NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|827433385|gb|AKJ08513|]
View 

anti-sigma regulatory factor [Streptomyces incarnatus]

Protein Classification

anti-sigma regulatory factor( domain architecture ID 13014755)

anti-sigma regulatory factor similar to RsbT, an ATPase with serine/threonine kinase activity that phosphorylates its antagonist RsbS and stimulates the phosphatase RsbU in a signaling cascade that results in active sigma-B

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 18-133 5.62e-30

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


:

Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 104.76  E-value: 5.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827433385  18 DLAWVRQHVRRAAADLGFSLVQQTKLVTAVSELARNTLVHGGGGSMAMTILEEGGRRGLRLSFVDAGPGIRDIDQAMTDG 97
Cdd:cd16934    1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 827433385  98 YTTGGGLGLGLSGAKRLVQEFSIDSSPGKGTTVTIT 133
Cdd:cd16934   81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVAR 116
 
Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 18-133 5.62e-30

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 104.76  E-value: 5.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827433385  18 DLAWVRQHVRRAAADLGFSLVQQTKLVTAVSELARNTLVHGGGGSMAMTILEEGGRRGLRLSFVDAGPGIRDIDQAMTDG 97
Cdd:cd16934    1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 827433385  98 YTTGGGLGLGLSGAKRLVQEFSIDSSPGKGTTVTIT 133
Cdd:cd16934   81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVAR 116
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
10-133 1.68e-14

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 65.32  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827433385  10 RLPIGSD-ADLAWVRQHVRRAAADLGFSLVQQTKLVTAVSELARNTLVHGGGGSMAMTI-LE-EGGRRGLRLSFVDAGPG 86
Cdd:COG2172    1 SLSLPADlEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDPDGPVeVElELDPDGLEIEVRDEGPG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 827433385  87 IRDIDqamtdgYTTGGGLGLGL----SGAKRLVQEFSIDSSPGkGTTVTIT 133
Cdd:COG2172   81 FDPED------LPDPYSTLAEGgrglFLIRRLMDEVEYESDPG-GTTVRLV 124
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 40-133 4.92e-05

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 40.04  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827433385   40 QTKLVTAVSELARNTLVHGGGGSMAMTILEEGGRrgLRLSFVDAGPGIRDIDQAMTDGYTTGGGLGLGLSG------AKR 113
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAAKAGEITVTLSEGGE--LTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGGGTglglsiVRK 80

                          90       100
                  ....*....|....*....|....
gi 827433385  114 LVQ----EFSIDSSPGKGTTVTIT 133
Cdd:pfam02518  81 LVEllggTITVESEPGGGTTVTLT 104
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
 20-133 1.62e-04

anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA. [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 130980 [Multi-domain]  Cd Length: 137  Bit Score: 39.14  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827433385   20 AWVRQHVRRAAADLGFSLVQQTKLVTAVSELARNTLVHG-----GGGSMAMTILEEggrRGLRLSFVDAGPGIRDIDQAM 94
Cdd:TIGR01925  17 SFARVTVASFIAQLDPTMEELTDIKTAVSEAVTNAIIHGyeencEGVVYISATIED---HEVYITVRDEGIGIENLEEAR 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 827433385   95 T---DGYTTGGGLGLGLSGAKRLVQEFSIDSSPGKGTTVTIT 133
Cdd:TIGR01925  94 EplyTSKPELERSGMGFTVMENFMDDVSVDSEKEKGTKIIMK 135
 
Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 18-133 5.62e-30

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 104.76  E-value: 5.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827433385  18 DLAWVRQHVRRAAADLGFSLVQQTKLVTAVSELARNTLVHGGGGSMAMTILEEGGRRGLRLSFVDAGPGIRDIDQAMTDG 97
Cdd:cd16934    1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 827433385  98 YTTGGGLGLGLSGAKRLVQEFSIDSSPGKGTTVTIT 133
Cdd:cd16934   81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVAR 116
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
10-133 1.68e-14

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 65.32  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827433385  10 RLPIGSD-ADLAWVRQHVRRAAADLGFSLVQQTKLVTAVSELARNTLVHGGGGSMAMTI-LE-EGGRRGLRLSFVDAGPG 86
Cdd:COG2172    1 SLSLPADlEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDPDGPVeVElELDPDGLEIEVRDEGPG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 827433385  87 IRDIDqamtdgYTTGGGLGLGL----SGAKRLVQEFSIDSSPGkGTTVTIT 133
Cdd:COG2172   81 FDPED------LPDPYSTLAEGgrglFLIRRLMDEVEYESDPG-GTTVRLV 124
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 40-133 4.92e-05

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 40.04  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827433385   40 QTKLVTAVSELARNTLVHGGGGSMAMTILEEGGRrgLRLSFVDAGPGIRDIDQAMTDGYTTGGGLGLGLSG------AKR 113
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAAKAGEITVTLSEGGE--LTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGGGTglglsiVRK 80

                          90       100
                  ....*....|....*....|....
gi 827433385  114 LVQ----EFSIDSSPGKGTTVTIT 133
Cdd:pfam02518  81 LVEllggTITVESEPGGGTTVTLT 104
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
 20-133 1.62e-04

anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA. [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 130980 [Multi-domain]  Cd Length: 137  Bit Score: 39.14  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827433385   20 AWVRQHVRRAAADLGFSLVQQTKLVTAVSELARNTLVHG-----GGGSMAMTILEEggrRGLRLSFVDAGPGIRDIDQAM 94
Cdd:TIGR01925  17 SFARVTVASFIAQLDPTMEELTDIKTAVSEAVTNAIIHGyeencEGVVYISATIED---HEVYITVRDEGIGIENLEEAR 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 827433385   95 T---DGYTTGGGLGLGLSGAKRLVQEFSIDSSPGKGTTVTIT 133
Cdd:TIGR01925  94 EplyTSKPELERSGMGFTVMENFMDDVSVDSEKEKGTKIIMK 135
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
 20-133 1.31e-03

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 36.75  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827433385  20 AWVRQHVRRAAADLGFSLVQQTKLVTAVSELARNTLVHGGG--GSMAMTILEEGGRRGLRLSFVDAGPGIRDIDQAMT-- 95
Cdd:cd16942   16 SFARVTVAAFVAQLDPTIDELTEIKTVVSEAVTNAIIHGYNndPNGIVSISVIIEDGVVHLTVRDEGVGIPDIEEARQpl 95

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 827433385  96 -DGYTTGGGLGLGLSGAKRLVQEFSIDSSPGKGTTVTIT 133
Cdd:cd16942   96 fTTKPELERSGMGFTIMENFMDEVIVESEVNKGTTVYLK 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH