flagellar biosynthesis anti-sigma factor FlgM [Anaeromusa acidaminophila]
flagellar biosynthesis anti-sigma factor FlgM( domain architecture ID 10515847)
flagellar biosynthesis anti-sigma factor FlgM binds and inhibits the activity of the transcription factor sigma 28
List of domain hits
Name | Accession | Description | Interval | E-value | ||
FlgM | pfam04316 | Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor ... |
37-90 | 6.07e-15 | ||
Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor sigma 28. Inhibition of sigma 28 prevents the expression of genes from flagellar transcriptional class 3, which include genes for the filament and chemotaxis. Correctly assembled basal body-hook structures export FlgM, relieving inhibition of sigma 28 and allowing expression of class 3 genes. NMR studies show that free FlgM is mostly unfolded, which may facilitate its export. The C terminal half of FlgM adopts a tertiary structure when it binds to sigma 28. All mutations in FlgM that prevent sigma 28 inhibition affect the C-terminal domain and is the region thought to constitute the binding domain. A minimal binding domain has been identified between Glu 64 and Arg 88 in Salmonella typhimurium. The N-terminal portion remains unstructured and may be necessary for recognition by the export machinery. : Pssm-ID: 461260 Cd Length: 54 Bit Score: 62.89 E-value: 6.07e-15
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Name | Accession | Description | Interval | E-value | |||
FlgM | pfam04316 | Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor ... |
37-90 | 6.07e-15 | |||
Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor sigma 28. Inhibition of sigma 28 prevents the expression of genes from flagellar transcriptional class 3, which include genes for the filament and chemotaxis. Correctly assembled basal body-hook structures export FlgM, relieving inhibition of sigma 28 and allowing expression of class 3 genes. NMR studies show that free FlgM is mostly unfolded, which may facilitate its export. The C terminal half of FlgM adopts a tertiary structure when it binds to sigma 28. All mutations in FlgM that prevent sigma 28 inhibition affect the C-terminal domain and is the region thought to constitute the binding domain. A minimal binding domain has been identified between Glu 64 and Arg 88 in Salmonella typhimurium. The N-terminal portion remains unstructured and may be necessary for recognition by the export machinery. Pssm-ID: 461260 Cd Length: 54 Bit Score: 62.89 E-value: 6.07e-15
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FlgM_jcvi | TIGR03824 | flagellar biosynthesis anti-sigma factor FlgM; FlgM interacts with and inhibits the ... |
26-91 | 1.86e-13 | |||
flagellar biosynthesis anti-sigma factor FlgM; FlgM interacts with and inhibits the alternative sigma factor sigma(28) FliA. The C-terminus of FlgM contains the sigma(28)-binding domain. Pssm-ID: 274802 Cd Length: 95 Bit Score: 60.05 E-value: 1.86e-13
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FlgM | COG2747 | Negative regulator of flagellin synthesis (anti-sigma28 factor) [Transcription, Cell motility]; ... |
1-91 | 1.14e-12 | |||
Negative regulator of flagellin synthesis (anti-sigma28 factor) [Transcription, Cell motility]; Pssm-ID: 442044 Cd Length: 101 Bit Score: 58.15 E-value: 1.14e-12
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START_STARD4-like | cd08902 | Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ... |
32-81 | 1.19e-03 | |||
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4 and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7alpha-hydroxycholesterol. STARD4 is ubiquitously expressed, with highest levels in liver and kidney. Pssm-ID: 176911 Cd Length: 202 Bit Score: 36.09 E-value: 1.19e-03
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Name | Accession | Description | Interval | E-value | |||
FlgM | pfam04316 | Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor ... |
37-90 | 6.07e-15 | |||
Anti-sigma-28 factor, FlgM; FlgM binds and inhibits the activity of the transcription factor sigma 28. Inhibition of sigma 28 prevents the expression of genes from flagellar transcriptional class 3, which include genes for the filament and chemotaxis. Correctly assembled basal body-hook structures export FlgM, relieving inhibition of sigma 28 and allowing expression of class 3 genes. NMR studies show that free FlgM is mostly unfolded, which may facilitate its export. The C terminal half of FlgM adopts a tertiary structure when it binds to sigma 28. All mutations in FlgM that prevent sigma 28 inhibition affect the C-terminal domain and is the region thought to constitute the binding domain. A minimal binding domain has been identified between Glu 64 and Arg 88 in Salmonella typhimurium. The N-terminal portion remains unstructured and may be necessary for recognition by the export machinery. Pssm-ID: 461260 Cd Length: 54 Bit Score: 62.89 E-value: 6.07e-15
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FlgM_jcvi | TIGR03824 | flagellar biosynthesis anti-sigma factor FlgM; FlgM interacts with and inhibits the ... |
26-91 | 1.86e-13 | |||
flagellar biosynthesis anti-sigma factor FlgM; FlgM interacts with and inhibits the alternative sigma factor sigma(28) FliA. The C-terminus of FlgM contains the sigma(28)-binding domain. Pssm-ID: 274802 Cd Length: 95 Bit Score: 60.05 E-value: 1.86e-13
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FlgM | COG2747 | Negative regulator of flagellin synthesis (anti-sigma28 factor) [Transcription, Cell motility]; ... |
1-91 | 1.14e-12 | |||
Negative regulator of flagellin synthesis (anti-sigma28 factor) [Transcription, Cell motility]; Pssm-ID: 442044 Cd Length: 101 Bit Score: 58.15 E-value: 1.14e-12
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START_STARD4-like | cd08902 | Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ... |
32-81 | 1.19e-03 | |||
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4 and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7alpha-hydroxycholesterol. STARD4 is ubiquitously expressed, with highest levels in liver and kidney. Pssm-ID: 176911 Cd Length: 202 Bit Score: 36.09 E-value: 1.19e-03
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Blast search parameters | ||||
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