  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  46 GSVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAAN--PTGFVVMGHPGddAYEPLIDEAFAKG--- 120
Cdd:cd06324    8 GKEDEPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARPpkPDYLILVNEKG--VAPELLELAEQAKipv 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 121 -MIVTCVDTALPRLQGKYQARGFGYVGT---DNWRQGAEMAREILRRGGLKQ-----------GDRAFVWGLKRLEGrgr 185
Cdd:cd06324   86 fLINNDLTDEERALLGKPREKFKYWLGSivpDNEQAGYLLAKALIKAARKKSddgkirvlaisGDKSTPASILREQG--- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 186 rARALLEEFGKAGLTvdyleisDEINKD--AALGAPVLSGYLASHPDCKVI-----VVDHGGLTGqlgnfLRAAGVKPGE 258
Cdd:cd06324  163 -LRDALAEHPDVTLL-------QIVYANwsEDEAYQKTEKLLQRYPDIDIVwaandAMALGAIDA-----LEEAGLKPGK 229

                        250       260
                 ....*....|....*....|
gi 282586574 259 -IYATGFSLTPATVGAIEAG 277
Cdd:cd06324  230 dVLVGGIDWSPEALQAVKDG 249
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 51-314 1.06e-05

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


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 46.46  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  51 PYATTVVNGAKQAAIDLGVdlKIVY----SDWNPE---KMLENFktgLAANPTGFVVMghPGDD-AYEPLIDEAFAKGMI 122
Cdd:cd20004   12 DFWKSVKAGAEKAAQELGV--EIYWrgpsREDDVEaqiQIIEYF---IDQGVDGIVLA--PLDRkALVAPVERARAQGIP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 123 VTCVDTALprlqGKYQARGfgYVGTDNWRQGAEMAREILrrgglkqgdrafvwglKRLEGRGR---------------RA 187
Cdd:cd20004   85 VVIIDSDL----GGDAVIS--FVATDNYAAGRLAAKRMA----------------KLLNGKGKvallrlakgsasttdRE 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 188 RALLEEFGKA--GLTVD---YLEISDEINKDAAlgAPVLSgylaSHPDCKVIV-VDHGGLTGQLgNFLRAAGvKPGEIYA 261
Cdd:cd20004  143 RGFLEALKKLapGLKVVddqYAGGTVGEARSSA--ENLLN----QYPDVDGIFtPNESTTIGAL-RALRRLG-LAGKVKF 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 282586574 262 TGFSLTPATVGAIEAGYLNLTSEAQPYLMGYLSVLQIVNTAKYKFGGLNVDTG 314
Cdd:cd20004  215 IGFDASDLLLDALRAGEISALVVQDPYRMGYLGVKTAVAALRGKPVPKRIDTG 267
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 51-322 2.98e-05

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: 45.09  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  51 PYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTgLAANPTGFVVMGHPGDDAYEPLIDEAFAKGMIVTCVDTAL 130
Cdd:cd06318   12 PYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVED-LITRGVDVLILNPVDPEGLTPAVKAAKAAGIPVITVDSAL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 131 prlqgKYQARGFGYVGTDNWRQGAEMAREILRRGGLKQGDRAFVWGLK-RLEGRGRR-------ARALLEEFGKAGLTV- 201
Cdd:cd06318   91 -----DPSANVATQVGRDNKQNGVLVGKEAAKALGGDPGKIIELSGDKgNEVSRDRRdgflagvNEYQLRKYGKSNIKVv 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 202 --DYleisDEINKDAALGApvLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGvKPGEIYATGFSLTPATVGAIEAGYL 279
Cdd:cd06318  166 aqPY----GNWIRSGAVAA--MEDLLQAHPDINVVYAENDDMALGAMKALKAAG-MLDKVKVAGADGQKEALKLIKDGKY 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 282586574 280 NLTSEAQPYLMGYLSVLQIVNTAK--YKFGGLNvDTGGGYISQDN 322
Cdd:cd06318  239 VATGLNDPDLLGKTAVDTAAKVVKgeESFPEFT-YTPTALITKDN 282
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 51-295 3.40e-05

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: 44.95  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  51 PYATTVVNGAKQAAIDLGVDLKI--VYSDWNPEKMLENFKTGLAANPTGFVVMghP-GDDAYEPLIDEAFAKGMIVTCVD 127
Cdd:cd06320   12 PFWVAMKDGIEAEAKKLGVKVDVqaAPSETDTQGQLNLLETMLNKGYDAILVS--PiSDTNLIPPIEKANKKGIPVINLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 128 TALprLQGKYQARGF---GYVGTDNWRQGAEMAREILRRGGlKQGDRAFVWGL---KRLEGRGRRARALLEEFGK----A 197
Cdd:cd06320   90 DAV--DADALKKAGGkvtSFIGTDNVAAGALAAEYIAEKLP-GGGKVAIIEGLpgnAAAEARTKGFKETFKKAPGlklvA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 198 GLTVDYleisdeinkDAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGvKPGEIYATGFSLTPATVGAIEAG 277
Cdd:cd06320  167 SQPADW---------DRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAG-KTGKVLVVGTDGIPEAKKSIKAG 236

                        250
                 ....*....|....*...
gi 282586574 278 YLNLTSEAQPYLMGYLSV 295
Cdd:cd06320  237 ELTATVAQYPYLEGAMAV 254
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 51-308 3.70e-05

periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 44.52  E-value: 3.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  51 PYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMghPGDD-AYEPLIDEAFAKGMIVTCVDTA 129
Cdd:cd06309   12 PWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILIS--PIDAtGWDPVLKEAKDAGIPVILVDRT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 130 LPRLQGKYQArgfGYVGTDNWRQGAEMAREILRRGGLKQGDRAFVWGLKRL---EGRGRRARALLEEFGKagltvdyLEI 206
Cdd:cd06309   90 IDGEDGSLYV---TFIGSDFVEEGRRAAEWLVKNYKGGKGNVVELQGTAGSsvaIDRSKGFREVIKKHPN-------IKI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 207 SDEINKD--AALGAPVLSGYLASHPDCKVIVVDH------GGLTGqlgnfLRAAGVKPGE-IYATGFSLTPATVGAIEAG 277
Cdd:cd06309  160 VASQSGNftREKGQKVMENLLQAGPGDIDVIYAHnddmalGAIQA-----LKEAGLKPGKdVLVVGIDGQKDALEAIKAG 234

                        250       260       270
                 ....*....|....*....|....*....|.
gi 282586574 278 YLNLTSEAQPYlMGYlsvlQIVNTAKYKFGG 308
Cdd:cd06309  235 ELNATVECNPL-FGP----TAFDTIAKLLAG 260
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 50-237 4.54e-05

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: 44.42  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574   50 EPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMGhPGDDAYEPLIDEAFAKGMIVTCVDTA 129
Cdd:pfam00532  13 EPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITT-PAPSGDDITAKAEGYGIPVIAADDAF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  130 lprlqgkYQARGFGYVGTDNWRQGAEMAREILRRGglKQGDRAFVWGLKRLEGRGRRA---RALLEEFGKAGLTVDYLEI 206
Cdd:pfam00532  92 -------DNPDGVPCVMPDDTQAGYESTQYLIAEG--HKRPIAVMAGPASALTARERVqgfMAALAAAGREVKIYHVATG 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 282586574  207 SDEINkDAALGAPVLsgyLASHPDCKVIVVD 237
Cdd:pfam00532 163 DNDIP-DAALAANAM---LVSHPTIDAIVAM 189
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
25-295 6.96e-04

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 40.84  E-value: 6.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  25 SAGASEMAQSGKGMTVwfdagGSVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFK-------TGLAANPTG 97
Cdd:PRK10653  18 TVSANAMAKDTIALVV-----STLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQdltvrgtKILLINPTD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  98 FVVMGHP---GDDAYEPLI--DEAFAKGMIVTcvdtalprlqgkyqargfgYVGTDNwRQGAEMAREILRRgglKQGDRA 172
Cdd:PRK10653  93 SDAVGNAvkmANQANIPVItlDRGATKGEVVS-------------------HIASDN-VAGGKMAGDFIAK---KLGEGA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 173 FVWGLKRLEGRGrRARALLEEFGKAGLTVDY-LEISDEINKDAALGAPVLSGYLASHPDCKVIVVDHGGLTgqLGNF--L 249
Cdd:PRK10653 150 KVIQLEGIAGTS-AARERGEGFKQAVAAHKFnVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMA--LGALraL 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 282586574 250 RAAGvkPGEIYATGFSLTPATVGAIEAGYLNLTSEAQPYLMGYLSV 295
Cdd:PRK10653 227 QTAG--KSDVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGV 270
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
 145-264 7.17e-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: 40.56  E-value: 7.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 145 VGTDNWRQGAEMAREILRRGglkqgdR---AFVWGLKRLEGRGR-RARALLEEFGKAGLTVDYLEISDEINkDAALGAPV 220
Cdd:cd01575   96 VGFSNFAAGRAMARHLIERG------YrriAFVGARLDGDSRARqRLEGFRDALAEAGLPLPLVLLVELPS-SFALGREA 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 282586574 221 LSGYLASHPDCKVIV-----VDHGGLTgqlgnFLRAAGVK-PGEIYATGF 264
Cdd:cd01575  169 LAELLARHPDLDAIFcsnddLALGALF-----ECQRRGIRvPGDIAIAGF 213
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
 47-322 8.42e-04

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: 40.69  E-value: 8.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  47 SVGEPYATTVVNGAKQAAIDLGVDLkiVY---SDWNPEK---MLENFKT------GLAANPTgfvvmghpgdDAYEPLID 114
Cdd:cd06302    8 VVGIPYFDAAEEGAKKAAKELGVEV--VYtgpTQADAAQqvqIVENLIAqgvdaiAVSPNDA----------DALAPVLK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 115 EAFAKGMIVTCVDTALPRLQGKYQARGFGYVGtdnwrQGAEMAREILRRGGlKQGDRAFVWG-------LKRLEGrgrrA 187
Cdd:cd06302   76 KAKDAGIKVITWDSDAPPSARDYFVNQADDEG-----LGEALVDSLAKEIG-GKGKVAILSGsltatnlNAWIKA----M 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 188 RALLEEFGKAGLTVDYLEISDEINKDAALGAPVLSGYlashPDCKVIVVDHGGLTGQLGNFLRAAGvKPGEIYATGFSlT 267
Cdd:cd06302  146 KEYLKSKYPDIELVDTYYTDDDQQKAYTQAQNLIQAY----PDLKGIIGVSTTAPPAAAQAVEEAG-KTGKVAVTGIG-L 219

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 282586574 268 PATVGA-IEAGYLNLTSEAQPYLMGYLSVL---QIVNTAKYKFGGLNVDTGGGYISQDN 322
Cdd:cd06302  220 PNTARPyLKDGSVKEGVLWDPAKLGYLTVYaayQLLKGKGFTEDSDDVGTGGKVKVDVA 278
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 57-131 8.54e-04

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: 40.36  E-value: 8.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 282586574  57 VNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMgHPGDDAYEPLIDEAFAKGMIVTCVDTALP 131
Cdd:cd06305   18 LQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIIS-HGDADALDPKLKKALDAGIPVVTFDTDSQ 91
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 37-291 9.04e-04

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: 40.35  E-value: 9.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  37 GMTVwfdagGSVGEPYATTVVNGAKQAA--IDLGVDLKIVYSDWNPEKMLENFKTGLAANPTgfVVMGHPGD-DAYEPLI 113
Cdd:cd06321    3 GVTV-----QDLGNPFFVAMVRGAEEAAaeINPGAKVTVVDARYDLAKQFSQIDDFIAQGVD--LILLNAADsAGIEPAI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 114 DEAFAKGMIVTCVDTAlprlqgkyqARGF-GYVGTDNWRQGAEMAREILRRGGLKqGDRAFVWG------LKRLEGrgrr 186
Cdd:cd06321   76 KRAKDAGIIVVAVDVA---------AEGAdATVTTDNVQAGYLACEYLVEQLGGK-GKVAIIDGppvsavIDRVNG---- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 187 ARALLEEFgkAGltvdyLEISDEINKDA--ALGAPVLSGYLASHPDCKVI--VVDhgglTGQLGNFLRAAGVKPGEIYAT 262
Cdd:cd06321  142 CKEALAEY--PG-----IKLVDDQNGKGsrAGGLSVMTRMLTAHPDVDGVfaIND----PGAIGALLAAQQAGRDDIVIT 210

                        250       260       270
                 ....*....|....*....|....*....|.
gi 282586574 263 GFSLTPATVGAI--EAGYLNLTSEAQPYLMG 291
Cdd:cd06321  211 SVDGSPEAVAALkrEGSPFIATAAQDPYDMA 241
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
111-303 1.62e-03

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 39.86  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 111 PLIDEAFAKGMIVTCVDT-----ALPRLQGKYQArgfgYVGTDNWRQGAEMAREILRRGGLKQGDRAFVWGLK-RLEGRG 184
Cdd:PRK09701  98 MPVARAWKKGIYLVNLDEkidmdNLKKAGGNVEA----FVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAgNASGEA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 185 RRARALlEEFGKAGLTvdYLEISDEINKDAALGAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGvKPGEIYATGF 264
Cdd:PRK09701 174 RRNGAT-EAFKKASQI--KLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAG-KTGKVLVVGT 249

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 282586574 265 SLTPATVGAIEAGYLNLTSEAQPYLMGYLSVLQIVNTAK 303
Cdd:PRK09701 250 DGIPEARKMVEAGQMTATVAQNPADIGATGLKLMVDAEK 288
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 104-295 2.01e-03

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


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 39.16  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 104 PGDD-AYEPLIDEAFAKGMIVTCVDTALPRLQGKYQARGFGYVGTDNwRQGAEMAREILRrGGLKQGDRAFVwglkrLEG 182
Cdd:cd19970   66 PADSkALVPVLKKAVDAGIAVINIDNRLDADALKEGGINVPFVGPDN-RQGAYLAGDYLA-KKLGKGGKVAI-----IEG 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 183 -------RGRRARALlEEFGKAGLTVDYLEISD-EINKdaalGAPVLSGYLASHPDCKVIVV--DHGGLTGQlgNFLRAA 252
Cdd:cd19970  139 ipgadnaQQRKAGFL-KAFEEAGMKIVASQSANwEIDE----ANTVAANLLTAHPDIRGILCanDNMALGAI--KAVDAA 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 282586574 253 GvKPGEIYATGFSLTPATVGAIEAGYLNLTSEAQPYLMGYLSV 295
Cdd:cd19970  212 G-KAGKVLVVGFDNIPAVRPLLKDGKMLATIDQHPAKQAVYGI 253
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 51-202 2.95e-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: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 38.75  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  51 PYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMGHPGDDAYEPLIdeafAKGMIVTCVDTAL 130
Cdd:cd06290   12 PFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLL----AEGIPVVLVDREL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282586574 131 PRLqgkyqarGFGYVGTDNwRQGAEMAREILrrggLKQGDR--AFVWGLKR-LEGRGRRA---RALLeefgKAGLTVD 202
Cdd:cd06290   88 EGL-------NLPVVNVDN-EQGGYNATNHL----IDLGHRriVHISGPEDhPDAQERYAgyrRALE----DAGLEVD 149
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
 141-264 3.06e-03

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


Pssm-ID: 380512 [Multi-domain]  Cd Length: 268  Bit Score: 38.70  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 141 GFGYVGTDNwRQGAEMAREILrrggLKQGDR--AFVWGLKRLEGRGRRARALLEEFGKAGLTVDY-LEISDEINKDAALG 217
Cdd:cd06289   93 DLDYVGIDN-RLGAQLATEHL----IALGHRriAFLGGLSDSSTRRERLAGFRAALAEAGLPLDEsLIVPGPATREAGAE 167

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 282586574 218 ApvLSGYLASHPDCKVIV-----VDHGGLTGqlgnfLRAAGVKPGEIYA-TGF 264
Cdd:cd06289  168 A--ARELLDAAPPPTAVVcfndlVALGAMLA-----LRRRGLEPGRDIAvVGF 213
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
 97-287 3.40e-03

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


Pssm-ID: 380502 [Multi-domain]  Cd Length: 284  Bit Score: 38.73  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  97 GFVVMGHPGDDayePLIDEAFAKGMIVTCVDTALPRlqgkyqarGFGYVGTDNWRQGAEMAREIL----RRGG-----LK 167
Cdd:cd06279   59 GFIVYGLSDDD---PAVAALRRRGLPLVVVDGPAPP--------GIPSVGIDDRAAARAAARHLLdlghRRIAilslrLD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 168 QGDRAFVWGLKRLEGRG-----RRARALLEEFGKAGLTVDYL---EISDEINKDAALGAPVLsgyLASHPDCKVIV---- 235
Cdd:cd06279  128 RGRERGPVSAERLAAATnsvarERLAGYRDALEEAGLDLDDVpvvEAPGNTEEAGRAAARAL---LALDPRPTAILcmsd 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 282586574 236 -VDHGGLTGqlgnfLRAAGVK-PGEIYATGFSLTPATvgaiEAGYLNLTSEAQP 287
Cdd:cd06279  205 vLALGALRA-----ARERGLRvPEDLSVTGFDDIPEA----AAADPGLTTVRQP 249
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
 48-202 3.49e-03

ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation; This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to 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: 380519 [Multi-domain]  Cd Length: 270  Bit Score: 38.41  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  48 VGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTGLAANPTGFVVMGHPGDDAYeplIDEAFAKGMIVTCVD 127
Cdd:cd06296    9 LDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQ---LRLLRSAGIPFVLID 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282586574 128 talPRLQGkyqARGFGYVGTDNWRQGAEMAREILRRG----GLKQGDRAFVWGLKRLEGrgrrARALLEEfgkAGLTVD 202
Cdd:cd06296   86 ---PVGEP---DPDLPSVGATNWAGGRLATEHLLDLGhrriAVITGPPRSVSGRARLAG----YRAALAE---AGIAVD 151
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 40-268 9.12e-03

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


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 37.25  E-value: 9.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574  40 VWFDAGGSVGEPYATTVVNGAKQAAIDLGVDLKIVYSDWNPEKMLENFKTgLAANPTGFVVMGHPGDDAYEPlIDEAFAK 119
Cdd:cd01391    4 VVTSSLHQIREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIE-FIRDNIAGVIGPGSSSVAIVI-QNLAQLF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 120 GMIVTCVDTALPRLQGKYQARGFGYVGTDNWRQGAEMAREILRRGGlkqGDRAFVWGLKRLEGRGRRArALLEEFGKAGL 199
Cdd:cd01391   82 DIPQLALDATSQDLSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNW---TYVAAIHGEGLNSGELRMA-GFKELAKQEGI 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282586574 200 TvdyLEISDEINKDAAL-GAPVLSGYLASHPDCKVIVVDHGGLTGQLGNFLRAAGVKpGEIYATGFSLTP 268
Cdd:cd01391  158 C---IVASDKADWNAGEkGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLV-GDVSVIGSDGWA 223
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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