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Conserved domains on  [gi|16130089|ref|NP_416656|]
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DNA-binding transcriptional dual regulator GalS [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

HTH-type transcriptional regulator GalS( domain architecture ID 11484695)

HTH-type transcriptional regulator GalS is a repressor of the mgl operon

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
1-346 0e+00

HTH-type transcriptional regulator GalS;


:

Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 725.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    1 MITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
Cdd:PRK10401   1 MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPGMVLINRVVPGYAHRCVCLDN 160
Cdd:PRK10401  81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  161 LSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLTA 240
Cdd:PRK10401 161 VSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLQLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  241 VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCFM 320
Cdd:PRK10401 241 VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNLDPRASHCFM 320
                        330       340
                 ....*....|....*....|....*.
gi 16130089  321 PTLVRRHSVATRQNAAAITNSTNQAM 346
Cdd:PRK10401 321 PTLVRRHSVATRQNAAAITNSTNQAM 346
 
Name Accession Description Interval E-value
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
1-346 0e+00

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 725.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    1 MITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
Cdd:PRK10401   1 MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPGMVLINRVVPGYAHRCVCLDN 160
Cdd:PRK10401  81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  161 LSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLTA 240
Cdd:PRK10401 161 VSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLQLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  241 VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCFM 320
Cdd:PRK10401 241 VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNLDPRASHCFM 320
                        330       340
                 ....*....|....*....|....*.
gi 16130089  321 PTLVRRHSVATRQNAAAITNSTNQAM 346
Cdd:PRK10401 321 PTLVRRHSVATRQNAAAITNSTNQAM 346
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
61-327 3.52e-132

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


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 377.63  E-value: 3.52e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPG 140
Cdd:cd06270   1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 141 MVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPD 220
Cdd:cd06270  81 LVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGDFT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 221 MPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLAT 300
Cdd:cd06270 161 IEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQAAA 240
                       250       260
                ....*....|....*....|....*..
gi 16130089 301 ELALQGAAGNIDPRaSHCFMPTLVRRH 327
Cdd:cd06270 241 ELALNLAYGEPLPI-SHEFTPTLIERD 266
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
1-330 2.57e-124

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 360.28  E-value: 2.57e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   1 MITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
Cdd:COG1609   3 RVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD-NIPgMVLINRVVPGYAHRCVCLD 159
Cdd:COG1609  83 IEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEaGIP-VVLIDRPLPDPGVPSVGVD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 160 NLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLT 239
Cdd:COG1609 162 NRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPT 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 240 AVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCF 319
Cdd:COG1609 242 AIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLL 321
                       330
                ....*....|.
gi 16130089 320 MPTLVRRHSVA 330
Cdd:COG1609 322 PPELVVRESTA 332
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
171-329 3.23e-32

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: 118.21  E-value: 3.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   171 LLNNGHQRIGYL--SSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRnlQLTAVFAYNDNM 248
Cdd:pfam13377   2 LAELGHRRIALIgpEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGA--LPTAVFVANDEV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   249 AAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:pfam13377  80 ALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERES 159

                  .
gi 16130089   329 V 329
Cdd:pfam13377 160 T 160
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
2-71 7.80e-31

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 111.52  E-value: 7.80e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089      2 ITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSD 71
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
 
Name Accession Description Interval E-value
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
1-346 0e+00

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 725.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    1 MITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
Cdd:PRK10401   1 MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPGMVLINRVVPGYAHRCVCLDN 160
Cdd:PRK10401  81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  161 LSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLTA 240
Cdd:PRK10401 161 VSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLQLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  241 VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCFM 320
Cdd:PRK10401 241 VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNLDPRASHCFM 320
                        330       340
                 ....*....|....*....|....*.
gi 16130089  321 PTLVRRHSVATRQNAAAITNSTNQAM 346
Cdd:PRK10401 321 PTLVRRHSVATRQNAAAITNSTNQAM 346
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
1-343 2.86e-152

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 431.49  E-value: 2.86e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    1 MITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
Cdd:PRK10727   1 MATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPGMVLINRVVPGYAHRCVCLDN 160
Cdd:PRK10727  81 VEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASLMKQIPGMVLINRILPGFENRCIALDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  161 LSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLTA 240
Cdd:PRK10727 161 RYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRGRNFTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  241 VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCFM 320
Cdd:PRK10727 241 VACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADNRPLPEITNVFS 320
                        330       340
                 ....*....|....*....|...
gi 16130089  321 PTLVRRHSVATRQNAAAITNSTN 343
Cdd:PRK10727 321 PTLVRRHSVSTPSLEASHHATSD 343
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
61-327 3.52e-132

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


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 377.63  E-value: 3.52e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPG 140
Cdd:cd06270   1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 141 MVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPD 220
Cdd:cd06270  81 LVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGDFT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 221 MPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLAT 300
Cdd:cd06270 161 IEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQAAA 240
                       250       260
                ....*....|....*....|....*..
gi 16130089 301 ELALQGAAGNIDPRaSHCFMPTLVRRH 327
Cdd:cd06270 241 ELALNLAYGEPLPI-SHEFTPTLIERD 266
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
1-330 2.57e-124

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 360.28  E-value: 2.57e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   1 MITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
Cdd:COG1609   3 RVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD-NIPgMVLINRVVPGYAHRCVCLD 159
Cdd:COG1609  83 IEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEaGIP-VVLIDRPLPDPGVPSVGVD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 160 NLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLT 239
Cdd:COG1609 162 NRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPT 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 240 AVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCF 319
Cdd:COG1609 242 AIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLL 321
                       330
                ....*....|.
gi 16130089 320 MPTLVRRHSVA 330
Cdd:COG1609 322 PPELVVRESTA 332
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
61-324 4.10e-80

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: 245.12  E-value: 4.10e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD-NIP 139
Cdd:cd06267   1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAaGIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTP 219
Cdd:cd06267  81 -VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 220 DMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLA 299
Cdd:cd06267 160 SEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAA 239
                       250       260
                ....*....|....*....|....*
gi 16130089 300 TELALQGAAGNIDPRASHCFMPTLV 324
Cdd:cd06267 240 AELLLERIEGEEEPPRRIVLPTELV 264
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
61-328 2.79e-66

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


Pssm-ID: 380631 [Multi-domain]  Cd Length: 268  Bit Score: 209.80  E-value: 2.79e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD--NI 138
Cdd:cd19976   1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLLKeeKI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 139 PgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGT 218
Cdd:cd19976  81 P-VVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 219 PDMPGGEAAMVELLGRNlQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKL 298
Cdd:cd19976 160 SSLEGGYKAAEELLKSK-NPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQE 238
                       250       260       270
                ....*....|....*....|....*....|
gi 16130089 299 ATELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:cd19976 239 AAKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
1-330 2.39e-65

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 209.97  E-value: 2.39e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    1 MITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
Cdd:PRK10703   1 MATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   81 VDLVAQQhQKYVLI-GNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD--NIPgMVLINRVVPGYAHRCVC 157
Cdd:PRK10703  81 VEKNCYQ-KGYTLIlCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEyrHIP-MVVMDWGEAKADFTDAI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  158 LDN-LSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNL 236
Cdd:PRK10703 159 IDNaFEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQKH 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  237 QLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRAS 316
Cdd:PRK10703 239 RPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQT 318
                        330
                 ....*....|....
gi 16130089  317 HCFMPTLVRRHSVA 330
Cdd:PRK10703 319 IEVHPRLVERRSVA 332
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
61-329 7.05e-63

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: 201.30  E-value: 7.05e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSkALSDDELAQFMDN--I 138
Cdd:cd06285   1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITP-ARDDAPDLQELAArgV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 139 PgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLS----SSHGIEddamRKAGWMSALKEQDIIPPESWI 214
Cdd:cd06285  80 P-VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAgplnASTGRD----RLRGYRRALAEAGLPVPDERI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 215 GAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIAS 294
Cdd:cd06285 155 VPGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYE 234
                       250       260       270
                ....*....|....*....|....*....|....*
gi 16130089 295 MAKLATELALQGAAGNIDPRASHCFMPTLVRRHSV 329
Cdd:cd06285 235 MGRRAAELLLQLIEGGGRPPRSITLPPELVVREST 269
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
61-328 1.12e-61

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


Pssm-ID: 380630 [Multi-domain]  Cd Length: 269  Bit Score: 198.16  E-value: 1.12e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQF-MDNIP 139
Cdd:cd19975   1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLkNMNIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSsshGIEDDAM----RKAGWMSALKEQDIIPPESWIG 215
Cdd:cd19975  81 -VVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMIS---GPLDDPNagypRYEGYKKALKDAGLPIKENLIV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 216 AGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASM 295
Cdd:cd19975 157 EGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEM 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 16130089 296 AKLATELALQGaAGNIDPRASHCFMPT-LVRRHS 328
Cdd:cd19975 237 GKKAVELLLDL-IKNEKKEEKSIVLPHqIIERES 269
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
61-328 4.18e-61

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: 196.71  E-value: 4.18e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDD--ELAQFMDNI 138
Cdd:cd06275   1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDdaELLAALRSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 139 PgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGT 218
Cdd:cd06275  81 P-VVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 219 PDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKL 298
Cdd:cd06275 160 FEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGEL 239
                       250       260       270
                ....*....|....*....|....*....|.
gi 16130089 299 ATELALQgAAGNIDPRASHCFM-PTLVRRHS 328
Cdd:cd06275 240 AVELLLD-RIENKREEPQSIVLePELIERES 269
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
61-328 4.62e-59

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: 191.29  E-value: 4.62e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPg 140
Cdd:cd06290   1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLAEGIP- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 141 MVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPD 220
Cdd:cd06290  80 VVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDFT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 221 MPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLAT 300
Cdd:cd06290 160 EESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTAA 239
                       250       260       270
                ....*....|....*....|....*....|.
gi 16130089 301 E--LALQGAAGNIDPRAShcfMPT-LVRRHS 328
Cdd:cd06290 240 EilLELIEGKGRPPRRII---LPTeLVIRES 267
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
61-305 1.67e-57

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: 187.34  E-value: 1.67e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFmdNIPg 140
Cdd:cd06291   1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYKKL--NIP- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 141 MVLINRVVPGYAHrCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPD 220
Cdd:cd06291  78 IVSIDRYLSEGIP-SVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 221 MPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLAT 300
Cdd:cd06291 157 EEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEAV 236

                ....*
gi 16130089 301 ELALQ 305
Cdd:cd06291 237 ELLLK 241
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
61-302 1.34e-56

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


Pssm-ID: 380632 [Multi-domain]  Cd Length: 264  Bit Score: 184.66  E-value: 1.34e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDN-IP 139
Cdd:cd19977   1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEKLVKSgIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGY----LSSSHGIEddamRKAGWMSALKEQDIIPPESWIg 215
Cdd:cd19977  81 -VVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFitypLELSTRQE----RLEGYKAALADHGLPVDEELI- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 216 AGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASM 295
Cdd:cd19977 155 KHVDRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEI 234

                ....*..
gi 16130089 296 AKLATEL 302
Cdd:cd19977 235 GRKAAEL 241
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
61-305 8.53e-55

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: 180.15  E-value: 8.53e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFM-DNIP 139
Cdd:cd06280   1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLkHGIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTP 219
Cdd:cd06280  81 -IVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGDS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 220 DMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLA 299
Cdd:cd06280 160 TIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIA 239

                ....*.
gi 16130089 300 TELALQ 305
Cdd:cd06280 240 AQLLLE 245
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
61-328 9.14e-55

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


Pssm-ID: 380507 [Multi-domain]  Cd Length: 267  Bit Score: 180.04  E-value: 9.14e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPg 140
Cdd:cd06284   1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELSKRYP- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 141 MVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPD 220
Cdd:cd06284  80 IVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGDFS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 221 MPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLAT 300
Cdd:cd06284 160 FEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAA 239
                       250       260       270
                ....*....|....*....|....*....|..
gi 16130089 301 EL---ALQGAAgnidPRASHCFMPT-LVRRHS 328
Cdd:cd06284 240 ELlleKIEGEG----VPPEHIILPHeLIVRES 267
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
61-328 1.28e-54

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: 180.05  E-value: 1.28e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFF-GALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIP 139
Cdd:cd06288   1 TIGLITDDIATTPFaGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLPPELTDIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTP 219
Cdd:cd06288  81 -LVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHGDW 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 220 DMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLA 299
Cdd:cd06288 160 GRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGRRA 239
                       250       260
                ....*....|....*....|....*....
gi 16130089 300 TELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:cd06288 240 AELLLDGIEGEPPEPGVIRVPCPLIERES 268
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
61-328 2.52e-53

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


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 176.69  E-value: 2.52e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPG 140
Cdd:cd06293   1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 141 MVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPD 220
Cdd:cd06293  81 VVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEVVRELSAPD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 221 MP--GGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKL 298
Cdd:cd06293 161 ANaeLGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELGRA 240
                       250       260       270
                ....*....|....*....|....*....|
gi 16130089 299 ATELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:cd06293 241 AADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
61-327 3.35e-53

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: 176.22  E-value: 3.35e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIV----HSKALSDDELAQfmD 136
Cdd:cd06289   1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILspaaGTTAELLRRLKA--W 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 137 NIPgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYL----SSSHGIEddamRKAGWMSALKEQDIIPPES 212
Cdd:cd06289  79 GIP-VVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLgglsDSSTRRE----RLAGFRAALAEAGLPLDES 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 213 WIGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPI 292
Cdd:cd06289 154 LIVPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHP 233
                       250       260       270
                ....*....|....*....|....*....|....*
gi 16130089 293 ASMAKLATELALQGAAGNIDPRASHCFMPTLVRRH 327
Cdd:cd06289 234 REIGRRAARLLLRRIEGPDTPPERIIIEPRLVVRE 268
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
61-328 7.29e-53

Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to 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 I 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: 380515 [Multi-domain]  Cd Length: 273  Bit Score: 175.53  E-value: 7.29e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVV----MDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERhAIEVLIRQ-RCNALIVHSKALSDDELAQFM 135
Cdd:cd06292   1 LIGYVVpelpGGFSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEID-YYRDLVRSrRVDGFVLASTRHDDPRVRYLH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 136 D-NIPgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWI 214
Cdd:cd06292  80 EaGVP-FVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 215 GAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIAS 294
Cdd:cd06292 159 VEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDE 238
                       250       260       270
                ....*....|....*....|....*....|....
gi 16130089 295 MAKLATELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:cd06292 239 IGRAVVDLLLAAIEGNPSEPREILLQPELVVRES 272
lacI PRK09526
lac repressor; Reviewed
2-337 2.08e-52

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 176.34  E-value: 2.08e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    2 ITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAV 81
Cdd:PRK09526   6 VTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQIAAAI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   82 DLVAQQHQKYVLIGN-SYHEAEKERHAIEVLIRQRCNALIVhSKALSDDE---LAQFMDNIPgmVLINRVVPGYAHRCVC 157
Cdd:PRK09526  86 KSRADQLGYSVVISMvERSGVEACQAAVNELLAQRVSGVII-NVPLEDADaekIVADCADVP--CLFLDVSPQSPVNSVS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  158 LDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPpeSWIGAGTPDMPGGEAAMVELLGRNLQ 237
Cdd:PRK09526 163 FDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQP--IAVREGDWSAMSGYQQTLQMLREGPV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  238 LTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGniDPRASH 317
Cdd:PRK09526 241 PSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALSQG--QAVKGS 318
                        330       340
                 ....*....|....*....|.
gi 16130089  318 CFMPT-LVRRHSVATRQNAAA 337
Cdd:PRK09526 319 QLLPTsLVVRKSTAPPNTQTA 339
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
61-328 1.30e-50

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


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 169.66  E-value: 1.30e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVH-SK-ALSDDELA---QFM 135
Cdd:cd01541   1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEpTKsALPNPNLDlyeELQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 136 D-NIPgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGylssshGI--EDD---AMRKAGWMSALKEQDIIP 209
Cdd:cd01541  81 KkGIP-VVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIA------GIfkSDDlqgVERYQGFIKALREAGLPI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 210 PESWIGA-GTPDM--PGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLT 286
Cdd:cd01541 154 DDDRILWySTEDLedRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLT 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 16130089 287 TVRYPIASMAKLATELALQGAAGNiDPRASHCFMPTLVRRHS 328
Cdd:cd01541 234 SVVHPKEELGRKAAELLLRMIEEG-RKPESVIFPPELIERES 274
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
61-328 1.40e-48

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


Pssm-ID: 380488 [Multi-domain]  Cd Length: 265  Bit Score: 164.29  E-value: 1.40e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKE-RHAIEVLIRQRCNALIV-HSKALSDDELAQFMDNI 138
Cdd:cd01574   1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDEDDPASvREALDRLLSQRVDGIIViAPDEAVLEALRRLPPGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 139 PgMVLINrVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGT 218
Cdd:cd01574  81 P-VVIVG-SGPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLPPPPVVEGDWS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 219 PDmpGGEAAMVELLgRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKL 298
Cdd:cd01574 159 AA--SGYRAGRRLL-DDGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRR 235
                       250       260       270
                ....*....|....*....|....*....|
gi 16130089 299 ATELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:cd01574 236 AVELLLALIEGPAPPPESVLLPPELVVRES 265
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
4-329 2.88e-48

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 165.26  E-value: 2.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    4 IRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVDL 83
Cdd:PRK10423   1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   84 VAQQhQKYVLI-GNSYHEAEKERHAIEVLIRQRCNALIV---HSKALSDDELAQFmDNIPgMVLINRVvPGYAHRCVCLD 159
Cdd:PRK10423  81 SCFE-RGYSLVlCNTEGDEQRMNRNLETLMQKRVDGLLLlctETHQPSREIMQRY-PSVP-TVMMDWA-PFDGDSDLIQD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  160 N-LSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQL 238
Cdd:PRK10423 157 NsLLGGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPLRP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  239 TAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAgniDPRASH- 317
Cdd:PRK10423 237 QAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMA---QPTLQQq 313
                        330
                 ....*....|....
gi 16130089  318 --CFMPTLVRRHSV 329
Cdd:PRK10423 314 rlQLTPELMERGSV 327
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
108-328 4.97e-47

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


Pssm-ID: 380487 [Multi-domain]  Cd Length: 270  Bit Score: 160.41  E-value: 4.97e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 108 IEVLIRQRCNALIVhSKALSDD-ELAQFMD--NIPgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSS 184
Cdd:cd01545  49 RRFLSRSRPDGVIL-TPPLSDDpALLDALDelGIP-YVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAG 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 185 SHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIP 264
Cdd:cd01545 127 PPDHGASAERLEGFRDALAEAGLPLDPDLVVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVP 206
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130089 265 LHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:cd01545 207 DDLSVAGFDDSPIARLVWPPLTTVRQPIAEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
61-328 5.23e-47

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


Pssm-ID: 380522 [Multi-domain]  Cd Length: 268  Bit Score: 160.14  E-value: 5.23e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPG 140
Cdd:cd06299   1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIAQGLP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 141 MVLINRVVPGYAHRCVCL-DNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTP 219
Cdd:cd06299  81 VVFVDREVEGLGGVPVVTsDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 220 DMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLA 299
Cdd:cd06299 161 RQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRRA 240
                       250       260       270
                ....*....|....*....|....*....|
gi 16130089 300 TELALqgAAGNIDPRASHCFMPT-LVRRHS 328
Cdd:cd06299 241 VELLL--ALIENGGRATSIRVPTeLIPRES 268
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
28-306 6.02e-47

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 161.32  E-value: 6.02e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   28 VSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHA 107
Cdd:PRK11041   4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  108 IEVLIRQRCNALIVHSKALSDDELAQFMDNIPGMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSsshG 187
Cdd:PRK11041  84 VNLIITKQIDGMLLLGSRLPFDASKEEQRNLPPMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIA---G 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  188 IEDDAM---RKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIP 264
Cdd:PRK11041 161 PEEMPLchyRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGLRVP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 16130089  265 LHLSIIGFDDIPIARYTDPQLTTV---RYPIASMAKLATELALQG 306
Cdd:PRK11041 241 QDLSIIGFDDIDLAQYCDPPLTTVaqpRYEIGREAMLLLLEQLQG 285
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
61-328 7.86e-47

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: 159.62  E-value: 7.86e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERhAIEVLIRQRCNALIVHSKALSDDELAQFMD-NIP 139
Cdd:cd06278   1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDD-ALRQLLQYRVDGVIVTSATLSSELAEECARrGIP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPesWIGAGTP 219
Cdd:cd06278  80 -VVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPPP--AVEAGDY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 220 DMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALK-DNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKL 298
Cdd:cd06278 157 SYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARqEGGLVVPEDISVVGFDDIPMAAWPSYDLTTVRQPIEEMAEA 236
                       250       260       270
                ....*....|....*....|....*....|
gi 16130089 299 ATELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:cd06278 237 AVDLLLERIENPETPPERRVLPGELVERGS 266
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
73-301 3.12e-45

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: 380500 [Multi-domain]  Cd Length: 275  Bit Score: 155.86  E-value: 3.12e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  73 FFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEvLIRQRCNALIVHSKALSDDELAQFMDNIPGMVLINRVVPGYA 152
Cdd:cd06277  20 FFSELIDGIEREARKYGYNLLISSVDIGDDFDEILKE-LTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNYFEDLN 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 153 HRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELL 232
Cdd:cd06277  99 FDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEPEFVVSVGPEGAYKDMKALL 178
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 233 GRNLQL-TAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATE 301
Cdd:cd06277 179 DTGPKLpTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVR 248
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
61-326 1.34e-44

ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to CcpA which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree.


Pssm-ID: 380509 [Multi-domain]  Cd Length: 262  Bit Score: 153.86  E-value: 1.34e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPg 140
Cdd:cd06286   1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDWEVIEPYAKYGP- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 141 MVLINRVvPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYL------SSSHGIEddamRKAGWMSALKEQDIIPPESWI 214
Cdd:cd06286  80 IVLCEET-DSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYClgrpesSSASTQA----RLKAYQDVLGEHGLSLREEWI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 215 GAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYtdPQLTTVRYPIAS 294
Cdd:cd06286 155 FTNCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL--LNLTTIDQPLEE 232
                       250       260       270
                ....*....|....*....|....*....|..
gi 16130089 295 MAKLATELALQgaAGNIDPRASHCFMPTLVRR 326
Cdd:cd06286 233 MGKEAFELLLS--QLESKEPTKKELPSKLIER 262
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
61-314 4.70e-43

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


Pssm-ID: 380484 [Multi-domain]  Cd Length: 259  Bit Score: 149.57  E-value: 4.70e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD-NIP 139
Cdd:cd01542   1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKlKIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLINRVVPGYAhrCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHgiEDDAM---RKAGWMSALKEQDIIPPEswIGA 216
Cdd:cd01542  81 -VVVLGQEHEGFS--CVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDE--EDIAVgvaRKQGYLDALKEHGIDEVE--IVE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 217 GTPDMPGGEAAMVELLGRNlQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMA 296
Cdd:cd01542 154 TDFSMESGYEAAKELLKEN-KPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAG 232
                       250
                ....*....|....*...
gi 16130089 297 KLATELALQGAAGNIDPR 314
Cdd:cd01542 233 EKAAELLLDMIEGEKVPK 250
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
61-328 1.14e-42

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


Pssm-ID: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 148.81  E-value: 1.14e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIV----HSKALsDDELAQFmd 136
Cdd:cd06273   1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILvgsdHDPEL-FELLEQR-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 137 NIPgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAM-RKAGWMSALKEQDIIPPESWIG 215
Cdd:cd06273  78 QVP-YVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRARaRLAGIRDALAERGLELPEERVV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 216 AGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASM 295
Cdd:cd06273 157 EAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREI 236
                       250       260       270
                ....*....|....*....|....*....|...
gi 16130089 296 AKLATELALQGAAGNiDPRASHCFMPTLVRRHS 328
Cdd:cd06273 237 GELAARYLLALLEGG-PPPKSVELETELIVRES 268
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
61-328 3.94e-40

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


Pssm-ID: 380489 [Multi-domain]  Cd Length: 269  Bit Score: 142.25  E-value: 3.94e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD-NIP 139
Cdd:cd01575   1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAaGIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gmvlinrVV--------PGYAhrCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIED-DAMRKAGWMSALKEQDIIPP 210
Cdd:cd01575  81 -------VVetwdlpddPIDM--AVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPLP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 211 ESWIGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRY 290
Cdd:cd01575 152 LVLLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRV 231
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 16130089 291 PIASMAKLATELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:cd01575 232 PRYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
61-328 7.93e-40

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: 141.51  E-value: 7.93e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMD-----VSDAFFGALVKAVDLVAQQHQkyVLIGNSYHEAEKERHAIEvlirqRCNALIVHSKaLSDDELAQFM 135
Cdd:cd01544   1 TIGIIQWYseeeeLEDPYYLSIRLGIEKEAKKLG--YEIKTIFRDDEDLESLLE-----KVDGIIAIGK-FSKEEIEKLK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 136 DNIPGMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYL-----SSSHGIEDDAMRKAGWMSALKEQDIIPP 210
Cdd:cd01544  73 KLNPNIVFVDSNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIggkeyTSDDGEEIEDPRLRAFREYMKEKGLYNE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 211 EsWIGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRY 290
Cdd:cd01544 153 E-YIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHI 231
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 16130089 291 PIASMAKLATELALQGAAGNIDPrASHCFMPT-LVRRHS 328
Cdd:cd01544 232 PTEEMGRTAVRLLLERINGGRTI-PKKVLLPTkLIERES 269
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
61-329 1.35e-38

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


Pssm-ID: 380504 [Multi-domain]  Cd Length: 270  Bit Score: 138.14  E-value: 1.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDN--I 138
Cdd:cd06281   1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDPELAAALARldI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 139 PgMVLINRVVPGYAHRcVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGT 218
Cdd:cd06281  81 P-VVLIDRDLPGDIDS-VLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 219 PDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKL 298
Cdd:cd06281 159 FSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRA 238
                       250       260       270
                ....*....|....*....|....*....|..
gi 16130089 299 ATELALQGAAGNIDPRASHCFMPT-LVRRHSV 329
Cdd:cd06281 239 AAELLLDRIEGPPAGPPRRIVVPTeLILRDSC 270
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
2-326 1.88e-38

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 139.84  E-value: 1.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    2 ITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAV 81
Cdd:PRK10014   7 ITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   82 DLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD--NIPgMVLINRVVPGYAHRCVCLD 159
Cdd:PRK10014  87 TEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMAEekGIP-VVFASRASYLDDVDTVRPD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  160 NLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLT 239
Cdd:PRK10014 166 NMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVLECTSSQKQAAEAITALLRHNPTIS 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  240 AVFAYNDNMAAGALTALKDNGIA---------IPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGN 310
Cdd:PRK10014 246 AVVCYNETIAMGAWFGLLRAGRQsgesgvdryFEQQVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRMMQRITHE 325
                        330
                 ....*....|....*.
gi 16130089  311 IDPRASHCFMPTLVRR 326
Cdd:PRK10014 326 ETHSRNLIIPPRLIAR 341
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
61-329 4.91e-37

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


Pssm-ID: 380519 [Multi-domain]  Cd Length: 270  Bit Score: 133.94  E-value: 4.91e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD-NIP 139
Cdd:cd06296   1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSaGIP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLINRV-VPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGT 218
Cdd:cd06296  81 -FVLIDPVgEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREGD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 219 PDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKL 298
Cdd:cd06296 160 FTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGAV 239
                       250       260       270
                ....*....|....*....|....*....|..
gi 16130089 299 ATELALQGAAGnIDPRASHCFMPT-LVRRHSV 329
Cdd:cd06296 240 AVRLLLRLLEG-GPPDARRIELATeLVVRGST 270
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
61-322 2.17e-36

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


Pssm-ID: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 132.41  E-value: 2.17e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD--NI 138
Cdd:cd06282   1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSEALELLEeeGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 139 PgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDA-MRKAGWMSALKEQDIIPPEswIGAG 217
Cdd:cd06282  81 P-YVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSASDRArLRYQGYRDALKEAGLKPIP--IVEV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 218 TPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAK 297
Cdd:cd06282 158 DFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGR 237
                       250       260
                ....*....|....*....|....*...
gi 16130089 298 LATELALQGAAGNIDP---RASHCFMPT 322
Cdd:cd06282 238 AAADLLLAEIEGESPPtsiRLPHHLREG 265
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
62-314 4.40e-36

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: 131.60  E-value: 4.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  62 IGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD--NIP 139
Cdd:cd01537   2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARgqNVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLIN----RVVPGYAhrcVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIG 215
Cdd:cd01537  82 -VVFFDkepsRYDKAYY---VITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 216 AGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASM 295
Cdd:cd01537 158 TGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNL 237
                       250       260
                ....*....|....*....|
gi 16130089 296 AKLATELALQGA-AGNIDPR 314
Cdd:cd01537 238 GKTTFDLLLNLAdNWKIDNK 257
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
61-292 5.93e-36

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


Pssm-ID: 380521 [Multi-domain]  Cd Length: 268  Bit Score: 131.26  E-value: 5.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD-NIP 139
Cdd:cd06298   1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRsPVP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIE-DDAMRKAGWMSALKEQDIIPPESWIGAGT 218
Cdd:cd06298  81 -VVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYiNNDKKLQGYKRALEEAGLEFNEPLIFEGD 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130089 219 PDMPGGEAAMVELLGRNLqLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPI 292
Cdd:cd06298 160 YDYDSGYELYEELLESGE-PDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPL 232
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
61-324 7.83e-36

Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I 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: 380665 [Multi-domain]  Cd Length: 269  Bit Score: 130.75  E-value: 7.83e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVV----MDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYhEAEKERHAIEVLI-RQRCNALIVHSkALSDDELAQFM 135
Cdd:cd20010   1 AIGLVLpldpGDLGDPFFLEFLAGLSEALAERGLDLLLAPAP-SGEDELATYRRLVeRGRVDGFILAR-TRVNDPRIAYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 136 --DNIPgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESW 213
Cdd:cd20010  79 leRGIP-FVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 214 IGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIP-IARYTDPQLTTVRYPI 292
Cdd:cd20010 158 VREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLpALEYFSPPLTTTRSSL 237
                       250       260       270
                ....*....|....*....|....*....|..
gi 16130089 293 ASMAKLATELALQGAAGNIDPRASHCFMPTLV 324
Cdd:cd20010 238 RDAGRRLAEMLLALIDGEPAAELQELWPPELI 269
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
171-329 3.23e-32

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: 118.21  E-value: 3.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   171 LLNNGHQRIGYL--SSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRnlQLTAVFAYNDNM 248
Cdd:pfam13377   2 LAELGHRRIALIgpEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGA--LPTAVFVANDEV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   249 AAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:pfam13377  80 ALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERES 159

                  .
gi 16130089   329 V 329
Cdd:pfam13377 160 T 160
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
61-305 6.19e-32

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: 120.35  E-value: 6.19e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKAL-SDDELAQFMDNIP 139
Cdd:cd06283   1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNnNDAYLELAQKGLP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 140 gMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSS-HGIEDDAMRKAGWMSALKEQDIIPPESWIGAGT 218
Cdd:cd06283  81 -VVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPiKGISTRRERLQGFLDALARYNIEGDVYVIEIED 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 219 PDMPggEAAMVELLGRN-LQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAK 297
Cdd:cd06283 160 TEDL--QQALAAFLSQHdGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGK 237

                ....*...
gi 16130089 298 LATELALQ 305
Cdd:cd06283 238 AAAEILLE 245
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
61-328 7.29e-31

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


Pssm-ID: 380502 [Multi-domain]  Cd Length: 284  Bit Score: 118.08  E-value: 7.29e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMD-----VSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIrqrcNALIVHSKALSDDELAQFM 135
Cdd:cd06279   1 AIGVLLPDdlsyaFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAAV----DGFIVYGLSDDDPAVAALR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 136 D-NIPgMVLI-NRVVPGYAHrcVCLDNLSGARMATRMLLNNGHQRIGYLS-------------------SSHGIEDDamR 194
Cdd:cd06279  77 RrGLP-LVVVdGPAPPGIPS--VGIDDRAAARAAARHLLDLGHRRIAILSlrldrgrergpvsaerlaaATNSVARE--R 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 195 KAGWMSALKEQDIIPPESWIG-AGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFD 273
Cdd:cd06279 152 LAGYRDALEEAGLDLDDVPVVeAPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFD 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130089 274 DIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGnidPRASHCFMPT-LVRRHS 328
Cdd:cd06279 232 DIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPG---APPRPVILPTeLVVRAS 284
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
2-71 7.80e-31

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 111.52  E-value: 7.80e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089      2 ITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSD 71
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
61-305 1.24e-29

ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which 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: 380517 [Multi-domain]  Cd Length: 269  Bit Score: 114.22  E-value: 1.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVV--VMDVSDA---FFGALVKAVDLVAQQHQKYVLI--GNSyheAEKERHAIEVLIRQR-CNALIVhSKALSDDELA 132
Cdd:cd06294   1 TIGLVlpSSAEELFqnpFFSEVLRGISQVANENGYSLLLatGNT---EEELLEEVKRMVRGRrVDGFIL-LYSKEDDPLI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 133 QFMD--NIPgMVLINRvvPGYAHR--CVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDII 208
Cdd:cd06294  77 EYLKeeGFP-FVVIGK--PLDDNDvlYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 209 PPESWIGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTV 288
Cdd:cd06294 154 LDDDYILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSV 233
                       250
                ....*....|....*..
gi 16130089 289 RYPIASMAKLATELALQ 305
Cdd:cd06294 234 DINPYELGREAAKLLIN 250
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
57-298 1.27e-28

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: 111.96  E-value: 1.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  57 QVSDTIGVVV-MD------VSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVlirQRCNALIVHSKALSDD 129
Cdd:cd06295   1 QRSRTIAVVVpMDphgdqsITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLDS---GRADGLIVLGQGLDHD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 130 ELAQF-MDNIPgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDdAMRKAGWMSALKEQDII 208
Cdd:cd06295  78 ALRELaQQGLP-MVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEV-ADRLQGYRDALAEAGLE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 209 PPESWIGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTV 288
Cdd:cd06295 156 ADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTV 235
                       250
                ....*....|
gi 16130089 289 RYPIASMAKL 298
Cdd:cd06295 236 RQDLALAGRL 245
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
61-305 3.37e-26

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: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 105.32  E-value: 3.37e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMD---VSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKaLSDDELAQFMD- 136
Cdd:cd19974   1 NIAVLIPErffGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGE-ISKEYLEKLKEl 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 137 NIPgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGY---LSSSHGIEDdamRKAGWMSALKEQDI-IPPES 212
Cdd:cd19974  80 GIP-VVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFvgdINYTSSFMD---RYLGYRKALLEAGLpPEKEE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 213 WIGAGTPDmPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPI 292
Cdd:cd19974 156 WLLEDRDD-GYGLTEEIELPLKLMLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEVDK 234
                       250
                ....*....|...
gi 16130089 293 ASMAKLATELALQ 305
Cdd:cd19974 235 EAMGRRAVEQLLW 247
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
84-326 8.12e-25

ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to 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: 380496 [Multi-domain]  Cd Length: 266  Bit Score: 101.30  E-value: 8.12e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  84 VAQQHQKYVLIGNSYheaeKERH---AIEVLIRQRCNALIVHSKALSDDE-LAQFMDNIPgMVLINRVVPGYAhrCVCLD 159
Cdd:cd06272  26 ISKQGYNINLSICPY----KVGHlctAKGLFSENRFDGVIVFGISDSDIEyLNKNKPKIP-IVLYNRESPKYS--TVNVD 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 160 NLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQLT 239
Cdd:cd06272  99 NEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTLRGKGFIETCEKHGIHLSDSIIDSRGLSIEGGDNAAKKLLKKKTLPK 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 240 AVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNIDPRASHCF 319
Cdd:cd06272 179 AIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIAEESLRLILKLIEGRENEIQQLIL 258

                ....*..
gi 16130089 320 MPTLVRR 326
Cdd:cd06272 259 YPELIFR 265
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
61-328 2.23e-24

ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380520 [Multi-domain]  Cd Length: 268  Bit Score: 100.23  E-value: 2.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDNIPG 140
Cdd:cd06297   1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELFEEVIVPTEKP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 141 MVLINRVVPGYahRCVCLDNLSGARMATRMLLNNGHQRIG--YLSSSHGIEDDAM--RKAGWMSALKEQDIIPPESWIGA 216
Cdd:cd06297  81 VVLIDANSMGY--DCVYVDNVKGGFMATEYLAGLGEREYVffGIEEDTVFTETVFreREQGFLEALNKAGRPISSSRMFR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 217 GTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIAryTDPQLTTVRYPIASMA 296
Cdd:cd06297 159 IDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWA--ASPGLTTVRQPVEEMG 236
                       250       260       270
                ....*....|....*....|....*....|..
gi 16130089 297 KLATELALQGAAGNIDPRASHCFMPTLVRRHS 328
Cdd:cd06297 237 EAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
4-304 2.56e-24

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 101.26  E-value: 2.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    4 IRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVDL 83
Cdd:PRK14987   8 LQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   84 VAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQF-MDNIPGMVLINRVVPGYaHRCVCLDNLS 162
Cdd:PRK14987  88 VTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIeVAGIPVVELMDSQSPCL-DIAVGFDNFE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  163 GARMATRMLLNNGHQRIGYLSSSHGiEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEaAMVELLGRNLQLTAVF 242
Cdd:PRK14987 167 AARQMTTAIIARGHRHIAYLGARLD-ERTIIKQKGYEQAMLDAGLVPYSVMVEQSSSYSSGIE-LIRQARREYPQLDGVF 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130089  243 AYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELAL 304
Cdd:PRK14987 245 CTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLL 306
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
5-56 2.62e-21

Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.


Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 85.54  E-value: 2.62e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 16130089   5 RDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPNANAQALAT 56
Cdd:cd01392   1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
PRK11303 PRK11303
catabolite repressor/activator;
6-327 7.72e-21

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 91.48  E-value: 7.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    6 DVARQAGVSVATVSRVLNNST---LVSADTREAVMKAVSELDYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVD 82
Cdd:PRK11303   5 EIARLAGVSRTTASYVINGKAkqyRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAKYLE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   83 LVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDN--IPgMVLINRVVPGYAHRCVCLDN 160
Cdd:PRK11303  85 RQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTSLPPEHPFYQRLQNdgLP-IIALDRALDREHFTSVVSDD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  161 LSGARMATRMLLNNGHQRIGY------LSSSHgieddaMRKAGWMSALKEQDIIPpeSWIGAGTPDMPGGEAAMVELLGR 234
Cdd:PRK11303 164 QDDAEMLAESLLKFPAESILLlgalpeLSVSF------EREQGFRQALKDDPREV--HYLYANSFEREAGAQLFEKWLET 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  235 NLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDipiarytDPQLTTVRYPIASM-------AKLATELALQGA 307
Cdd:PRK11303 236 HPMPDALFTTSYTLLQGVLDVLLERPGELPSDLAIATFGD-------NELLDFLPCPVNAVaqqhrliAERALELALAAL 308
                        330       340
                 ....*....|....*....|
gi 16130089  308 AGNIDPRAShcfmPTLVRRH 327
Cdd:PRK11303 309 DEPRKPKPG----LTRIRRN 324
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
1-305 1.80e-20

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 90.59  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    1 MITIRDVARQAGVSVATVSRVLNNS-TL-VSADTREAVMKAVSELDYRpNANAQALATQVSDTIGVVVM-------DVSD 71
Cdd:PRK10339   1 MATLKDIAIEAGVSLATVSRVLNDDpTLnVKEETKHRILEIAEKLEYK-TSSARKLQTGAVNQHHILAIysyqqelEIND 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   72 AFFGALVKAVDlvAQQHQKYVLIGNSY-HEAEKERHAIEVLIrqrcnaLIVHSKALSDDELAQFMDNIpgmVLINRVVPG 150
Cdd:PRK10339  80 PYYLAIRHGIE--TQCEKLGIELTNCYeHSGLPDIKNVTGIL------IVGKPTPALRAAASALTDNI---CFIDFHEPG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  151 YAHRCVCLDNLSGARMATRMLLNNGHQRIGYLssshGIEDDA----MRKAGWM------SALKEQDIippesWIGaGTPD 220
Cdd:PRK10339 149 SGYDAVDIDLARISKEIIDFYINQGVNRIGFI----GGEDEPgkadIREVAFAeygrlkQVVREEDI-----WRG-GFSS 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  221 MPGGEAAMvELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLAT 300
Cdd:PRK10339 219 SSGYELAK-QMLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGV 297

                 ....*
gi 16130089  301 ELALQ 305
Cdd:PRK10339 298 NLLYE 302
LacI pfam00356
Bacterial regulatory proteins, lacI family;
3-48 4.30e-19

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 79.60  E-value: 4.30e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 16130089     3 TIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKAVSELDYRPN 48
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
61-314 1.31e-18

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


Pssm-ID: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 84.18  E-value: 1.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSkALSDDELAQFM--DNI 138
Cdd:cd06274   1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAP-STPPDDIYYLCqaAGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 139 PgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQRIGYL---SSSHGIEDdamRKAGWMSALKEQDIIPPESWIG 215
Cdd:cd06274  80 P-VVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLggrPELPSTAE---RIRGFRAALAEAGITEGDDWIL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 216 AGTPDMPGGEAAMVELLGRNLQL-TAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIAS 294
Cdd:cd06274 156 AEGYDRESGYQLMAELLARLGGLpQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDHDE 235
                       250       260
                ....*....|....*....|
gi 16130089 295 MAKLATELALQGAAGNIDPR 314
Cdd:cd06274 236 IAEHAFELLDALIEGQPEPG 255
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
61-309 1.37e-18

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: 84.16  E-value: 1.37e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHskALSDDELAQFMD---- 136
Cdd:cd01536   1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIA--PVDSEALVPAVKkana 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 137 -NIPgMVLINRVVPGYAHR--CVCLDNLSGARMATRMLLN--NGHQRIGYLSSSHGIEDDAMRKAGWMSALKE-QDIIPP 210
Cdd:cd01536  79 aGIP-VVAVDTDIDGGGDVvaFVGTDNYEAGKLAGEYLAEalGGKGKVAILEGPPGSSTAIDRTKGFKEALKKyPDIEIV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 211 ESWIGAGTPDMpgGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIplHLSIIGFDDIP--IARYTDPQLT-T 287
Cdd:cd01536 158 AEQPANWDRAK--ALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTG--DIKIVGVDGTPeaLKAIKDGELDaT 233
                       250       260
                ....*....|....*....|..
gi 16130089 288 VRYPIASMAKLATELALQGAAG 309
Cdd:cd01536 234 VAQDPYLQGYLAVEAAVKLLNG 255
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
99-304 2.75e-17

ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to 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: 380495 [Multi-domain]  Cd Length: 264  Bit Score: 80.55  E-value: 2.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  99 HEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFM--DNIPgMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGH 176
Cdd:cd06271  40 FEEAES*VPIRDLVETGSADGVILSEIEPNDPRVQFLtkQNFP-FVAHGRSD*PIGHAWVDIDNEAGAYEAVERLAGLGH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 177 QRIGYLS--SSHGIEDDAMRkaGWMSALKEQDIIPpesWIGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALT 254
Cdd:cd06271 119 RRIAFIVppARYSPHDRRLQ--GYVRA*RDAGLTG---YPLDADTTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVA 193
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 16130089 255 ALKDNGIAIPLHLSIIGFDDIP-IARYTDPQLTTVRYPIASMAKLATELAL 304
Cdd:cd06271 194 GLQAAGLKIGEDVSIIGKDSAPfLGAMITPPLTTVHAPIAEAGRELAKALL 244
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
59-317 3.86e-17

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: 80.25  E-value: 3.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    59 SDTIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELA--QFMD 136
Cdd:pfam00532   1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITakAEGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   137 NIPGMVLINRVVPGYAHRCVCLDNLSGARMATRMLLNNGHQR-IGYLS--SSHGIEDDamRKAGWMSALKEQDIIPPESW 213
Cdd:pfam00532  81 GIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAgpASALTARE--RVQGFMAALAAAGREVKIYH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   214 IGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNG-IAIPL-----HLSIIGFDDIpiaryTDPQLTT 287
Cdd:pfam00532 159 VATGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDivgigINSVVGFDGL-----SKAQDTG 233
                         250       260       270
                  ....*....|....*....|....*....|
gi 16130089   288 VRYPIASMAKLATELALQGAAGNIDPRASH 317
Cdd:pfam00532 234 LYLSPLTVIQLPRQLLGIKASDMVYQWIPK 263
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
61-314 1.14e-16

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: 79.20  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHskALSDDELAQFMD---- 136
Cdd:COG1879  35 TIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVS--PVDPDALAPALKkaka 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 137 -NIPgMVLINRVVPGYAHRC-VCLDNLSGARMATRMLLN--NGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQ---DIIP 209
Cdd:COG1879 113 aGIP-VVTVDSDVDGSDRVAyVGSDNYAAGRLAAEYLAKalGGKGKVAILTGSPGAPAANERTDGFKEALKEYpgiKVVA 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 210 PESwigaGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHlsIIGFDDIPIARY---TDPQLT 286
Cdd:COG1879 192 EQY----ADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKGDVK--VVGFDGSPEALQaikDGTIDA 265
                       250       260
                ....*....|....*....|....*...
gi 16130089 287 TVRYPIASMAKLATELALQGAAGNIDPR 314
Cdd:COG1879 266 TVAQDPYLQGYLAVDAALKLLKGKEVPK 293
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
62-310 2.54e-15

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: 74.65  E-value: 2.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089    62 IGVVVMDVSDAFFGALVKAV-DLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHskALSDDELAQFMD---- 136
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAeEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVA--PVDPTALAPVLKkakd 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   137 -NIPgMVLINRVVPGYAH-RCVCLDNLSGARMATRMLLN--NGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQD---IIP 209
Cdd:pfam13407  79 aGIP-VVTFDSDAPSSPRlAYVGFDNEAAGEAAGELLAEalGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYpgiKVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   210 PESWIGAGTPDMpgGEAAMVELLGRNL-QLTAVFAYNDNMAAGALTALKDNGIAIPLHlsIIGFDDIPIARY--TDPQLT 286
Cdd:pfam13407 158 AEVEGTNWDPEK--AQQQMEALLTAYPnPLDGIISPNDGMAGGAAQALEAAGLAGKVV--VTGFDATPEALEaiKDGTID 233
                         250       260
                  ....*....|....*....|....*
gi 16130089   287 -TVRYPIASMAKLATELALQGAAGN 310
Cdd:pfam13407 234 aTVLQDPYGQGYAAVELAAALLKGK 258
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
61-314 1.06e-11

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: 64.49  E-value: 1.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAV-DLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVhsKALSDDELAQFMD--- 136
Cdd:cd06308   1 VIGFSQCSLNDPWRAAMNEEIkAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIV--SPNEADALTPVVKkay 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 137 --NIPgMVLINRVVPGY---AHrcVCLDNLSGARMATRML--LNNGHQRI----GYLSSSHGIEddamRKAGWMSALKEQ 205
Cdd:cd06308  79 daGIP-VIVLDRKVSGDdytAF--IGADNVEIGRQAGEYIaeLLNGKGNVveiqGLPGSSPAID----RHKGFLEAIAKY 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 206 DIIP-----PESWIGAGtpdmpgGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAipLHLSIIGFDDIPIARY 280
Cdd:cd06308 152 PGIKivasqDGDWLRDK------AIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGRE--KEIKIIGVDGLPEAGE 223
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 16130089 281 T---DPQLT-TVRYPiaSMAKLATELALQGAAGNIDPR 314
Cdd:cd06308 224 KavkDGILAaTFLYP--TGGKEAIEAALKILNGEKVPK 259
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
152-309 2.28e-10

Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I 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: 380664 [Multi-domain]  Cd Length: 266  Bit Score: 60.24  E-value: 2.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 152 AHRCVCLDNLSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVEL 231
Cdd:cd20009  94 PHAYFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAARRL 173
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130089 232 LGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAG 309
Cdd:cd20009 174 LRQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEG 251
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
85-291 5.46e-10

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


Pssm-ID: 380485 [Multi-domain]  Cd Length: 265  Bit Score: 59.14  E-value: 5.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  85 AQQHQKYVLignsYHEAEKERHAIEVLIRQRCNALIVHskALSDDELAQFMD-NIPgMVLINRVVPGYAHRCVCLDNLSG 163
Cdd:cd01543  24 AREHGPWSL----YLEPPGYEELLDLLKGWKGDGIIAR--LDDPELAEALRRlGIP-VVNVSGSRPEPGFPRVTTDNEAI 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 164 ARMATRMLLNNGHQRIGYLSSShGIEDDAMRKAGWMSALKEQDIiPPESWIGAGTPDMPGGEAAMVELLGRNLQL---TA 240
Cdd:cd01543  97 GRMAAEHLLERGFRHFAFCGFR-NAAWSRERGEGFREALREAGY-ECHVYESPPSGSSRSWEEEREELADWLKSLpkpVG 174
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 16130089 241 VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIP-IARYTDPQLTTVRYP 291
Cdd:cd01543 175 IFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDElICELSSPPLSSIALD 226
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
61-279 7.25e-10

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


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 58.80  E-value: 7.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAvdlvAQQHQK----YVLI---GNSYHEAEKERHAIEVLIRQRCNALIV---HSKA----- 125
Cdd:cd19970   1 KVALVMKSLANEFFIEMEKG----ARKHAKeangYELLvkgIKQETDIEQQIAIVENLIAQKVDAIVIapaDSKAlvpvl 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 126 ----------------LSDDELAQFMDNIPgmvlinrvvpgyahrCVCLDNLSGARMATRMLLNN--GHQRIGYLSSSHG 187
Cdd:cd19970  77 kkavdagiavinidnrLDADALKEGGINVP---------------FVGPDNRQGAYLAGDYLAKKlgKGGKVAIIEGIPG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 188 IEDDAMRKAGWMSALKEQD--IIPPES--WigagtpDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAi 263
Cdd:cd19970 142 ADNAQQRKAGFLKAFEEAGmkIVASQSanW------EIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKA- 214
                       250
                ....*....|....*.
gi 16130089 264 pLHLSIIGFDDIPIAR 279
Cdd:cd19970 215 -GKVLVVGFDNIPAVR 229
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
61-309 1.47e-08

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


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 55.06  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVH----SKALSDDELAQFMd 136
Cdd:cd06319   1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISptnsSAAPTVLDLANEA- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 137 NIPGMVLINRVVPGYAHRCVCLDNLSGAR-----MATRMLLNNGHQ-RIGYL----SSSHGIE-----DDAMRKAGWMSA 201
Cdd:cd06319  80 KIPVVIADIGTGGGDYVSYIISDNYDGGYqageyLAEALKENGWGGgSVGIIaipqSRVNGQArtagfEDALEEAGVEEV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 202 LKEQDiippeswigaGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAipLHLSIIGFDDIPIARYT 281
Cdd:cd06319 160 ALRQT----------PNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDGDPEALDL 227
                       250       260       270
                ....*....|....*....|....*....|.
gi 16130089 282 DPQLT---TVRYPIASMAKLATELALQGAAG 309
Cdd:cd06319 228 IKDGKldgTVAQQPFGMGARAVELAIQALNG 258
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
62-306 3.31e-08

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


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 54.20  E-value: 3.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  62 IGVV--VMDVSDAFFGA-LVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQR-----------CNALIVHSKALS 127
Cdd:cd01391   2 IGVVtsSLHQIREQFGIqRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNiagvigpgsssVAIVIQNLAQLF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 128 D------DELAQFMDNIPGMVLINRVVPGyahrcvclDNLSGARMATRMLLNNGhqriGYLSSSHGIEDDAM--RKAGWM 199
Cdd:cd01391  82 DipqlalDATSQDLSDKTLYKYFLSVVFS--------DTLGARLGLDIVKRKNW----TYVAAIHGEGLNSGelRMAGFK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 200 SALKEQDIIPPESWIgAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAipLHLSIIGFDDIPIAR 279
Cdd:cd01391 150 ELAKQEGICIVASDK-ADWNAGEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGWADRD 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 16130089 280 YTD-----PQLTTVRYPIASMAKLATELALQG 306
Cdd:cd01391 227 EVGyeveaNGLTTIKQQKMGFGITAIKAMADG 258
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
61-279 7.65e-08

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


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 52.66  E-value: 7.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALI---VHSKALSDDELAQFMDN 137
Cdd:cd06322   1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIIlapVDSGGIVPAIEAANEAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 138 IPGMVLINRVVPGYAHRCVCLDNLSGARMA----TRMLLNNGHQ--RIGYLSSSHGIEddamRKAGWMSALKEQDIIPPE 211
Cdd:cd06322  81 IPVFTVDVKADGAKVVTHVGTDNYAGGKLAgeyaLKALLGGGGKiaIIDYPEVESVVL----RVNGFKEAIKKYPNIEIV 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130089 212 SwIGAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHlsIIGFDDIPIAR 279
Cdd:cd06322 157 A-EQPGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDKIK--VIGFDGNPEAI 221
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
61-273 1.46e-07

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


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 51.96  E-value: 1.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFF-----GALVKAVDL------VAQQHQKYVLIGNSyheaekerhAIEVLIRQRCNALIVhsKALSDD 129
Cdd:cd06310   1 KIGVVLKGTTSAFWrtvreGAEAAAKDLgvkiifVGPESEEDVAGQNS---------LLEELINKKPDAIVV--APLDSE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 130 ELAQFMD-----NIPGMVLINRVVPGYAHRCVCLDNLSGARMATRMLLN--NGHQRIGYLSSSHGIEDDAMRKAGWMSAL 202
Cdd:cd06310  70 DLVDPLKdakdkGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEalGGKGKVAVLSLTAGNSTTDQREEGFKEYL 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130089 203 KEQDIIppESWIGAGTPDMPGGEAA--MVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPlhLSIIGFD 273
Cdd:cd06310 150 KKHPGG--IKVLASQYAGSDYAKAAneTEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQ--IKIVGFD 218
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
102-273 9.78e-07

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


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 49.54  E-value: 9.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 102 EKERHAIEVLIRQRCNALIV---HSKALSDDeLAQFMD-NIPgMVLINRVVPGYAHRC-VCLDNLSGARMATRMLLN--N 174
Cdd:cd20004  44 EAQIQIIEYFIDQGVDGIVLaplDRKALVAP-VERARAqGIP-VVIIDSDLGGDAVISfVATDNYAAGRLAAKRMAKllN 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 175 GHQRIGYLSSSHGIEDDAMRKAGWMSALKEQD---IIPPESWIGAgtpDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAG 251
Cdd:cd20004 122 GKGKVALLRLAKGSASTTDRERGFLEALKKLApglKVVDDQYAGG---TVGEARSSAENLLNQYPDVDGIFTPNESTTIG 198
                       170       180
                ....*....|....*....|..
gi 16130089 252 ALTALKDNGIAIPLHLsiIGFD 273
Cdd:cd20004 199 ALRALRRLGLAGKVKF--IGFD 218
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
61-276 1.44e-06

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: 48.83  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVH---SKALSDDELAQFMDN 137
Cdd:cd06323   1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINptdSDAVSPAVEEANEAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 138 IPgMVLINRVVPG---YAHrcVCLDNLSGARMATRMLLN--NGHQRI----GYLSSSHGIEddamRKAGWMSALKEQ--- 205
Cdd:cd06323  81 IP-VITVDRSVTGgkvVSH--IASDNVAGGEMAAEYIAKklGGKGKVvelqGIPGTSAARE----RGKGFHNAIAKYpki 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130089 206 DIIPPEswigAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGiaiPLHLSIIGFDDIP 276
Cdd:cd06323 154 NVVASQ----TADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGTP 217
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
61-310 3.25e-06

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 48.05  E-value: 3.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQ---KYVLIGNSYHEAeKERHAIEVLIRQRCNALI---VHSKALSDDELAQF 134
Cdd:cd06321   1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINpgaKVTVVDARYDLA-KQFSQIDDFIAQGVDLILlnaADSAGIEPAIKRAK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 135 MDNIPgMVLINRVVPGyAHRCVCLDNLSGARMATRMLLN--NGHQRIGYLSsshGIEDDAM--RKAGWMSALKE-QDIIP 209
Cdd:cd06321  80 DAGII-VVAVDVAAEG-ADATVTTDNVQAGYLACEYLVEqlGGKGKVAIID---GPPVSAVidRVNGCKEALAEyPGIKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 210 PESWIGAGTPDmpGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNG-IAIPlhlsIIGFDDIPIA----RYTDPQ 284
Cdd:cd06321 155 VDDQNGKGSRA--GGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGrDDIV----ITSVDGSPEAvaalKREGSP 228
                       250       260
                ....*....|....*....|....*...
gi 16130089 285 L--TTVRYPiASMAKLATELALQGAAGN 310
Cdd:cd06321 229 FiaTAAQDP-YDMARKAVELALKILNGQ 255
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
61-305 1.87e-05

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


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 45.65  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAV-DLVAQQHQKYVLIGNSYhEAEKERHAIEVLIRQRCNALI---VHSKALSDDELAQFMD 136
Cdd:cd19971   1 KFGFSYMTMNNPFFIAINDGIkKAVEANGDELITRDPQL-DQNKQNEQIEDMINQGVDAIFlnpVDSEGIRPALEAAKEA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 137 NIPgMVLINRVV--PGYAHRCVCLDN-----LSGARMAtRMLLNNGhqRIGYLSSSHGiEDDAMRKAGWMSALK------ 203
Cdd:cd19971  80 GIP-VINVDTPVkdTDLVDSTIASDNynagkLCGEDMV-KKLPEGA--KIAVLDHPTA-ESCVDRIDGFLDAIKknpkfe 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 204 ---EQDiippeswiGAGTPD--MPggeaAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGiaIPLHLSIIGFDDIPIA 278
Cdd:cd19971 155 vvaQQD--------GKGQLEvaMP----IMEDILQAHPDLDAVFALNDPSALGALAALKAAG--KLGDILVYGVDGSPDA 220
                       250       260       270
                ....*....|....*....|....*....|.
gi 16130089 279 ----RYTDPQLTTVRYPIaSMAKLATELALQ 305
Cdd:cd19971 221 kaaiKDGKMTATAAQSPI-EIGKKAVETAYK 250
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
223-328 2.04e-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: 380510 [Multi-domain]  Cd Length: 268  Bit Score: 45.49  E-value: 2.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 223 GGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATEL 302
Cdd:cd06287 164 AGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYDGIRARTADPPLTAVDLHLDRVARTAIDL 243
                        90       100
                ....*....|....*....|....*....
gi 16130089 303 ---ALQGAAGNidPRASHcfMPTLVRRHS 328
Cdd:cd06287 244 lfaSLSGEERS--VEVGP--APELVVRAS 268
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
193-309 1.07e-04

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: 43.38  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 193 MRKAGWMSALKEQ----DI-IPPESWIGAGTPDmpggEAA--MVELLGRN-LQLTAVFAYNDNMAAGALTALKDNGIAIP 264
Cdd:cd19991 137 LFREGQMKVLQPLidsgDIkVVGDQWVDDWDPE----EALkiMENALTANnNKIDAVIASNDGTAGGAIQALAEQGLAGK 212
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 16130089 265 LHLSIIGFDDIPIAR-YTDPQLTTVRYPIASMAKLATELALQGAAG 309
Cdd:cd19991 213 VAVSGQDADLAACQRiVEGTQTMTIYKPIKELAEKAAELAVALAKG 258
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
61-273 1.09e-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: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 43.37  E-value: 1.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQ-KYVLIG-NSYHEAEKERHAIEVLIRQRCNALIVhskALSDDEL-----AQ 133
Cdd:cd20008   1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGvEVTFLGpATEADIAGQVNLVENAISRKPDAIVL---APNDTAAlvpavEA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 134 FMDNIPgMVLI-NRVVPGYAHRCVCLDNLSGARMATRMLLN------NGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQD 206
Cdd:cd20008  78 ADAGIP-VVLVdSGANTDDYDAFLATDNVAAGALAADELAEllkasgGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKY 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130089 207 ----IIPPESWIGagtpDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIA--IPLhlsiIGFD 273
Cdd:cd20008 157 pdieIVDVQYSDG----DIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAgkIVL----VGFD 221
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
61-304 1.43e-04

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: 42.76  E-value: 1.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVH---SKALSDDELAQFMDN 137
Cdd:cd19968   1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSpidVKALVPAIEAAIKAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 138 IPgMVLINRVVPG---YAHrcVCLDNLSGARMATRML---LNNGHQRI---GYLSSSHGIEddamRKAGWMSALKEQDII 208
Cdd:cd19968  81 IP-VVTVDRRAEGaapVPH--VGADNVAGGREVAKFVvdkLPNGAKVIeltGTPGSSPAID----RTKGFHEELAAGPKI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 209 ------PPESWIGAGTPDMpggEAAMVELLGrnlQLTAVFAYNDNMAAGALTALKDNGIAIPlHLSIIGFDDIP--IARY 280
Cdd:cd19968 154 kvvfeqTGNFERDEGLTVM---ENILTSLPG---PPDAIICANDDMALGAIEAMRAAGLDLK-KVKVIGFDAVPdaLQAI 226
                       250       260
                ....*....|....*....|....*
gi 16130089 281 TDPQL-TTVRYPIASMAKLATELAL 304
Cdd:cd19968 227 KDGELyATVEQPPGGQARTALRILV 251
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
61-310 1.55e-04

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: 42.96  E-value: 1.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKY-VLIGNSYHEAEKERHAIEVLIRQRCNALIVhskALSDDELAQFM---- 135
Cdd:cd01539   2 KIGVFIYNYDDTFISSVRKALEKAAKAGGKIeLEIYDAQNDQSTQNDQIDTMIAKGVDLLVV---NLVDRTAAQTIidka 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 136 --DNIPgMVLINR-----VVPGYAHRC-VCLDNLSGARMATRMLLN----------NGHQRIGY--LSSSHGIEDDAMRK 195
Cdd:cd01539  79 kaANIP-VIFFNRepsreDLKSYDKAYyVGTDAEESGIMQGEIIADywkanpeidkNGDGKIQYvmLKGEPGHQDAIART 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 196 AGWMSALKEQDIIPPESWIGAGTPDMPGGEAAMVELLGRNLQ-LTAVFAYNDNMAAGALTALKDNG---IAIPLHLSIIG 271
Cdd:cd01539 158 KYSVKTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYGDkIELVIANNDDMALGAIEALKAAGyntGDGDKYIPVFG 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 16130089 272 FDDIPIARYT--DPQLT-TVRYPIASMAKLATELALQGAAGN 310
Cdd:cd01539 238 VDATPEALEAikEGKMLgTVLNDAKAQAKAIYELAKNLANGK 279
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
61-260 1.76e-04

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: 42.78  E-value: 1.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVH---SKALSDDELAQFMDN 137
Cdd:cd06318   1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNpvdPEGLTPAVKAAKAAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 138 IPgMVLINRVVPGYAHRC--VCLDNLSGARMATRMLLN---NGHQRIGYLSSSHGIEDDAMRKAGWMSAL-KEQDIIPPE 211
Cdd:cd06318  81 IP-VITVDSALDPSANVAtqVGRDNKQNGVLVGKEAAKalgGDPGKIIELSGDKGNEVSRDRRDGFLAGVnEYQLRKYGK 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 16130089 212 SWI-----GAGTPDMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNG 260
Cdd:cd06318 160 SNIkvvaqPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAG 213
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
61-310 1.82e-04

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: 42.64  E-value: 1.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALI---VHSKALSDdELAQFMD- 136
Cdd:cd06313   1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIvvpVDADALAP-AVEKAKEa 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 137 NIPGMVLINRVVPGYAHRCVCLDNLSGARMATRMLLN--NGHQRIGYLSSSHGIEDDAMRKAGWMSALKEQDII-----P 209
Cdd:cd06313  80 GIPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADrlGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYPDIkvlaeQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 210 PESWIGAgtpdmpggEA-AMVE--LLGRNLQLTAVFAYNDNMAAGALTALKDNGIA-IPlhlsIIGFDDIPIARYT---D 282
Cdd:cd06313 160 TANWSRD--------EAmSLMEnwLQAYGDEIDGIIAQNDDMALGALQAVKAAGRDdIP----VVGIDGIEDALQAvksG 227
                       250       260
                ....*....|....*....|....*...
gi 16130089 283 PQLTTVRYPIASMAKLATELALQGAAGN 310
Cdd:cd06313 228 ELIATVLQDAEAQGKGAVEVAVDAVKGE 255
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
37-273 1.91e-04

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 42.77  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089   37 MKAVSELdyrpnANAQALATQVS------DTIGVVVMDVSDAFF-----GALVKAVDLvaqqhqKYVLIG-NSYHEAEKE 104
Cdd:PRK10653   3 MKKLATL-----VSAVALSATVSanamakDTIALVVSTLNNPFFvslkdGAQKEADKL------GYNLVVlDSQNNPAKE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  105 RHAIEVLIRQRCNALIVH---SKALSDDELAQFMDNIPGMVLINRVVPGYAHRCVCLDNLSGARMATRML---LNNGHQR 178
Cdd:PRK10653  72 LANVQDLTVRGTKILLINptdSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIakkLGEGAKV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  179 I---GYLSSSHGIEddamRKAGWMSALKEQDIIppeswIGAGTP---DMPGGEAAMVELLGRNLQLTAVFAYNDNMAAGA 252
Cdd:PRK10653 152 IqleGIAGTSAARE----RGEGFKQAVAAHKFN-----VLASQPadfDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGA 222
                        250       260
                 ....*....|....*....|.
gi 16130089  253 LTALKDNGIAIPLhlsIIGFD 273
Cdd:PRK10653 223 LRALQTAGKSDVM---VVGFD 240
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
61-278 2.73e-04

periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily.


Pssm-ID: 380524 [Multi-domain]  Cd Length: 272  Bit Score: 42.22  E-value: 2.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQK-YVLIGNSYHEAEKERHAIEVLIRQRCNALIVhsKALSDDELAQFMD--- 136
Cdd:cd06301   2 KIGVSMQNFSDEFLTYLRDAIEAYAKEYPGvKLVIVDAQSDAAKQLSQVENFIAQGVDAIIV--NPVDTDASAPAVDaaa 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 137 --NIPgMVLINRVVPGYAHRCV---CLDNLSGARMATRML-LNNGHQRIGYLSSSHGIEDDAMRKAGWMSALKE------ 204
Cdd:cd06301  80 daGIP-LVYVNREPDSKPKGVAfvgSDDIESGELQMEYLAkLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKypgmki 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 205 -------------QDIIppESWIGAGTpdmpggeaamvellgrnlQLTAVFAYNDNMAAGALTALKDNGIAIplHLSIIG 271
Cdd:cd06301 159 vaeqtanwsrekaMDIV--ENWLQSGD------------------KIDAIVANNDEMAIGAILALEAAGKKD--DILVAG 216

                ....*..
gi 16130089 272 FDDIPIA 278
Cdd:cd06301 217 IDATPDA 223
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
163-261 3.30e-04

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 41.82  E-value: 3.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 163 GARMAtRMLLNNGHQRI-----------GYLSSSHGIEddamRKAGWMSALKEQDIIPPESWIGAG-TPDmpGGEAAMVE 230
Cdd:cd06324 122 GYLLA-KALIKAARKKSddgkirvlaisGDKSTPASIL----REQGLRDALAEHPDVTLLQIVYANwSED--EAYQKTEK 194
                        90       100       110
                ....*....|....*....|....*....|.
gi 16130089 231 LLGRNLQLTAVFAYNDNMAAGALTALKDNGI 261
Cdd:cd06324 195 LLQRYPDIDIVWAANDAMALGAIDALEEAGL 225
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
238-276 7.42e-04

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: 40.67  E-value: 7.42e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 16130089 238 LTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIP 276
Cdd:cd06309 187 IDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQK 225
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
228-303 9.37e-04

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


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 40.38  E-value: 9.37e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130089 228 MVELLGRNLQLTAVFAYNDNMAAGALTALKDNGiaIPLHLSIIGFD--DIPIARYTDPQLT-TVRYPIASMAKLATELA 303
Cdd:cd19967 173 MESILQANPDIKGVICGNDEMALGAIAALKAAG--RAGDVIIVGFDgsNDVRDAIKEGKISaTVLQPAKLIARLAVEQA 249
VapI COG3093
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense ...
2-32 1.92e-03

Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms];


Pssm-ID: 442327 [Multi-domain]  Cd Length: 87  Bit Score: 36.71  E-value: 1.92e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 16130089   2 ITIRDVARQAGVSVATVSRVLNNSTLVSADT 32
Cdd:COG3093  23 LSQTELAKALGVSRQRISEILNGKRAITADT 53
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
2-39 2.02e-03

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 35.99  E-value: 2.02e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 16130089   2 ITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKA 39
Cdd:cd00093  13 LTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKA 50
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
2-39 2.44e-03

Transcriptional regulator, contains XRE-family HTH domain [Transcription];


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 36.51  E-value: 2.44e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 16130089   2 ITIRDVARQAGVSVATVSRVLNNSTLVSADTREAVMKA 39
Cdd:COG1396  21 LTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKA 58
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
61-276 4.36e-03

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: 38.51  E-value: 4.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVhsKALSDDELAQFMDN--- 137
Cdd:cd06317   1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIIL--DAIDVNGSIPAIKRase 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 138 --IPgMVLINRVVP-GYAHRCVCLDNLSGARMATRMLL------NNGHQRIGYL-SSSHGIEDdaMRKAGWMSALKEQdi 207
Cdd:cd06317  79 agIP-VIAYDAVIPsDFQAAQVGVDNLEGGKEIGKYAAdyikaeLGGQAKIGVVgALSSLIQN--QRQKGFEEALKAN-- 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130089 208 ipPESWIGAGTPDMPGGEAAMVE---LLGRNLQLTAVFAYNDNMAAGALTALKDNGIAipLHLSIIGFDDIP 276
Cdd:cd06317 154 --PGVEIVATVDGQNVQEKALSAaenLLTANPDLDAIYATGEPALLGAVAAVRSQGRQ--GKIKVFGWDLTK 221
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
2-32 4.75e-03

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 34.80  E-value: 4.75e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 16130089      2 ITIRDVARQAGVSVATVSRVLNNSTLVSADT 32
Cdd:smart00530  11 LTQEELAEKLGVSRSTLSRIENGKRKPSLET 41
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
195-310 5.01e-03

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


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 38.33  E-value: 5.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130089 195 KAGWMSALKE----QDI-IPPESWIGAGTPDmpggEA-AMVE--LLGRNLQLTAVFAYNDNMAAGALTALKDNGIAipLH 266
Cdd:cd19992 139 TAGAMDVLQPaidsGDIkIVLDQYVKGWSPD----EAmKLVEnaLTANNNNIDAVLAPNDGMAGGAIQALKAQGLA--GK 212
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 16130089 267 LSIIGFD-DIPIARY--TDPQLTTVRYPIASMAKLATELALQGAAGN 310
Cdd:cd19992 213 VFVTGQDaELAALKRivEGTQTMTVWKDLKELARAAADAAVKLAKGE 259
 
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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