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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 570294815   5 WQGYRQAMARAGLPIIAGYEVVSDFEFGGGLVALKQRLNNPE 46
Cdd:cd06292  139 LAGYRAALEEAGLPFDPGLVVEGENTEEGGYAAAARLLDLGP 180

DNA-binding transcriptional regulator CytR; Provisional

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 570294815   6 QGYRQAMARAGLPIIAGYEVVSDFEFGGGLVALKQRLNNPE 46
Cdd:PRK11041 172 QGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQ 212

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 570294815   5 WQGYRQAMARAGLPIIAGYEVVSDFEFGGGLVALKQRLNNPE 46
Cdd:cd06284  134 LEGYRRALAEAGLPVDEDLIIEGDFSFEAGYAAARALLALPE 175

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 570294815   6 QGYRQAMARAGLPIIAGYEVVSDFEFGGGLVALKQRLNNPE 46
Cdd:cd06267  136 EGYRDALAEAGLPVDPELVVEGDFSEESGYEAARELLALPP 176

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 570294815   5 WQGYRQAMARAGLPIIAGYEVVSDFEFGGGL---VALKQRLNNPEA 47
Cdd:cd19974  137 YLGYRKALLEAGLPPEKEEWLLEDRDDGYGLteeIELPLKLMLPTA 182

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.

                         10        20
                 ....*....|....*....|....*.
gi 570294815  38 LKQRLNNPEAEPQVLPLTPELIERGS 63
Cdd:cd06275  244 LLDRIENKREEPQSIVLEPELIERES 269

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 570294815   7 GYRQAMARAGLPIIAGYEVVSDFEFGGGLVALKQRLNNPE 46
Cdd:cd06285  137 GYRRALAEAGLPVPDERIVPGGFTIEAGREAAYRLLSRPE 176

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 570294815  14 RAGLPIIAGYEVVSDFEFGGG-----LVALKQRLNNPEAEPQVLPLTP 56
Cdd:cd17939   26 RAIVPIIKGRDVIAQAQSGTGktatfSIGALQRIDTTVRETQALVLAP 73

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 570294815   6 QGYRQAMARAGLPIIAGYEVVSDFEFGGGLVALKQRLNNPE 46
Cdd:cd19975  137 EGYKKALKDAGLPIKENLIVEGDFSFKSGYQAMKRLLKNKK 177

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.

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 570294815   6 QGYRQAMARAGLPIIAGYEVVSDFEFGGGLVALKQRL 42
Cdd:cd06290  135 AGYRRALEDAGLEVDPRLIVEGDFTEESGYEAMKKLL 171