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Conserved domains on  [gi|489995810|ref|WP_003898845|]
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MULTISPECIES: anti-sigma-F factor antagonist RsfA [Mycobacterium]

Protein Classification

anti-sigma factor antagonist( domain architecture ID 10794536)

anti-sigma factor antagonist is a positive regulator of sigma factor activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
 15-122 2.12e-37

anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to SpoIIAA of Bacillus subtilis, an anti-anti-sigma factor. SpoIIAA can bind to and inhibit the anti-sigma F factor SpoIIAB. Also, it can be phosphorylated by SpoIIAB on a Ser residue at position 59 of the seed alignment. A similar arrangement is inferred for RsbV, an anti-anti-sigma factor for sigma B. This Ser is fairly well conserved within a motif resembling MXS[STA]G[VIL]X[VIL][VILF] among homologous known or predicted anti-anti-sigma factors. Regions similar to SpoIIAA and apparently homologous, but differing considerably near the phosphorlated Ser of SpoIIAA, appear in a single copy in several longer proteins. [Regulatory functions, Protein interactions]


:

Pssm-ID: 273042 [Multi-domain]  Cd Length: 108  Bit Score: 122.71  E-value: 2.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995810   15 NALKATIQHHDSAVIIHARGEIDAANEHTWQDLVTKAAAATTaPEPLVVNLNGLDFMGCCAVAVLAHEAERCRRRGVDVR 94
Cdd:TIGR00377   1 MNLNIETEVQEGVVVVRLSGELDAHTAPLLREKVTPAAERTG-IRPIVLDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLV 79

                          90       100
                  ....*....|....*....|....*...
gi 489995810   95 LVSRDRAVARIIHACGYGDVLPVHPTTE 122
Cdd:TIGR00377  80 LVSVSPRVARLLDITGLLRIIPIYPTVE 107
 
Name Accession Description Interval E-value
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
 15-122 2.12e-37

anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to SpoIIAA of Bacillus subtilis, an anti-anti-sigma factor. SpoIIAA can bind to and inhibit the anti-sigma F factor SpoIIAB. Also, it can be phosphorylated by SpoIIAB on a Ser residue at position 59 of the seed alignment. A similar arrangement is inferred for RsbV, an anti-anti-sigma factor for sigma B. This Ser is fairly well conserved within a motif resembling MXS[STA]G[VIL]X[VIL][VILF] among homologous known or predicted anti-anti-sigma factors. Regions similar to SpoIIAA and apparently homologous, but differing considerably near the phosphorlated Ser of SpoIIAA, appear in a single copy in several longer proteins. [Regulatory functions, Protein interactions]


Pssm-ID: 273042 [Multi-domain]  Cd Length: 108  Bit Score: 122.71  E-value: 2.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995810   15 NALKATIQHHDSAVIIHARGEIDAANEHTWQDLVTKAAAATTaPEPLVVNLNGLDFMGCCAVAVLAHEAERCRRRGVDVR 94
Cdd:TIGR00377   1 MNLNIETEVQEGVVVVRLSGELDAHTAPLLREKVTPAAERTG-IRPIVLDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLV 79

                          90       100
                  ....*....|....*....|....*...
gi 489995810   95 LVSRDRAVARIIHACGYGDVLPVHPTTE 122
Cdd:TIGR00377  80 LVSVSPRVARLLDITGLLRIIPIYPTVE 107
STAS pfam01740
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
 18-124 2.02e-24

STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.


Pssm-ID: 426404 [Multi-domain]  Cd Length: 106  Bit Score: 89.60  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995810   18 KATIQHHDSAVIIHARGEIDAANEHTWQDLVTKAAAATTaPEPLVVNLNGLDFMGCCAVAVLAHEAERCRRRGVDVRLVS 97
Cdd:pfam01740   1 YPEAEEIPGILILRLDGPLDFANAESLRERLLRALEEGE-IKHVVLDLSAVPFIDSSGLGALEELYKELRRRGVELVLVG 79

                          90       100
                  ....*....|....*....|....*..
gi 489995810   98 RDRAVARIIHACGYGDVLPVHPTTESA 124
Cdd:pfam01740  80 PSPEVARTLEKTGLDDIIKIFPTVAEA 106
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
 20-119 5.72e-17

Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation; Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.


Pssm-ID: 132914 [Multi-domain]  Cd Length: 99  Bit Score: 70.24  E-value: 5.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995810  20 TIQHHDSAVIIHARGEIDAANEHTWQDLVTKAAAATtaPEPLVVNLNGLDFMGCCAVAVLAHEAERCRRRGVDVRLVSRD 99
Cdd:cd07043    2 TVEERGGVLVVRLSGELDAATAPELREALEELLAEG--PRRLVLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVS 79

                         90       100
                 ....*....|....*....|
gi 489995810 100 RAVARIIHACGYGDVLPVHP 119
Cdd:cd07043   80 PAVRRVLELTGLDRLFPIYP 99
SpoIIAA COG1366
Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction ...
 20-110 6.61e-14

Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction mechanisms];


Pssm-ID: 440977 [Multi-domain]  Cd Length: 93  Bit Score: 62.56  E-value: 6.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995810  20 TIQHHDSAVIIHARGEIDAANEHTWQDLVTKAAAATtaPEPLVVNLNGLDFMGCCAVAVLAHEAERCRRRGVDVRLVSRD 99
Cdd:COG1366    3 PVEVRDGVLVLPLIGELDAARAPELREALLEALETG--ARRVVLDLSGVTFIDSSGLGALLSLAKAARLLGGRLVLVGVS 80

                         90
                 ....*....|.
gi 489995810 100 RAVARIIHACG 110
Cdd:COG1366   81 PAVARVLELTG 91
 
Name Accession Description Interval E-value
ant_ant_sig TIGR00377
anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to ...
 15-122 2.12e-37

anti-anti-sigma factor; This superfamily includes small (105-125 residue) proteins related to SpoIIAA of Bacillus subtilis, an anti-anti-sigma factor. SpoIIAA can bind to and inhibit the anti-sigma F factor SpoIIAB. Also, it can be phosphorylated by SpoIIAB on a Ser residue at position 59 of the seed alignment. A similar arrangement is inferred for RsbV, an anti-anti-sigma factor for sigma B. This Ser is fairly well conserved within a motif resembling MXS[STA]G[VIL]X[VIL][VILF] among homologous known or predicted anti-anti-sigma factors. Regions similar to SpoIIAA and apparently homologous, but differing considerably near the phosphorlated Ser of SpoIIAA, appear in a single copy in several longer proteins. [Regulatory functions, Protein interactions]


Pssm-ID: 273042 [Multi-domain]  Cd Length: 108  Bit Score: 122.71  E-value: 2.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995810   15 NALKATIQHHDSAVIIHARGEIDAANEHTWQDLVTKAAAATTaPEPLVVNLNGLDFMGCCAVAVLAHEAERCRRRGVDVR 94
Cdd:TIGR00377   1 MNLNIETEVQEGVVVVRLSGELDAHTAPLLREKVTPAAERTG-IRPIVLDLEDLEFMDSSGLGVLLGRYKQVRRVGGQLV 79

                          90       100
                  ....*....|....*....|....*...
gi 489995810   95 LVSRDRAVARIIHACGYGDVLPVHPTTE 122
Cdd:TIGR00377  80 LVSVSPRVARLLDITGLLRIIPIYPTVE 107
STAS pfam01740
STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is ...
 18-124 2.02e-24

STAS domain; The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.


Pssm-ID: 426404 [Multi-domain]  Cd Length: 106  Bit Score: 89.60  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995810   18 KATIQHHDSAVIIHARGEIDAANEHTWQDLVTKAAAATTaPEPLVVNLNGLDFMGCCAVAVLAHEAERCRRRGVDVRLVS 97
Cdd:pfam01740   1 YPEAEEIPGILILRLDGPLDFANAESLRERLLRALEEGE-IKHVVLDLSAVPFIDSSGLGALEELYKELRRRGVELVLVG 79

                          90       100
                  ....*....|....*....|....*..
gi 489995810   98 RDRAVARIIHACGYGDVLPVHPTTESA 124
Cdd:pfam01740  80 PSPEVARTLEKTGLDDIIKIFPTVAEA 106
STAS_anti-anti-sigma_factors cd07043
Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key ...
 20-119 5.72e-17

Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation; Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.


Pssm-ID: 132914 [Multi-domain]  Cd Length: 99  Bit Score: 70.24  E-value: 5.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995810  20 TIQHHDSAVIIHARGEIDAANEHTWQDLVTKAAAATtaPEPLVVNLNGLDFMGCCAVAVLAHEAERCRRRGVDVRLVSRD 99
Cdd:cd07043    2 TVEERGGVLVVRLSGELDAATAPELREALEELLAEG--PRRLVLDLSGVTFIDSSGLGVLLGAYKRARAAGGRLVLVNVS 79

                         90       100
                 ....*....|....*....|
gi 489995810 100 RAVARIIHACGYGDVLPVHP 119
Cdd:cd07043   80 PAVRRVLELTGLDRLFPIYP 99
SpoIIAA COG1366
Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction ...
 20-110 6.61e-14

Anti-anti-sigma regulatory factor (antagonist of anti-sigma factor) [Signal transduction mechanisms];


Pssm-ID: 440977 [Multi-domain]  Cd Length: 93  Bit Score: 62.56  E-value: 6.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489995810  20 TIQHHDSAVIIHARGEIDAANEHTWQDLVTKAAAATtaPEPLVVNLNGLDFMGCCAVAVLAHEAERCRRRGVDVRLVSRD 99
Cdd:COG1366    3 PVEVRDGVLVLPLIGELDAARAPELREALLEALETG--ARRVVLDLSGVTFIDSSGLGALLSLAKAARLLGGRLVLVGVS 80

                         90
                 ....*....|.
gi 489995810 100 RAVARIIHACG 110
Cdd:COG1366   81 PAVARVLELTG 91
 
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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