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Conserved domains on  [gi|517532035|ref|WP_018702243|]
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flagellar biosynthesis anti-sigma factor FlgM [Anaeromusa acidaminophila]

Protein Classification

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

Graphical summary

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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
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517532035  37 DSVVLSPKAQEFAGLLAKLQQTPEVRTDVVQRISAQVENGEYRVDSAAVAKNLL 90
Cdd:pfam04316  1 DSVELSSEAKDLQKAKQALAAAPDVREDKVAELKAAIANGTYKVDAEKIADKLL 54
 
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
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517532035  37 DSVVLSPKAQEFAGLLAKLQQTPEVRTDVVQRISAQVENGEYRVDSAAVAKNLL 90
Cdd:pfam04316  1 DSVELSSEAKDLQKAKQALAAAPDVREDKVAELKAAIANGTYKVDAEKIADKLL 54
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
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517532035  26 KTTATSAAKASDSVVLSPKAQEFAGLLAKLQQTPEVRTDVVQRISAQVENGEYRVDSAAVAKNLLA 91
Cdd:TIGR03824 28 AAAAAAAAASGDSVSLSSLAQQLQSLEAALASSPDVDAEKVAEIKAAIANGSYKVDAEKIADKLLD 93
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517532035   1 MNVSGSQFHGILKLYGEQTKVNRML----KTTATSAAKASDSVVLSPKAQEFAGLlAKLQQTPEVRTDVVQRISAQVENG 76
Cdd:COG2747    1 MKINGTGPLSVTAVNPYQKAAATAAsagkAAAAASAAAASDSVELSSAAKQLQQL-EELASSPDIDAERVAEIKQAIANG 79
                         90
                 ....*....|....*
gi 517532035  77 EYRVDSAAVAKNLLA 91
Cdd:COG2747   80 TYKVDAEKIADKLLA 94
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
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 517532035  32 AAKASDSVVLSPKAQEFAGLLAKLQQTPEvrtDVVQRISAQVENGEYRVD 81
Cdd:cd08902   28 AKKSKDVTVWRKPSEEFGGYLYKAQGVVE---DVYNRIVDHIRPGPYRLD 74
 
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
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517532035  37 DSVVLSPKAQEFAGLLAKLQQTPEVRTDVVQRISAQVENGEYRVDSAAVAKNLL 90
Cdd:pfam04316  1 DSVELSSEAKDLQKAKQALAAAPDVREDKVAELKAAIANGTYKVDAEKIADKLL 54
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
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517532035  26 KTTATSAAKASDSVVLSPKAQEFAGLLAKLQQTPEVRTDVVQRISAQVENGEYRVDSAAVAKNLLA 91
Cdd:TIGR03824 28 AAAAAAAAASGDSVSLSSLAQQLQSLEAALASSPDVDAEKVAEIKAAIANGSYKVDAEKIADKLLD 93
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
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517532035   1 MNVSGSQFHGILKLYGEQTKVNRML----KTTATSAAKASDSVVLSPKAQEFAGLlAKLQQTPEVRTDVVQRISAQVENG 76
Cdd:COG2747    1 MKINGTGPLSVTAVNPYQKAAATAAsagkAAAAASAAAASDSVELSSAAKQLQQL-EELASSPDIDAERVAEIKQAIANG 79
                         90
                 ....*....|....*
gi 517532035  77 EYRVDSAAVAKNLLA 91
Cdd:COG2747   80 TYKVDAEKIADKLLA 94
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
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 517532035  32 AAKASDSVVLSPKAQEFAGLLAKLQQTPEvrtDVVQRISAQVENGEYRVD 81
Cdd:cd08902   28 AKKSKDVTVWRKPSEEFGGYLYKAQGVVE---DVYNRIVDHIRPGPYRLD 74
 
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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