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Conserved domains on  [gi|490522029|ref|WP_004387464|]
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MULTISPECIES: galactose/glucose ABC transporter substrate-binding protein MglB [Cronobacter]

Protein Classification

galactose ABC transporter substrate-binding protein( domain architecture ID 10794151)

periplasmic galactose-binding protein (GBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15395 PRK15395
galactose/glucose ABC transporter substrate-binding protein MglB;
2-329 0e+00

galactose/glucose ABC transporter substrate-binding protein MglB;


:

Pssm-ID: 185293 [Multi-domain]  Cd Length: 330  Bit Score: 652.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   2 NKKVLTLSAVMSCMLFGTAAQAAD-RIGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
Cdd:PRK15395   1 NKKVLTLSALMASMLFGAAAAAADtRIGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  81 GVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAGWDLNKD 160
Cdd:PRK15395  81 GVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANPAWDLNKD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 161 GQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 240
Cdd:PRK15395 161 GKIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 241 VEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTDWKIENKVVRIPYVGV 320
Cdd:PRK15395 241 VEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAEGTNWKIENKVVRVPYVGV 320

                 ....*....
gi 490522029 321 DKDNLAEIT 329
Cdd:PRK15395 321 DKDNLAEFT 329
 
Name Accession Description Interval E-value
PRK15395 PRK15395
galactose/glucose ABC transporter substrate-binding protein MglB;
2-329 0e+00

galactose/glucose ABC transporter substrate-binding protein MglB;


Pssm-ID: 185293 [Multi-domain]  Cd Length: 330  Bit Score: 652.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   2 NKKVLTLSAVMSCMLFGTAAQAAD-RIGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
Cdd:PRK15395   1 NKKVLTLSALMASMLFGAAAAAADtRIGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  81 GVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAGWDLNKD 160
Cdd:PRK15395  81 GVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANPAWDLNKD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 161 GQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 240
Cdd:PRK15395 161 GKIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 241 VEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTDWKIENKVVRIPYVGV 320
Cdd:PRK15395 241 VEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAEGTNWKIENKVVRVPYVGV 320

                 ....*....
gi 490522029 321 DKDNLAEIT 329
Cdd:PRK15395 321 DKDNLAEFT 329
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
26-320 2.50e-156

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: 439.71  E-value: 2.50e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd01539    2 KIGVFIYNYDDTFISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAGWDLNKDGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd01539   82 NIPVIFFNREPSREDLKSYDKAYYVGTDAEESGIMQGEIIADYWKANPEIDKNGDGKIQYVMLKGEPGHQDAIARTKYSV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNaNKIEVVIANNDAMAMGAVEALKAHN------KSSIPVFGVDA 259
Cdd:cd01539  162 KTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYG-DKIELVIANNDDMALGAIEALKAAGyntgdgDKYIPVFGVDA 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490522029 260 LPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTD-WKIENKVVRIPYVGV 320
Cdd:cd01539  241 TPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLETGYkFLVEGKYVRIPYKKV 302
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
5-325 3.53e-60

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: 195.14  E-value: 3.53e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   5 VLTLSAVMSCMLFG---------TAAQAADRIGVTIYKYDDNFMSVVRKAIEkDASASPDVQLLMNDSQNDQSKQNDQID 75
Cdd:COG1879    5 LLAAVLALALALAAcgsaaaeaaAAAAKGKTIGFVVKTLGNPFFVAVRKGAE-AAAKELGVELIVVDAEGDAAKQISQIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  76 VLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPsrkalDSYDKAYYVGTDSKESGIIQGDLIAKHWKanagw 155
Cdd:COG1879   84 DLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDV-----DGSDRVAYVGSDNYAAGRLAAEYLAKALG----- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 156 dlnkdGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGiKTEQLQLDTAMWDTAQAKDKMDAWLSgpnAN-KIEVVIANND 234
Cdd:COG1879  154 -----GKGKVAILTGSPGAPAANERTDGFKEALKEYP-GIKVVAEQYADWDREKALEVMEDLLQ---AHpDIDGIFAAND 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 235 AMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKgaadgtdwKIEnKVV 313
Cdd:COG1879  225 GMALGAAQALKAAGRKGdVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGK--------EVP-KEI 295
                        330
                 ....*....|..
gi 490522029 314 RIPYVGVDKDNL 325
Cdd:COG1879  296 LTPPVLVTKENV 307
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
27-298 4.20e-58

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: 188.29  E-value: 4.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   27 IGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  107 IPIVFFNKEpsrkaLDSYDKAYYVGTDSKESGIIQGDLIAKHWKanagwdlnkdGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:pfam13407  81 IPVVTFDSD-----APSSPRLAYVGFDNEAAGEAAGELLAEALG----------GKGKVAILSGSPGDPNANERIDGFKK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  187 ELNDK--GIKTEQLQlDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIP-VFGVDALPEA 263
Cdd:pfam13407 146 VLKEKypGIKVVAEV-EGTNWDPEKAQQQMEALLTA-YPNPLDGIISPNDGMAGGAAQALEAAGLAGKVvVTGFDATPEA 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 490522029  264 LALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:pfam13407 224 LEAIKDGTIDATVLQDPYGQGYAAVELAAALLKGK 258
 
Name Accession Description Interval E-value
PRK15395 PRK15395
galactose/glucose ABC transporter substrate-binding protein MglB;
2-329 0e+00

galactose/glucose ABC transporter substrate-binding protein MglB;


Pssm-ID: 185293 [Multi-domain]  Cd Length: 330  Bit Score: 652.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   2 NKKVLTLSAVMSCMLFGTAAQAAD-RIGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
Cdd:PRK15395   1 NKKVLTLSALMASMLFGAAAAAADtRIGVTIYKYDDNFMSVVRKAIEKDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  81 GVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAGWDLNKD 160
Cdd:PRK15395  81 GVKALAINLVDPAAAPTVIEKARGQDVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANPAWDLNKD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 161 GQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 240
Cdd:PRK15395 161 GKIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 241 VEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTDWKIENKVVRIPYVGV 320
Cdd:PRK15395 241 VEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLADGKGAAEGTNWKIENKVVRVPYVGV 320

                 ....*....
gi 490522029 321 DKDNLAEIT 329
Cdd:PRK15395 321 DKDNLAEFT 329
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
26-320 2.50e-156

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: 439.71  E-value: 2.50e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd01539    2 KIGVFIYNYDDTFISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAGWDLNKDGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd01539   82 NIPVIFFNREPSREDLKSYDKAYYVGTDAEESGIMQGEIIADYWKANPEIDKNGDGKIQYVMLKGEPGHQDAIARTKYSV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNaNKIEVVIANNDAMAMGAVEALKAHN------KSSIPVFGVDA 259
Cdd:cd01539  162 KTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYG-DKIELVIANNDDMALGAIEALKAAGyntgdgDKYIPVFGVDA 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490522029 260 LPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTD-WKIENKVVRIPYVGV 320
Cdd:cd01539  241 TPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLETGYkFLVEGKYVRIPYKKV 302
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
26-319 4.17e-118

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: 341.53  E-value: 4.17e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKDASAsPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGtVIEKARGQ 105
Cdd:cd01537    1 RIGVTIYSYDDNFMSVIRKAIEQDAKQ-PGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAG-VAEKARGQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKEPSRkaldsYDKAYYVGTDSKESGIIQGDLIAKHWkanagwdlnkdgQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd01537   79 NVPVVFFDKEPSR-----YDKAYYVITDSKEGGIIQGDLLAKHG------------HIQIVLLKGPLGHPDAEARLAGVI 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPnaNKIEVVIANNDAMAMGAVEALKAHNK---SSIPVFGVDALPE 262
Cdd:cd01537  142 KELNDKGIKTEQLQLDTGDWDTASGKDKMDQWLSGP--NKPTAVIANNDAMAMGAVEALKEHGLrvpSDISVFGYDALPE 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490522029 263 ALalvKSGALAGTVLNDANNQAKATFDLAKNLAagkgaadgTDWKIENKVVRIPYVG 319
Cdd:cd01537  220 AL---KSGPLLTTILQDANNLGKTTFDLLLNLA--------DNWKIDNKVVRVPYVL 265
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
5-325 3.53e-60

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: 195.14  E-value: 3.53e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   5 VLTLSAVMSCMLFG---------TAAQAADRIGVTIYKYDDNFMSVVRKAIEkDASASPDVQLLMNDSQNDQSKQNDQID 75
Cdd:COG1879    5 LLAAVLALALALAAcgsaaaeaaAAAAKGKTIGFVVKTLGNPFFVAVRKGAE-AAAKELGVELIVVDAEGDAAKQISQIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  76 VLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPsrkalDSYDKAYYVGTDSKESGIIQGDLIAKHWKanagw 155
Cdd:COG1879   84 DLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDV-----DGSDRVAYVGSDNYAAGRLAAEYLAKALG----- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 156 dlnkdGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGiKTEQLQLDTAMWDTAQAKDKMDAWLSgpnAN-KIEVVIANND 234
Cdd:COG1879  154 -----GKGKVAILTGSPGAPAANERTDGFKEALKEYP-GIKVVAEQYADWDREKALEVMEDLLQ---AHpDIDGIFAAND 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 235 AMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKgaadgtdwKIEnKVV 313
Cdd:COG1879  225 GMALGAAQALKAAGRKGdVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGK--------EVP-KEI 295
                        330
                 ....*....|..
gi 490522029 314 RIPYVGVDKDNL 325
Cdd:COG1879  296 LTPPVLVTKENV 307
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
27-297 2.10e-58

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: 189.36  E-value: 2.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06301    3 IGVSMQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSrkalDSYDKAYYVGTDSKESGIIQGDLIAKhwkanagwdlNKDGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06301   83 IPLVYVNREPD----SKPKGVAFVGSDDIESGELQMEYLAK----------LLGGKGNIAILDGVLGHEAQILRTEGNKD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELND-KGIKTEQLQldTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEAL 264
Cdd:cd06301  149 VLAKyPGMKIVAEQ--TANWSREKAMDIVENWLQ--SGDKIDAIVANNDEMAIGAILALEAAGKKdDILVAGIDATPDAL 224
                        250       260       270
                 ....*....|....*....|....*....|...
gi 490522029 265 ALVKSGALAGTVLNDANNQAKATFDLAKNLAAG 297
Cdd:cd06301  225 KAMKAGRLDATVFQDAAGQGETAVDVAVKAAKG 257
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
26-309 2.38e-58

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: 188.93  E-value: 2.38e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKDAsASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd01536    1 KIGVVVKDLTNPFWVAVKKGAEAAA-KELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNkepsRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWkanagwdlnkDGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd01536   80 GIPVVAVD----TDIDGGGDVVAFVGTDNYEAGKLAGEYLAEAL----------GGKGKVAILEGPPGSSTAIDRTKGFK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDKGiKTEQLQLDTAMWDTAQAKDKMDAWLsgpNAN-KIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEA 263
Cdd:cd01536  146 EALKKYP-DIEIVAEQPANWDRAKALTVTENLL---QANpDIDAVFAANDDMALGAAEALKAAGRTGdIKIVGVDGTPEA 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 490522029 264 LALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTDWKIE 309
Cdd:cd01536  222 LKAIKDGELDATVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPVT 267
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
27-298 4.20e-58

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: 188.29  E-value: 4.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   27 IGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  107 IPIVFFNKEpsrkaLDSYDKAYYVGTDSKESGIIQGDLIAKHWKanagwdlnkdGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:pfam13407  81 IPVVTFDSD-----APSSPRLAYVGFDNEAAGEAAGELLAEALG----------GKGKVAILSGSPGDPNANERIDGFKK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  187 ELNDK--GIKTEQLQlDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIP-VFGVDALPEA 263
Cdd:pfam13407 146 VLKEKypGIKVVAEV-EGTNWDPEKAQQQMEALLTA-YPNPLDGIISPNDGMAGGAAQALEAAGLAGKVvVTGFDATPEA 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 490522029  264 LALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:pfam13407 224 LEAIKDGTIDATVLQDPYGQGYAAVELAAALLKGK 258
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
26-327 3.52e-47

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: 160.51  E-value: 3.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKDAsASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd06313    1 KIGFTVYGLSSEFITNLVEAMKAVA-KELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKepsrkALDSYDKAYYVGTDSKESGIIQGDLIAKhwkanagwdlNKDGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd06313   80 GIPLVGVNA-----LIENEDLTAYVGSDDVVAGELEGQAVAD----------RLGGKGNVVILEGPIGQSAQIDRGKGIE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDK-GIKTeqLQLDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEAL 264
Cdd:cd06313  145 NVLKKYpDIKV--LAEQTANWSRDEAMSLMENWLQA-YGDEIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDAL 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490522029 265 ALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGaadgtdwkiENKVVRIPYVGVDKDNLAE 327
Cdd:cd06313  222 QAVKSGELIATVLQDAEAQGKGAVEVAVDAVKGEG---------VEKKYYIPFVLVTKDNVDD 275
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
43-318 1.61e-37

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: 135.40  E-value: 1.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  43 RKAIEKDAsASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALD 122
Cdd:cd19992   18 KEYMEEEA-KELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDRLILNADVD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 123 sydkaYYVGTDSKESGIIQGD-LIAKHWKANagwdlnkdgqiqYVLLKGEPGHPDAEARTT---YVIKELNDKG---IKT 195
Cdd:cd19992   97 -----LYVGRDNYKVGQLQAEyALEAVPKGN------------YVILSGDPGDNNAQLITAgamDVLQPAIDSGdikIVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 196 EQLqldTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAG 274
Cdd:cd19992  160 DQY---VKGWSPDEAMKLVENALTA-NNNNIDAVLAPNDGMAGGAIQALKAQGlAGKVFVTGQDAELAALKRIVEGTQTM 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 490522029 275 TVLNDANNQAKATFDLAKNLAAGKgAADGTDWKIENKVVRIPYV 318
Cdd:cd19992  236 TVWKDLKELARAAADAAVKLAKGE-KPQTTDETINNGGKDVPAI 278
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
48-328 2.86e-34

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 127.56  E-value: 2.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  48 KDASASPDVQllmnDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVffnkepsrkaldSYDK- 126
Cdd:COG4213   29 KELGYEVDVQ----NANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVI------------AYDRl 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 127 ------AYYVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIQYVLLKGEPGhpDAEARTTY-----VIKELNDKG--- 192
Cdd:COG4213   93 ilnsdvDYYVSFDNVKVGELQGQYLVDG--------LPLKGKGNIELFGGSPT--DNNATLFFegamsVLQPYIDSGklv 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 193 IKTEQlqlDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVF-GVDALPEALALVKSGA 271
Cdd:COG4213  163 VVSGQ---WTLGWDPETAQKRMENLLTA-NGNKVDAVLAPNDGLAGGIIQALKAQGLAGKVVVtGQDAELAAVQRILAGT 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490522029 272 LAGTVLNDANNQAKATFDLAKNLAAGKGAAdgTDWKIENKVVRIPY-----VGVDKDNLAEI 328
Cdd:COG4213  239 QYMTVYKDTRELAEAAAELAVALAKGEKPE--VNGTYDNGKKDVPSyllepVAVTKDNVKET 298
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
35-298 2.40e-32

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: 121.11  E-value: 2.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  35 DDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFnk 114
Cdd:cd06308   10 NDPWRAAMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVL-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 115 epSRKaLDSYDKAYYVGTDSKESGIIQGDLIAKhwkanagwDLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELND-KGI 193
Cdd:cd06308   88 --DRK-VSGDDYTAFIGADNVEIGRQAGEYIAE--------LLNGKGNV--VEIQGLPGSSPAIDRHKGFLEAIAKyPGI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 194 KteQLQLDTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDALPEAL-ALVKSGA 271
Cdd:cd06308  155 K--IVASQDGDWLRDKAIKVMEDLLQ--AHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGLPEAGeKAVKDGI 230
                        250       260
                 ....*....|....*....|....*..
gi 490522029 272 LAGTVLNDANnqAKATFDLAKNLAAGK 298
Cdd:cd06308  231 LAATFLYPTG--GKEAIEAALKILNGE 255
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
48-316 6.81e-28

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: 110.03  E-value: 6.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  48 KDASASPDVQLlmndSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFnkepSRKALDSYDKA 127
Cdd:cd19994   26 EEAGYTVDLQY----ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAY----DRLIMNTDAVD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 128 YYVGTDSKESGIIQGDLIAKHWKANAGwdlnkDGQIQYVLLKGEPGhpDAEARTTY-----VIKELNDKGI------KTE 196
Cdd:cd19994   98 YYVTFDNEKVGELQGQYLVDKLGLKDG-----KGPFNIELFAGSPD--DNNAQLFFkgameVLQPYIDDGTlvvrsgQTT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 197 QLQLDTAMWDTAQAKDKMDAWLSGPNA--NKIEVVIANNDAMAMGAVEALKAHNKSSIP---VFGVDALPEALALVKSGA 271
Cdd:cd19994  171 FEQVATPDWDTETAQARMETLLSAYYTggKKLDAVLSPNDGIARGVIEALKAAGYDTGPwpvVTGQDAEDASVKSILDGE 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 490522029 272 LAGTVLNDANNQAKATFDLAKNLAAGKGAADGTDWKIENKVVRIP 316
Cdd:cd19994  251 QSMTVFKDTRLLAKATVELVDALLEGEEVEVNDTKTYDNGVKVVP 295
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
38-327 2.11e-27

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: 108.46  E-value: 2.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  38 FMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkeps 117
Cdd:cd06309   13 WRVANTKSIKEAAKKR-GYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVD---- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 118 rKALDSYDKAYY---VGTDSKESGIIQGDLIAKHWKanagwdlNKDGQIqyVLLKGEPGHPDAEARTT---YVIKELNDK 191
Cdd:cd06309   88 -RTIDGEDGSLYvtfIGSDFVEEGRRAAEWLVKNYK-------GGKGNV--VELQGTAGSSVAIDRSKgfrEVIKKHPNI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 192 GIKTEQlqldTAMWDTAQAKDKMDAWL-SGPnaNKIEVVIANNDAMAMGAVEALKAHNKS---SIPVFGVDALPEALALV 267
Cdd:cd06309  158 KIVASQ----SGNFTREKGQKVMENLLqAGP--GDIDVIYAHNDDMALGAIQALKEAGLKpgkDVLVVGIDGQKDALEAI 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 268 KSGALAGTVLNDAnNQAKATFDLAKNLAAGKgaadgtdwKIEnKVVRIPYVGVDKDNLAE 327
Cdd:cd06309  232 KAGELNATVECNP-LFGPTAFDTIAKLLAGE--------KVP-KLIIVEERLFDKDNAAE 281
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
27-276 2.27e-27

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: 108.15  E-value: 2.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06323    2 IGLSVSTLNNPFFVSLKDGAQAEAKEL-GVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNkepsRKALDSyDKAYYVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYvIK 186
Cdd:cd06323   81 IPVITVD----RSVTGG-KVVSHIASDNVAGGEMAAEYIAKK--------LGGKGKV--VELQGIPGTSAARERGKG-FH 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALA 265
Cdd:cd06323  145 NAIAKYPKINVVASQTADFDRTKGLNVMENLLqAHPD---IDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVK 221
                        250
                 ....*....|.
gi 490522029 266 LVKSGALAGTV 276
Cdd:cd06323  222 AVKDGKLAATV 232
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
27-297 2.57e-27

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: 108.27  E-value: 2.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06318    2 IGFSQRTLASPYYAALVAAAKAEAKKL-GVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNkepsRKALDSYDKAYYVGTDSKESGIIQGdliakHWKANAgwdLNKDGqIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06318   81 IPVITVD----SALDPSANVATQVGRDNKQNGVLVG-----KEAAKA---LGGDP-GKIIELSGDKGNEVSRDRRDGFLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIKT------EQLQLDTAMWDTAQAKDKMDAWLSgpnANK-IEVVIANNDAMAMGAVEALKAHNKSSI-PVFGVD 258
Cdd:cd06318  148 GVNEYQLRKygksniKVVAQPYGNWIRSGAVAAMEDLLQ---AHPdINVVYAENDDMALGAMKALKAAGMLDKvKVAGAD 224
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 490522029 259 ALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAG 297
Cdd:cd06318  225 GQKEALKLIKDGKYVATGLNDPDLLGKTAVDTAAKVVKG 263
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
26-308 2.24e-26

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: 105.55  E-value: 2.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKDAsASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd19968    1 KIGFSFPNLSFPFFVYMHEQAVDEA-AKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNkepsRKAlDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAgwdlnkdgqiQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd19968   80 GIPVVTVD----RRA-EGAAPVPHVGADNVAGGREVAKFVVDKLPNGA----------KVIELTGTPGSSPAIDRTKGFH 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELnDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAH--NKSSIPVFGVDALPEA 263
Cdd:cd19968  145 EEL-AAGPKIKVVFEQTGNFERDEGLTVMENILTS-LPGPPDAIICANDDMALGAIEAMRAAglDLKKVKVIGFDAVPDA 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 490522029 264 LALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADGTDWKI 308
Cdd:cd19968  223 LQAIKDGELYATVEQPPGGQARTALRILVDYLKDKKAPKKVNLKP 267
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
26-325 1.85e-25

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: 103.21  E-value: 1.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIeKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd06319    1 KIGYSVYDLDNPFWQIMERGV-QAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFfnkepSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANaGWdlnkdGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd06319   80 KIPVVI-----ADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKEN-GW-----GGGSVGIIAIPQSRVNGQARTAGFE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 186 KELNDKGIKTEQLQLdTAMWDTAQAKDKM-DAWLSGPnanKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEA 263
Cdd:cd06319  149 DALEEAGVEEVALRQ-TPNSTVEETYSAAqDLLAANP---DIKGIFAQNDQMAQGALQAIEEAGRTGdILVVGFDGDPEA 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490522029 264 LALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAADgtdwkienKVVRIPYVGVDKDNL 325
Cdd:cd06319  225 LDLIKDGKLDGTVAQQPFGMGARAVELAIQALNGDNTVE--------KEIYLPVLLVTSENV 278
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
27-316 3.34e-25

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: 101.89  E-value: 3.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEKDASASPDvQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd19971    2 FGFSYMTMNNPFFIAINDGIKKAVEANGD-ELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPS-RKALDSydkayYVGTDSKESGIIQGDLIAKhwkanagwDLNKDGQIqyVLLKgepgHPDAEA---RTT 182
Cdd:cd19971   81 IPVINVDTPVKdTDLVDS-----TIASDNYNAGKLCGEDMVK--------KLPEGAKI--AVLD----HPTAEScvdRID 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 183 YVIKEL-NDKGIKTEQlQLDTAMwDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDA 259
Cdd:cd19971  142 GFLDAIkKNPKFEVVA-QQDGKG-QLEVAMPIMEDILqAHPD---LDAVFALNDPSALGALAALKAAGKlGDILVYGVDG 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490522029 260 LPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKgaadgtdwKIEnKVVRIP 316
Cdd:cd19971  217 SPDAKAAIKDGKMTATAAQSPIEIGKKAVETAYKILNGE--------KVE-KEIVVP 264
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
44-318 3.73e-25

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: 102.75  E-value: 3.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  44 KAIEKDAsasPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsrKALDS 123
Cdd:cd19995   24 KAMKKLC---PDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYD-----RLILG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 124 YDKAYYVGTDSKESGIIQGDLIAKHWKANAGwdlnKDGQIqyVLLKGEPGHPDA---EARTTYVIKELNDKGIKTEQLQL 200
Cdd:cd19995   96 GPADYYVSFDNVAVGEAQAQSLVDHLKAIGK----KGVNI--VMINGSPTDNNAglfKKGAHEVLDPLGDSGELKLVCEY 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 201 DTAMWDTAQAKDKMDAWLSgPNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAGTVLND 279
Cdd:cd19995  170 DTPDWDPANAQTAMEQALT-KLGNNIDGVLSANDGLAGGAIAALKAQGlAGKVPVTGQDATVAGLQRILAGDQYMTVYKP 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490522029 280 ANNQAKATFDLAKNLAAGKG-AADGTDWKIENKVVRIPYV 318
Cdd:cd19995  249 IKKEAAAAAKVAVALLKGETpPSDLVTGTVTNGGDKVPAV 288
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
26-326 1.40e-24

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: 100.80  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKDASASP-DVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARG 104
Cdd:cd06320    1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGvKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 105 QNIPIVFFNKEPSRKALDSY--DKAYYVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTT 182
Cdd:cd06320   81 KGIPVINLDDAVDADALKKAggKVTSFIGTDNVAAGALAAEYIAEK--------LPGGGKV--AIIEGLPGNAAAEARTK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 183 YVIKELNdKGIKTEQLQLDTAMWDTAQAKDKMDAWLSG-PNANKIevvIANNDAMAMGAVEALKAHNKSS-IPVFGVDAL 260
Cdd:cd06320  151 GFKETFK-KAPGLKLVASQPADWDRTKALDAATAILQAhPDLKGI---YAANDTMALGAVEAVKAAGKTGkVLVVGTDGI 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490522029 261 PEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKgaadgtdwKIENKVVrIPYVGVDKDNLA 326
Cdd:cd06320  227 PEAKKSIKAGELTATVAQYPYLEGAMAVEAALRLLQGQ--------KVPAVVA-TPQALITKDNVD 283
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
62-298 2.11e-24

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: 100.24  E-value: 2.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKepsrkaLDSYDKAYYVGTDSKESGIIQ 141
Cdd:cd19993   36 DAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDR------LIENPIAFYISFDNVEVGRMQ 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 142 GDLIakhwkanagwdLNKDGQIQYVLLKGEPGHPDAE---ARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWL 218
Cdd:cd19993  110 ARGV-----------LKAKPEGNYVFIKGSPTDPNADflrAGQMEVLQPAIDSGKIKIVGEQYTDGWKPANAQKNMEQIL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 219 SGpNANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAG 297
Cdd:cd19993  179 TA-NNNKVDAVVASNDGTAGGAVAALAAQGlAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKG 257

                 .
gi 490522029 298 K 298
Cdd:cd19993  258 T 258
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
53-316 1.24e-21

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: 92.87  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  53 SPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsRKALDSyDKAYYVGT 132
Cdd:cd01538   27 EKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYD----RLILNA-DVDYYISF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 133 DSKESGIIQGDLIAKhwkanagwdlnKDGQIQYVLLKGEPGHPDA---EARTTYVIKELNDKGIKTEQLQLDTAMWDTAQ 209
Cdd:cd01538  102 DNEKVGELQAQALLD-----------AKPEGNYVLIGGSPTDNNAklfRDGQMKVLQPAIDSGKIKVVGDQWVDDWLPAN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 210 AKDKMDAWLSGpNANKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTVLNDANNQAKATF 288
Cdd:cd01538  171 AQQIMENALTA-NGNNVDAVVASNDGTAGGAIAALKAQGLSGgVPVSGQDADLAAIKRILAGTQTMTVYKDIRLLADAAA 249
                        250       260
                 ....*....|....*....|....*...
gi 490522029 289 DLAknLAAGKGAADGTDWKIENKVVRIP 316
Cdd:cd01538  250 EVA--VALMRGEKPPINGTTNNGLKDVP 275
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
65-321 1.96e-21

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: 92.30  E-value: 1.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  65 NDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsRKALDSyDKAYYVGTDSKESGIIQGDL 144
Cdd:cd19991   39 GDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYD----RLILNA-DVDLYVSFDNEKVGELQAEA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 145 IAKHwkanagwdlnkDGQIQYVLLKGEPGHPDAE---ARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGp 221
Cdd:cd19991  114 LVKA-----------KPKGNYVLLGGSPTDNNAKlfrEGQMKVLQPLIDSGDIKVVGDQWVDDWDPEEALKIMENALTA- 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 222 NANKIEVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGA 300
Cdd:cd19991  182 NNNKIDAVIASNDGTAGGAIQALAEQGlAGKVAVSGQDADLAACQRIVEGTQTMTIYKPIKELAEKAAELAVALAKGEKN 261
                        250       260
                 ....*....|....*....|.
gi 490522029 301 ADGTdwKIENKVVRIPYVGVD 321
Cdd:cd19991  262 EANR--TINNGKKEVPSILLD 280
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
38-258 4.25e-21

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: 91.53  E-value: 4.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  38 FMSVVRKAIEKDASASPDV--QLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKE 115
Cdd:cd19996   13 WRVQMIAEFEAEAAKLKKLikELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 116 PsrkalDSYDKAYYVGTDSKESGIIQGDLIAKhwkanagwDLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELND-KGIK 194
Cdd:cd19996   93 V-----GSDKYTAFVGVDDAAFGRVGAEWLVK--------QLGGKGNI--IALRGIAGVSVSEDRWAGAKEVFKEyPGIK 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490522029 195 TeqLQLDTAMWDTAQAKDKMDAWLS-GPnanKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVD 258
Cdd:cd19996  158 I--VGEVYADWDYAKAKQAVESLLAaYP---DIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTGED 217
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
27-298 1.81e-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: 89.26  E-value: 1.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06322    2 IGVSLLTLQHPFFVDIKDAMKKEAAEL-GVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDLIAKHW---KANAGWDLNKDGQIQYVLLKG----EPGHPDAEa 179
Cdd:cd06322   81 IPVFTVDVKADGAKVVT-----HVGTDNYAGGKLAGEYALKALlggGGKIAIIDYPEVESVVLRVNGfkeaIKKYPNIE- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 180 rttyVIKELNDKGIKTEQLQldtAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHNKSS-IPVFGVD 258
Cdd:cd06322  155 ----IVAEQPGDGRREEALA---ATEDMLQANPDLDG------------IFAIGDPAALGALTAIESAGKEDkIKVIGFD 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 490522029 259 ALPEAL-ALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:cd06322  216 GNPEAIkAIAKGGKIKADIAQQPDKIGQETVEAIVKYLAGE 256
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
1-276 1.68e-19

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 87.07  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   1 MNKKVLTL-SAVMSCMLFGTAAQAADRIGVTIYKYDDNFMSVVRKAIEKDASaSPDVQLLMNDSQNDQSKQNDQIDVLLA 79
Cdd:PRK10653   2 NMKKLATLvSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEAD-KLGYNLVVLDSQNNPAKELANVQDLTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  80 KGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDLIAKHWKANAgwdlnk 159
Cdd:PRK10653  81 RGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVS-----HIASDNVAGGKMAGDFIAKKLGEGA------ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 160 dgqiQYVLLKGEPGHPDAEARTTYVIKELndKGIKTEQLQLDTAMWDTAQAKDKMDAWLSgpnAN-KIEVVIANNDAMAM 238
Cdd:PRK10653 150 ----KVIQLEGIAGTSAARERGEGFKQAV--AAHKFNVLASQPADFDRTKGLNVMQNLLT---AHpDVQAVFAQNDEMAL 220
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490522029 239 GAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTV 276
Cdd:PRK10653 221 GALRALQTAGKSDVMVVGFDGTPDGIKAVNRGKLAATI 258
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
62-294 1.81e-16

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: 78.13  E-value: 1.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEpsrkaLDSYDKAY-YVGTDSKESGII 140
Cdd:cd19967   36 DHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLIDRE-----INAEGVAVaQIVSDNYQGAVL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 141 QGDLIAKhwkanagwDLNKDGQiqYVLLKGEPGHPDAEART---TYVIKELNDKGIKTEQlqldTAMWDTAQAKDKMDAW 217
Cdd:cd19967  111 LAQYFVK--------LMGEKGL--YVELLGKESDTNAQLRSqgfHSVIDQYPELKMVAQQ----SADWDRTEAFEKMESI 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490522029 218 L-SGPnanKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNL 294
Cdd:cd19967  177 LqANP---DIKGVICGNDEMALGAIAALKAAGRAGdVIIVGFDGSNDVRDAIKEGKISATVLQPAKLIARLAVEQADQY 252
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
26-298 2.45e-15

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


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 74.69  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKdASASPDVQL--LMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKAR 103
Cdd:cd06310    1 KIGVVLKGTTSAFWRTVREGAEA-AAKDLGVKIifVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 104 GQNIPIVFFNkepSRKALDSYDKayYVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTY 183
Cdd:cd06310   80 DKGIPVIVID---SGIKGDAYLS--YIATDNYAAGRLAAQKLAEA--------LGGKGKV--AVLSLTAGNSTTDQREEG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 184 VIKEL--NDKGIKTEQLQLdtAMWDTAQAKDKMDAWLSGpnANKIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDAL 260
Cdd:cd06310  145 FKEYLkkHPGGIKVLASQY--AGSDYAKAANETEDLLGK--YPDIDGIFATNEITALGAAVAIKSRKLSgQIKIVGFDSQ 220
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490522029 261 PEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:cd06310  221 EELLDALKNGKIDALVVQNPYEIGYEGIKLALKLLKGE 258
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
35-272 2.99e-15

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: 74.67  E-value: 2.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  35 DDNFMSVVRKAIeKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGT-VIEKARGQNIPIVFFN 113
Cdd:cd19966   11 GDPFWTVVYNGA-KDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTpLIEAAKKAGIIVTSFN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 114 KePSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANAGwdlnkdgqiQYVLLKGEPGH-PDAEARTTYVIKELNDKG 192
Cdd:cd19966   90 T-DLPKLEYGDCGLGYVGADLYAAGYTLAKELVKRGGLKTG---------DRVFVPGLLPGqPYRVLRTKGVIDALKEAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 193 IKTEQLQLDTAMWDTAQAKDKMDAWLSgpnANK-IEVVIANNDAMAMGAVEALKAHNK--SSIPVFGVDALPEALALVKS 269
Cdd:cd19966  160 IKVDYLEISLEPNKPAEGIPVMTGYLA---ANPdVKAIVGDGGGLTANVAKYLKAAGKkpGEIPVAGFDLSPATVQAIKS 236

                 ...
gi 490522029 270 GAL 272
Cdd:cd19966  237 GYV 239
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
34-276 5.16e-15

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: 73.77  E-value: 5.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  34 YDDNFMSVVRKAIEKdASASPDVQLLMNDSQN-DQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFF 112
Cdd:cd06314    9 LNNPFWDLAEAGAEK-AAKELGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 113 NKEpsrkALDSYDKAyYVGTDSKESGIIQGDLIAKhwkanagwDLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELNDKG 192
Cdd:cd06314   88 DSD----APDSKRLA-YIGTDNYEAGREAGELMKK--------ALPGGGKV--AIITGGLGADNLNERIQGFKDALKGSP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 193 iKTEQLQLDTAMWDTAQAKDKMDAWLSG-PNANKIEVVIANNdamAMGAVEALKAHNK-SSIPVFGVDALPEALALVKSG 270
Cdd:cd06314  153 -GIEIVDPLSDNDDIAKAVQNVEDILKAnPDLDAIFGVGAYN---GPAIAAALKDAGKvGKVKIVGFDTLPETLQGIKDG 228

                 ....*.
gi 490522029 271 ALAGTV 276
Cdd:cd06314  229 VIAATV 234
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
35-276 1.10e-14

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


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 73.04  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  35 DDNFMSVVRKAIeKDASASPDVQL-LMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFN 113
Cdd:cd06312   11 SDPFWSVVKKGA-KDAAKDLGVTVqYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAIN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 114 KEPSRKALDSydkAY--YVGTDSKESGiiQGdliakhwkanAGWDLNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDK 191
Cdd:cd06312   90 SGDDRSKERL---GAltYVGQDEYLAG--QA----------AGERALEAGPKNALCVNHEPGNPGLEARCKGFADAFKGA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 192 GIKTEQLQLDTamwDTAQAKDKMDAWLsgpNANK-IEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKS 269
Cdd:cd06312  155 GILVELLDVGG---DPTEAQEAIKAYL---QADPdTDAVLTLGPVGADPALKAVKEAGLKGkVKIGTFDLSPETLEAIKD 228

                 ....*..
gi 490522029 270 GALAGTV 276
Cdd:cd06312  229 GKILFAI 235
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
27-298 3.28e-14

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: 71.70  E-value: 3.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd19972    2 IGLAVANLQADFFNQIKQSVEAEAKKK-GYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDLIAKHwkanagwdlnKDGQIQYVLLKGEPGHPDAEART---TY 183
Cdd:cd19972   81 IPVIAVDRNPEDAPGDT-----FIATDSVAAAKELGEWVIKQ----------TGGKGEIAILHGQLGTTPEVDRTkgfQE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 184 VIKELNDKGIKTEQlqldTAMWDTAQA-KDKMDAWLSGPNankIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALP 261
Cdd:cd19972  146 ALAEAPGIKVVAEQ----TADWDQDEGfKVAQDMLQANPN---ITVFFGQSDAMALGAAQAVKVAGLDHkIWVVGFDGDV 218
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 490522029 262 EALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:cd19972  219 AGLKAVKDGVLDATMTQQTQKMGRLAVDSAIDLLNGK 255
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
26-302 3.55e-14

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 71.55  E-value: 3.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKDA-SASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARG 104
Cdd:cd06321    1 VIGVTVQDLGNPFFVAMVRGAEEAAaEINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 105 QNIPIVffnkepsrkALDSYDKAY--YVGTDSKESGIIQGDLIAKhwkanagwDLNKDGQIqyVLLKGEPGHPD------ 176
Cdd:cd06321   81 AGIIVV---------AVDVAAEGAdaTVTTDNVQAGYLACEYLVE--------QLGGKGKV--AIIDGPPVSAVidrvng 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 177 -----AEARTTYVIKELNDKGIKTEQLqldTAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHNKSS 251
Cdd:cd06321  142 ckealAEYPGIKLVDDQNGKGSRAGGL---SVMTRMLTAHPDVDG------------VFAINDPGAIGALLAAQQAGRDD 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490522029 252 IPVFGVDALPEALALVK--SGALAGTVLNDANNQAKATFDLAKNLAAGKGAAD 302
Cdd:cd06321  207 IVITSVDGSPEAVAALKreGSPFIATAAQDPYDMARKAVELALKILNGQEPAP 259
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
20-263 6.06e-14

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 71.38  E-value: 6.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  20 AAQAADRIGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKslAINLVDPAAAGTVI 99
Cdd:COG1609   57 RTGRTRTIGVVVPDLSNPFFAELLRGIEEAARER-GYQLLLANSDEDPEREREALRLLLSRRVD--GLILAGSRLDDARL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 100 EKARGQNIPIVFFNKEPSRKALDSydkayyVGTDSKESGiiqgDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEA 179
Cdd:COG1609  134 ERLAEAGIPVVLIDRPLPDPGVPS------VGVDNRAGA----RLATEH--------LIELGHRRIAFIGGPADSSSARE 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 180 RTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNKsSIP----VF 255
Cdd:COG1609  196 RLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGP--RPTAIFCANDLMALGALRALREAGL-RVPedvsVV 272

                 ....*...
gi 490522029 256 GVDALPEA 263
Cdd:COG1609  273 GFDDIPLA 280
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
63-256 2.75e-13

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


Pssm-ID: 380654 [Multi-domain]  Cd Length: 313  Bit Score: 69.26  E-value: 2.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  63 SQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPsrkaldSYDKAYYVGTDSKESGIIQG 142
Cdd:cd19999   42 ADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPV------SSPDAINVVIDQYKWAAIQA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 143 DLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEAR---TTYVIKElnDKGIKTeqLQLDTAMWDTAQAKDKMDAWLS 219
Cdd:cd19999  116 QWLAEQ--------LGGKGNI--VAINGVAGNPANEARvkaADDVFAK--YPGIKV--LASVPGGWDQATAQQVMATLLA 181
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490522029 220 gpNANKIEVVIaNNDAMAMGAVEALKAHNKSSIPVFG 256
Cdd:cd19999  182 --TYPDIDGVL-TQDGMAEGVLRAFQAAGKDPPVMTG 215
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
34-276 2.85e-13

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: 68.84  E-value: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  34 YDDNFMSVVRKAIeKDASASPDVQLLMNDSQN-DQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFF 112
Cdd:cd19965    9 TTNPFFQPVKKGM-DDACELLGAECQFTGPQTfDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 113 NKEpsrkALDSYDKAY-YVGTDSKESGIIQGDLIAKhwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDK 191
Cdd:cd19965   88 NVD----APGGENARLaFVGQDLYPAGYVLGKRIAE---------KFKPGGGHVLLGISTPGQSALEQRLDGIKQALKEY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 192 GIKTEQLQLDTAMwDTAQAKDKMDAWLSG-PNANkieVVIANNDAMAMGAVEALKAHN-KSSIPVFGVDALPEALALVKS 269
Cdd:cd19965  155 GRGITYDVIDTGT-DLAEALSRIEAYYTAhPDIK---AIFATGAFDTAGAGQAIKDLGlKGKVLVGGFDLVPEVLQGIKA 230

                 ....*..
gi 490522029 270 GALAGTV 276
Cdd:cd19965  231 GYIDFTI 237
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
26-297 3.70e-13

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: 68.48  E-value: 3.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKDASAsPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQ 105
Cdd:cd06305    1 TIAVVRNGTSGDWDQQALQGAVAEAEK-LGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKEPSRKAL---DSYDKAyyVGTDSkesgiiqGDLIAKhwkanagwDLNKDGQIQYVLLKGEPghPDAEARTT 182
Cdd:cd06305   80 GIPVVTFDTDSQVPGVnniTQDDYA--LGTLS-------LGQLVK--------DLNGEGNIAVFNVFGVP--PLDKRYDI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 183 YVIKELNDKGIKTEQLQLDTAMWDTAQ-AKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALP 261
Cdd:cd06305  141 YKAVLKANPGIKKIVAELGDVTPNTAAdAQTQVEALLKKYPEGGIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISN 220
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490522029 262 EALALVK--SGALAGTVLNDANNQAKATFDLAKNLAAG 297
Cdd:cd06305  221 QDLELMAdeGSPWVATAAQDPALIGTVAVRNVARKLAG 258
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
38-276 4.59e-13

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: 68.43  E-value: 4.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  38 FMSVVRKAIEKDASASPDVQLLMNDSQNDQS--KQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKE 115
Cdd:cd19970   13 FFIEMEKGARKHAKEANGYELLVKGIKQETDieQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 116 PSRKALDSYDKAY-YVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELNDKGIK 194
Cdd:cd19970   93 LDADALKEGGINVpFVGPDNRQGAYLAGDYLAKK--------LGKGGKV--AIIEGIPGADNAQQRKAGFLKAFEEAGMK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 195 TEQLQldTAMWDTAQAKDKMDAWLSG-PNankIEVVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGAL 272
Cdd:cd19970  163 IVASQ--SANWEIDEANTVAANLLTAhPD---IRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKM 237

                 ....
gi 490522029 273 AGTV 276
Cdd:cd19970  238 LATI 241
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
27-263 8.06e-13

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: 67.54  E-value: 8.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKslAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06267    2 IGLIVPDISNPFFAELLRGIEDAARER-GYSLLLCNTDEDPEREREYLRLLLSRRVD--GIILAPSSLDDELLEELLAAG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayyVGTDSKESGIIQGD-LIAK-HWKanagwdlnkdgqIqyVLLKGEPGHPDAEARTTYV 184
Cdd:cd06267   79 IPVVLIDRRLDGLGVDS------VVVDNYAGAYLATEhLIELgHRR------------I--AFIGGPLDLSTSRERLEGY 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 185 IKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNKsSIP----VFGVDAL 260
Cdd:cd06267  139 RDALAEAGLPVDPELVVEGDFSEESGYEAARELLALPP--RPTAIFAANDLMAIGALRALRELGL-RVPedisVVGFDDI 215

                 ...
gi 490522029 261 PEA 263
Cdd:cd06267  216 PLA 218
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
36-276 1.01e-12

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: 67.63  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  36 DNFMsvvrkaieKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVD-PAAAGTVIEKARGQNIPIVFFNK 114
Cdd:cd06324   19 TRFM--------QAAAKDLGIELEVLYANRNRFKMLELAEELLARPPKPDYLILVNeKGVAPELLELAEQAKIPVFLINN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 115 EPSRKALDSYDK-----AYYVGT---DSKESGIiqgdLIAKHWkANAGWDLNKDGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06324   91 DLTDEERALLGKprekfKYWLGSivpDNEQAGY----LLAKAL-IKAARKKSDDGKIRVLAISGDKSTPASILREQGLRD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIkTEQLQLDTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNK---SSIPVFGVDALPEA 263
Cdd:cd06324  166 ALAEHPD-VTLLQIVYANWSEDEAYQKTEKLLQ--RYPDIDIVWAANDAMALGAIDALEEAGLkpgKDVLVGGIDWSPEA 242
                        250
                 ....*....|...
gi 490522029 264 LALVKSGALAGTV 276
Cdd:cd06324  243 LQAVKDGELTASV 255
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
62-325 1.03e-11

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: 64.65  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsrKALDSYDkAYYVGTDSKESGIIQ 141
Cdd:cd06300   41 NSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFD-----GAVTSPD-AYNVSNDQVEWGRLG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 142 GDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELnDKGIKTEQLQLDTAMWDTAQAKDKMDAWL-SG 220
Cdd:cd06300  115 AKWLFEA--------LGGKGNV--LVVRGIAGAPASADRHAGVKEAL-AEYPGIKVVGEVFGGWDEATAQTAMLDFLaTH 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 221 PNANKievvIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKsgalagtvLNDANNQAKATF----DLAKNLAA 296
Cdd:cd06300  184 PQVDG----VWTQGGEDTGVLQAFQQAGRPPVPIVGGDENGFAKQWWK--------HPKKGLTGAAVWpppaIGAAGLEV 251
                        250       260
                 ....*....|....*....|....*....
gi 490522029 297 GKGAADGTDWKIenKVVRIPYVGVDKDNL 325
Cdd:cd06300  252 ALRLLEGQGPKP--QSVLLPPPLITNDDA 278
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
27-325 1.07e-11

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


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 64.32  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAieKDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06317    3 ALVQINQQAQFFNQINQGA--QAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNkepsrKALDSYDKAYYVGTDSKESGIIQGDLIAKHWKANagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06317   81 IPVIAYD-----AVIPSDFQAAQVGVDNLEGGKEIGKYAADYIKAE----LGGQAKIGVVGALSSLIQNQRQKGFEEALK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIKTE---QLQLDTAMwdtAQAKDKMDAwlsgpNANkIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPE 262
Cdd:cd06317  152 ANPGVEIVATvdgQNVQEKAL---SAAENLLTA-----NPD-LDAIYATGEPALLGAVAAVRSQGRQgKIKVFGWDLTKQ 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490522029 263 -ALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKgaadgtdwKIEnKVVRIPYVGVDKDNL 325
Cdd:cd06317  223 aIFLGIDEGVLQAVVQQDPEKMGYEAVKAAVKAIKGE--------DVE-KTIDVPPTIVTKENV 277
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
62-276 1.16e-11

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


Pssm-ID: 380624 [Multi-domain]  Cd Length: 278  Bit Score: 64.28  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEpsrkALDSyDKAYYVGTDSKESGIIQ 141
Cdd:cd19969   37 PATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDSD----APES-KRISYVGTDNYEAGYAA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 142 GDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPD---------AEARTTYVIKELNDKGIKTEQLQLDTAMwdtAQAKD 212
Cdd:cd19969  112 AEKLAEL--------LGGKGKVAVLTGPGQPNHEErvegfkeafAEYPGIEVVAVGDDNDDPEKAAQNTSAL---LQAHP 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490522029 213 KMDAWLsGPNANKievvianndamAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTV 276
Cdd:cd19969  181 DLVGIF-GVDASG-----------GVGAAQAVREAGKTGkVKIVAFDDDPETLDLIKDGVIDASI 233
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
1-279 2.17e-11

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 63.74  E-value: 2.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   1 MNKKVLTLSAVMSCMLFGTAAQAADRIGVTIYKYDDNFMSVVRKAIEKDASASP-DVQLLMNDSQNDQSKQNDQIDVLLA 79
Cdd:PRK09701   1 MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGvSVDIFASPSEGDFQSQLQLFEDLSN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  80 KGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDSYDKAY--YVGTDSKESGIIQGDLIAKHWKANAGwdl 157
Cdd:PRK09701  81 KNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKKAGGNVeaFVTTDNVAVGAKGASFIIDKLGAEGG--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 158 nkdgqiQYVLLKGEPGHPDAEAR---TTYVIKElnDKGIKTEQLQldTAMWDTAQAKDKMDAWLS-GPNankIEVVIANN 233
Cdd:PRK09701 158 ------EVAIIEGKAGNASGEARrngATEAFKK--ASQIKLVASQ--PADWDRIKALDVATNVLQrNPN---IKAIYCAN 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 490522029 234 DAMAMGAVEALK-AHNKSSIPVFGVDALPEALALVKSGALAGTVLND 279
Cdd:PRK09701 225 DTMAMGVAQAVAnAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQN 271
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
62-323 3.60e-10

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


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 59.56  E-value: 3.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsrKALDSYDKAYYVGTDSKESGIIQ 141
Cdd:cd20005   38 DTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFD-----SGVPSDLPLATVATDNYAAGALA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 142 GDLIAKhwkanagwdlNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDK--GIKTEQLQLDTAmwDTAQAKDKMDAWLS 219
Cdd:cd20005  113 ADHLAE----------LIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKypDIKVVNVQYGVG--DHAKAADIAKAILQ 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 220 G-PNankIEVVIANNDAMAMGAVEALKAHNK-SSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAG 297
Cdd:cd20005  181 AnPD---LKGIYATNEGAAIGVANALKEMGKlGKIKVVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAAVKALKG 257
                        250       260
                 ....*....|....*....|....*.
gi 490522029 298 KGAAdgtdwkienKVVRIPYVGVDKD 323
Cdd:cd20005  258 EEVE---------KLIDTGAKWYDKD 274
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
64-280 1.27e-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: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 54.93  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  64 QNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNkepsrKALDSYDKAYYVGTDSKESGIIQGD 143
Cdd:cd20004   40 EDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIID-----SDLGGDAVISFVATDNYAAGRLAAK 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 144 LIAKhwkanagwDLNKDGQIqyVLLKGEPGHPDAEART---TYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSG 220
Cdd:cd20004  115 RMAK--------LLNGKGKV--ALLRLAKGSASTTDRErgfLEALKKLAPGLKVVDDQYAGGTVGEARSSAENLLNQYPD 184
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490522029 221 PNAnkievVIANNDAMAMGAVEALKAHNKSSIPVF-GVDALPEALALVKSGALAGTVLNDA 280
Cdd:cd20004  185 VDG-----IFTPNESTTIGALRALRRLGLAGKVKFiGFDASDLLLDALRAGEISALVVQDP 240
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
65-298 2.14e-08

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: 54.51  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  65 NDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDSydkayYVGTDSKESGIIQGDL 144
Cdd:cd06306   41 TNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNGIDSPKVAA-----RVLVDFYDMGYLAGEY 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 145 IAKHwkanagwdlNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTeqlqLDTAMWDT--AQAKDKMDAWL-SGP 221
Cdd:cd06306  116 LVEH---------HPGKPVKVAWFPGPAGAGWAEDREKGFKEALAGSNVEI----VATKYGDTgkAVQLNLVEDALqAHP 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490522029 222 NANkievVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:cd06306  183 DID----YIVGNAVAAEAAVGALREAGLTGkVKVVSTYLTPGVYRGIKRGKILAAPSDQPVLQGRIAVDQAVRALEGK 256
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
26-302 9.69e-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: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 52.62  E-value: 9.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  26 RIGVTIYKYDDNFMSVVRKAIEKdASASPDVQLLMN--DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKAR 103
Cdd:cd20008    1 KIAVIVKDTDSEYWQTVLKGAEK-AAKELGVEVTFLgpATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 104 gQNIPIVFFNkepSRKALDSYDKAYyvGTDSKESGIIQGDLIAKHWKANAGwdlnKDGQIqyVLLKGEPGHPDAEARTTY 183
Cdd:cd20008   80 -AGIPVVLVD---SGANTDDYDAFL--ATDNVAAGALAADELAELLKASGG----GKGKV--AIISFQAGSQTLVDREEG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 184 VIKEL--NDKGIKTEQLQLDTAmwDTAQAKDKM-DAWLSGPNANKIevvIANNDAMAMGAVEALKAHNKS-SIPVFGVDA 259
Cdd:cd20008  148 FRDYIkeKYPDIEIVDVQYSDG--DIAKALNQTtDLLTANPDLVGI---FGANNPSAVGVAQALAEAGKAgKIVLVGFDS 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 490522029 260 LPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGKGAAD 302
Cdd:cd20008  223 SPDEVALLKSGVIKALVVQDPYQMGYEGVKTAVKALKGEEIVE 265
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
1-325 1.29e-07

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 52.44  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   1 MNKKVLTLSAVMSCMLFGTAAQAAD-RIGVTIykyDDNFMSVVRK--AIEKDASASPDVQLLMNDSQNDQSKQNDQIDVL 77
Cdd:PRK10355   1 MKIKNILLTLCASLLLTSVAAHAKEvKIGMAI---DDLRLERWQKdrDIFVKKAESLGAKVFVQSANGNEETQMSQIENM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  78 LAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDsydkaYYVGTDSKESGIIQGDLIakhwkanagwdL 157
Cdd:PRK10355  78 INRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADID-----FYISFDNEKVGELQAKAL-----------V 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 158 NKDGQIQYVLLKGEPGHPDAE---ARTTYVIKELNDKG-IKTEQLQLDTAmWDTAQAKDKMDAWLSGpNANKIEVVIANN 233
Cdd:PRK10355 142 DKVPQGNYFLMGGSPVDNNAKlfrAGQMKVLKPYIDSGkIKVVGDQWVDG-WLPENALKIMENALTA-NNNKIDAVVASN 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 234 DAMAMGAVEALKAHNKS-SIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLaaGKGAADGTDWKIENKV 312
Cdd:PRK10355 220 DATAGGAIQALSAQGLSgKVAISGQDADLAAIKRIVAGTQTMTVYKPITKLANTAAEIAVEL--GNGEEPKANTTLNNGL 297
                        330
                 ....*....|....*...
gi 490522029 313 VRIPY-----VGVDKDNL 325
Cdd:PRK10355 298 KDVPSrlltpIDVNKNNI 315
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
58-263 3.21e-07

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: 50.64  E-value: 3.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  58 LLMNDSQNDQSKQNDQIDVLLAKGVKSLAINlvdpAAAGT---VIEKARGQNIPIVFFNKEPSRKALDsydkayYVGTDS 134
Cdd:cd06289   32 VFLANTGEDPERQRRFLRRMLEQGVDGLILS----PAAGTtaeLLRRLKAWGIPVVLALRDVPGSDLD------YVGIDN 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 135 KESGiiqgDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARttyviKELNDKGIKTEQLQLDTAMW-----DTAQ 209
Cdd:cd06289  102 RLGA----QLATEH--------LIALGHRRIAFLGGLSDSSTRRER-----LAGFRAALAEAGLPLDESLIvpgpaTREA 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490522029 210 AKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKSS---IPVFGVDALPEA 263
Cdd:cd06289  165 GAEAARELLD--AAPPPTAVVCFNDLVALGAMLALRRRGLEPgrdIAVVGFDDVPEA 219
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
27-246 5.31e-07

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: 50.33  E-value: 5.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEkDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLainLVDPAAAGT-VIEKARGQ 105
Cdd:cd06280    2 IGLIVPDITNPFFTTIARGIE-DAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGI---ILAPSAGPSrELKRLLKH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 106 NIPIVFFNKEPSRKALDSydkayyVGTDSKESGIIqgdlIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVI 185
Cdd:cd06280   78 GIPIVLIDREVEGLELDL------VAGDNREGAYK----AVKH--------LIELGHRRIGLITGPLEISTTRERLAGYR 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490522029 186 KELNDKGIKTEQ---LQLDTAMWDTAQAkdkMDAWLSGPNAnkIEVVIANNDAMAMGAVEALKA 246
Cdd:cd06280  140 EALAEAGIPVDEsliFEGDSTIEGGYEA---VKALLDLPPR--PTAIFATNNLMAVGALRALRE 198
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
27-254 5.49e-07

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: 50.06  E-value: 5.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEKDASASPDVQLLMNDSQNDQsKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06311    2 IGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNAN-EQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEpsrkaLDSYDKAYYVGTDSKESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06311   81 IPVVNFDRG-----LNVLIYDLYVAGDNPGMGVVSAEYIGKK--------LGGKGNV--VVLEVPSSGSVNEERVAGFKE 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490522029 187 ELNDK-GIKTEQLQLDTAMWDTAqAKDKMDAWLSGPnanKIEVVIANNDAMAMGAVEALKAHNKSSIPV 254
Cdd:cd06311  146 VIKGNpGIKILAMQAGDWTREDG-LKVAQDILTKNK---KIDAVWAADDDMAIGVLQAIKEAGRTDIKV 210
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
24-263 5.57e-07

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: 50.20  E-value: 5.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029   24 ADRIGVtIYKYDDN--FMSVVrKAIEKDASASP-DVQLLMNDSQNDQSKQndQIDVLLAKGVKSLAINLVDPAAAgTVIE 100
Cdd:pfam00532   1 TLKLGA-LVPQLDEpfFQDLV-KGITKAAKDHGfDVFLLAVGDGEDTLTN--AIDLLLASGADGIIITTPAPSGD-DITA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  101 KARGQNIPIVFFNKepsrkALDSYDKAYYVGTDSKESGiiqgdliakhwkANAGWDLNKDGQIQYVLLKGEP-GHPDAEA 179
Cdd:pfam00532  76 KAEGYGIPVIAADD-----AFDNPDGVPCVMPDDTQAG------------YESTQYLIAEGHKRPIAVMAGPaSALTARE 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  180 RTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHNKSSIP----- 253
Cdd:pfam00532 139 RVQGFMAALAAAGREVKIYHVATGDNDIPDAALAANAMLvSHPT---IDAIVAMNDEAAMGAVRALLKQGRVKIPdivgi 215
                         250
                  ....*....|....
gi 490522029  254 ----VFGVDALPEA 263
Cdd:pfam00532 216 ginsVVGFDGLSKA 229
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
58-253 1.10e-06

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: 49.06  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  58 LLMNdSQNDQSKQNDQIDVLLAkgvkslaiNLVD---PAAAGTVIEKARGQNIPIVFFNKEPSrkaldsyDKAYYVGTDS 134
Cdd:cd06291   33 ILCN-SNEDEEKEKEYLEMLKR--------NKVDgiiLGSHSLDIEEYKKLNIPIVSIDRYLS-------EGIPSVSSDN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 135 KESGIiqgdLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKM 214
Cdd:cd06291   97 YQGGR----LAAEH--------LIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFSEEDAYELA 164
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 490522029 215 DAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKsSIP 253
Cdd:cd06291  165 KELLE--KYPDIDGIFASNDLLAIGVLKALQKLGI-RVP 200
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
27-263 1.11e-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: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEkDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKslAINLVDPAAAGTVIEKARGQN 106
Cdd:cd06285    2 IGVLVSDLSNPFYAELVEGIE-DAARERGYTVLLADTGDDPERELAALDSLLSRRVD--GLIITPARDDAPDLQELAARG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayyVGTDSkESGiiqGDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06285   79 VPVVLVDRRIGDTALPS------VTVDN-ELG---GRLATRH--------LLELGHRRIAVVAGPLNASTGRDRLRGYRR 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPN---AnkievVIANNDAMAMGAVEALKAHNKsSIP----VFGVDA 259
Cdd:cd06285  141 ALAEAGLPVPDERIVPGGFTIEAGREAAYRLLSRPErptA-----VFAANDLMAIGVLRAARDLGL-RVPedlsVVGFDD 214

                 ....
gi 490522029 260 LPEA 263
Cdd:cd06285  215 IPLA 218
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
63-316 1.15e-06

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


Pssm-ID: 380525 [Multi-domain]  Cd Length: 296  Bit Score: 49.16  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  63 SQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPSRKALDsydkaYYV-GTDSKESGIIQ 141
Cdd:cd06302   38 TQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSDAPPSARD-----YFVnQADDEGLGEAL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 142 GDLIAKhwkanagwdlNKDGQIQYVLLKGEPGHPD----AEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAW 217
Cdd:cd06302  113 VDSLAK----------EIGGKGKVAILSGSLTATNlnawIKAMKEYLKSKYPDIELVDTYYTDDDQQKAYTQAQNLIQAY 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 218 lsgPNankIEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVdALP-EALALVKSGALAGTVLNDANNQAKATFDLAKNLA 295
Cdd:cd06302  183 ---PD---LKGIIGVSTTAPPAAAQAVEEAGKTgKVAVTGI-GLPnTARPYLKDGSVKEGVLWDPAKLGYLTVYAAYQLL 255
                        250       260
                 ....*....|....*....|.
gi 490522029 296 AGKGAADGTDWKIENKVVRIP 316
Cdd:cd06302  256 KGKGFTEDSDDVGTGGKVKVD 276
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
38-247 4.81e-06

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: 47.25  E-value: 4.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  38 FMSVVRkAIEkDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLainLVDPAAAGTVIEK--ARGQNIPIVFFNKE 115
Cdd:cd06275   14 FAEVVR-GVE-DACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGL---LLMCSEMTDDDAEllAALRSIPVVVLDRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 116 PSRKALDSydkayyVGTDSkESGiiqGDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIKT 195
Cdd:cd06275   89 IAGDNADA------VLDDS-FQG---GYLATRH--------LIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEV 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490522029 196 EQLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAH 247
Cdd:cd06275  151 PPSWIVEGDFEPEGGYEAMQRLLSQPP--RPTAVFACNDMMALGALRAAQEQ 200
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
63-256 5.70e-06

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


Pssm-ID: 380653 [Multi-domain]  Cd Length: 302  Bit Score: 47.28  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  63 SQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPsrkaldSYDKAYYVGTDSKESGIIQG 142
Cdd:cd19998   41 SGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVV------DEPCAYNVNTDQAKAGEQTA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 143 DLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEART---TYVIKELNDKGIKTEQlqldTAMWDTAQAKDKMDAWLs 219
Cdd:cd19998  115 QWLVDK--------LGGKGNI--LMVRGVPGTSVDRDRYegaKEVFKKYPDIKVVAEY----YGNWDDGTAQKAVADAL- 179
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490522029 220 gPNANKIEVVIAnNDAMAmGAVEALKAHNKSSIPVFG 256
Cdd:cd19998  180 -AAHPDVDGVWT-QGGET-GVIKALQAAGHPLVPVGG 213
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
27-267 6.98e-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: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 46.84  E-value: 6.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEKDASASpDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLainLVDPAAAGTVIEKARGQN 106
Cdd:cd06290    2 IGVLVPDIDSPFYSEILNGIEEVLAES-GYTLIVSTSHWNADRELEILRLLLARKVDGI---IVVGGFGDEELLKLLAEG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayyVGTDSKESGIIqgdlIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIK 186
Cdd:cd06290   78 IPVVLVDRELEGLNLPV------VNVDNEQGGYN----ATNH--------LIDLGHRRIVHISGPEDHPDAQERYAGYRR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 187 ELNDKGIK-----------TEQLQLDtAMWDTAQAKDKMDAwlsgpnankievVIANNDAMAMGAVEALKAHnKSSIP-- 253
Cdd:cd06290  140 ALEDAGLEvdprlivegdfTEESGYE-AMKKLLKRGGPFTA------------IFAANDLMALGAMKALREA-GIRVPdd 205
                        250
                 ....*....|....*.
gi 490522029 254 --VFGVDALPEALALV 267
Cdd:cd06290  206 vsVIGFDDLPFSKYTT 221
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-263 2.06e-05

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


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 45.22  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  58 LLMNDSQNDQskQNDQIDVLLAKGVKSLAINLVDPAAAgtVIEKARGQNIPIVFFNKEPSRKALDSydkayyVGTDSKES 137
Cdd:cd06278   33 LLFNVDDEDD--VDDALRQLLQYRVDGVIVTSATLSSE--LAEECARRGIPVVLFNRVVEDPGVDS------VSCDNRAG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 138 GiiqgDLIAKHwkanagwdLNKDGQIQYVLLKGEPGHPDAEARTTYVIKELNDKGIktEQLQLDTAMWDTAQAKDKMDAW 217
Cdd:cd06278  103 G----RLAADL--------LLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGL--PPPAVEAGDYSYEGGYEAARRL 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490522029 218 LSGPNAnkIEVVIANNDAMAMGAVEALKAHNKSSIP----VFGVDALPEA 263
Cdd:cd06278  169 LAAPDR--PDAIFCANDLMALGALDAARQEGGLVVPedisVVGFDDIPMA 216
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
62-327 3.72e-05

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: 44.54  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  62 DSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEPS-RKALDSYdkAYYVGTDSKESGII 140
Cdd:cd06316   37 DANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKLVFMDNVPDgLEAGKDY--VSVVSSDNRGNGQI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 141 QGDLIAKHwkanagwdLNKDGQIQYVllkgepGHP---------DAEARTTyvIKELNDkGIKTEQLQLDTAMWDTAQ-A 210
Cdd:cd06316  115 AAELLAEA--------IGGKGKVGII------YHDadfyatnqrDKAFKDT--LKEKYP-DIKIVAEQGFADPNDAEEvA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 211 KDKMDAWlsgPNANKIEVVIannDAMAMGAVEALKAHNKSSIPVFGVDALPE-ALALVKSGALAGTVLNDANNQAKATFD 289
Cdd:cd06316  178 SAMLTAN---PDIDGIYVSW---DTPALGVISALRAAGRSDIKITTVDLGTEiALDMAKGGNVKGIGAQRPYDQGVAEAL 251
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490522029 290 LAKNLAAGKGAAdgtdwkienKVVRIPYVGVDKDNLAE 327
Cdd:cd06316  252 AAALALLGKEVP---------PFIGVPPLAVTKDNLLE 280
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
173-263 7.84e-05

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


Pssm-ID: 380486 [Multi-domain]  Cd Length: 269  Bit Score: 43.67  E-value: 7.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 173 GHPDAEARTTYVIKELNDKGIKTEQLQLDTAmWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKsSI 252
Cdd:cd01544  129 GEEIEDPRLRAFREYMKEKGLYNEEYIYIGE-FSVESGYEAMKELLK--EGDLPTAFFVASDPMAIGALRALQEAGI-KV 204
                         90
                 ....*....|....*
gi 490522029 253 P----VFGVDALPEA 263
Cdd:cd01544  205 PedisIISFNDIEVA 219
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
163-263 1.71e-04

Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 41.55  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  163 IQYVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSG-PNAnkievVIANNDAMAMGAV 241
Cdd:pfam13377  10 IALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGAlPTA-----VFVANDEVALGVL 84
                          90       100
                  ....*....|....*....|....*.
gi 490522029  242 EALKAHNKsSIP----VFGVDALPEA 263
Cdd:pfam13377  85 QALREAGL-RVPedlsVIGFDDSPLA 109
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
31-275 2.53e-04

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


Pssm-ID: 380628 [Multi-domain]  Cd Length: 285  Bit Score: 42.07  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  31 IYKYDDN-FMSVVRKAIEKDASA-SPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIP 108
Cdd:cd19973    5 ITKTDTNpFFVKMKEGAQKAAKAlGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 109 IVFFNK--EPsrkaLDSYDKAYyvGTDSKESGIiqgdLIAKHWKANAGwdlNKDGQIqyVLLKGEPGHPDAEAR-----T 181
Cdd:cd19973   85 VIALDTptDP----IDAADATF--ATDNFKAGV----LIGEWAKAALG---AKDAKI--ATLDLTPGHTVGVLRhqgflK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 182 TYVIKELNDKGIKTEQ----LQLDTAMWDTAQAKDKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKAHNKSS-IPVFG 256
Cdd:cd19973  150 GFGIDEKDPESNEDEDdsqvVGSADTNGDQAKGQTAMENLLQ--KDPDINLVYTINEPAAAGAYQALKAAGKEKgVLIVS 227
                        250
                 ....*....|....*....
gi 490522029 257 VDALPEALALVKSGALAGT 275
Cdd:cd19973  228 VDGGCPGVKDVKDGIIGAT 246
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
55-277 3.29e-04

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 41.81  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  55 DVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFFNKEpsrkaLDSYDKAYYVGTDS 134
Cdd:cd20006   33 DLEFLGPESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSP-----VNSKKADSFVATDN 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 135 KESGIIQGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELNDKG---IKTEQLQLDtamwDTAQAK 211
Cdd:cd20006  108 YEAGKKAGEKLASL--------LGEKGKV--AIVSFVKGSSTAIEREEGFKQALAEYPnikIVETEYCDS----DEEKAY 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490522029 212 DKMDAWLSgpNANKIEVVIANNDAMAMGAVEALKA-HNKSSIPVFGVDALPEALALVKSGALAGTVL 277
Cdd:cd20006  174 EITKELLS--KYPDINGIVALNEQSTLGAARALKElGLGGKVKVVGFDSSVEEIQLLEEGIIDALVV 238
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
27-246 1.97e-03

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: 39.46  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  27 IGVTIYKYDDNFMSVVRKAIEkDASASPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKSLAINLVdpAAAGTVIEKARGQN 106
Cdd:cd06283    2 IGVIVADITNPFSSLLLKGIE-DVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPT--GNNNDAYLELAQKG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 107 IPIVFFNKEPSRKALDSydkayyVGTDSKESGIIQGDLIAKHwkanaGWDlnkdgqiQYVLLKGEPGHPDA-EARTTYVI 185
Cdd:cd06283   79 LPVVLVDRQIEPLNWDT------VVTDNYDATYEATEHLKEQ-----GYE-------RIVFVTEPIKGISTrRERLQGFL 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490522029 186 KELNDKGIKTEQLQLDTAmwDTAQAKDKMDAWLSGPNANKIeVVIANNDAMAMGAVEALKA 246
Cdd:cd06283  141 DALARYNIEGDVYVIEIE--DTEDLQQALAAFLSQHDGGKT-AIFAANGVVLLRVLRALKA 198
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
66-298 3.54e-03

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: 38.37  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029  66 DQSKQNDQIDVLLAKGVKSLAINLVDPAAAGTVIEKARGQNIPIVFfnkepsrkaLDSY--DKAY---YVGTDSKESGII 140
Cdd:cd20007   41 DPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVT---------VDTTlgDPSFvlsQIASDNVAGGAL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 141 QGDLIAKHwkanagwdLNKDGQIqyVLLKGEPGHPDAEARTTYVIKELnDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSg 220
Cdd:cd20007  112 AAEALAEL--------IGGKGKV--LVINSTPGVSTTDARVKGFAEEM-KKYPGIKVLGVQYSENDPAKAASIVAAALQ- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 221 pnANK-IEVVIANNDAMAMGAVEALKAHNKS-SIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLAAGK 298
Cdd:cd20007  180 --ANPdLAGIFGTNTFSAEGAAAALRNAGKTgKVKVVGFDASPAQVEQLKAGTIDALIAQKPAEIGYLAVEQAVAALTGK 257
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
170-258 4.00e-03

ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose 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: 380511 [Multi-domain]  Cd Length: 268  Bit Score: 38.30  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 170 GEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNanKIEVVIANNDAMAMGAVEALKAHNK 249
Cdd:cd06288  124 GPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHGDWGRESGYEAAKRLLSAPD--RPTAIFCGNDRMAMGVYQAAAELGL 201
                         90
                 ....*....|...
gi 490522029 250 sSIP----VFGVD 258
Cdd:cd06288  202 -RVPedlsVVGFD 213
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
170-277 5.64e-03

ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators; This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. 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: 380518 [Multi-domain]  Cd Length: 273  Bit Score: 38.00  E-value: 5.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522029 170 GEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWL-SGPNankIEVVIANNDAMAMGAVEALKAHN 248
Cdd:cd06295  131 GDPPHPEVADRLQGYRDALAEAGLEADPSLLLSCDFTEESGYAAMRALLdSGTA---FDAIFAASDLIAMGAIRALRERG 207
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490522029 249 KsSIP----VFGVDALPEA------LALVK-SGALAGTVL 277
Cdd:cd06295  208 I-SVPgdvaVVGYDDIPLAayfrppLTTVRqDLALAGRLL 246
 
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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