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Conserved domains on  [gi|1747870817|gb|QER88062|]
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anti-sigma regulatory factor [Streptomyces tendae]

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

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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 ...
 18-135 1.72e-34

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: 116.32  E-value: 1.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  18 DLAWVRQHVRQAATLVGFGLVDQTKLVTAASELARNTLVHGGGGVMETsRVTAADGTAGLRLVFSDEGPGIPDLDRALSD 97
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLL-EVVAEGGRVALEILAVDQGPGIADVDEALRD 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1747870817  98 GYTSGDGLGMGLGGSRRLVHDFEVDSTPGSGTTVRVTS 135
Cdd:cd16934    80 GFSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVARK 117
 
Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 18-135 1.72e-34

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: 116.32  E-value: 1.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  18 DLAWVRQHVRQAATLVGFGLVDQTKLVTAASELARNTLVHGGGGVMETsRVTAADGTAGLRLVFSDEGPGIPDLDRALSD 97
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLL-EVVAEGGRVALEILAVDQGPGIADVDEALRD 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1747870817  98 GYTSGDGLGMGLGGSRRLVHDFEVDSTPGSGTTVRVTS 135
Cdd:cd16934    80 GFSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVARK 117
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
10-137 7.80e-18

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 74.18  E-value: 7.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  10 RLPIRSDM-DLAWVRQHVRQAATLVGFGLVDQTKLVTAASELARNTLVHGGGGVMETS-RVTAADGTAGLRLVFSDEGPG 87
Cdd:COG2172     1 SLSLPADLeDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDPDGPvEVELELDPDGLEIEVRDEGPG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1747870817  88 IPDLDraLSDGYTSGDGLGMGLGGSRRLVHDFEVDSTPGsGTTVRVTSWV 137
Cdd:COG2172    81 FDPED--LPDPYSTLAEGGRGLFLIRRLMDEVEYESDPG-GTTVRLVKRL 127
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 39-134 1.57e-06

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 44.18  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817   39 DQTKLVTAASELARNTLVHGGGGVmeTSRVTAADGTAGLRLVFSDEGPGIP--DLDRALSDGYTSGDGLGMGLGG----- 111
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEGG--RITVTLERDGDHVEITVEDNGPGIPpeDLEKIFEPFFRTDKRSRKIGGTglgls 79

                           90       100
                   ....*....|....*....|....*...
gi 1747870817  112 -SRRLVHDF----EVDSTPGSGTTVRVT 134
Cdd:smart00387  80 iVKKLVELHggeiSVESEPGGGTTFTIT 107
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 39-134 9.56e-06

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: 41.97  E-value: 9.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  39 DQTKLVTAASELARNTLVHGGGGvmETSRVTAADGtAGLRLVFSDEGPGIP--DLDRALSDGYTSGDGLGMGL----GGS 112
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKA--GEITVTLSEG-GELTLTVEDNGIGIPpeDLPRIFEPFSTADKRGGGGTglglSIV 78

                          90       100
                  ....*....|....*....|....*.
gi 1747870817 113 RRLVH----DFEVDSTPGSGTTVRVT 134
Cdd:pfam02518  79 RKLVEllggTITVESEPGGGTTVTLT 104
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
 41-134 2.12e-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: 38.75  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  41 TKLVTAASELARNTLVHG----GGGVMETSRVTAADGtagLRLVFSDEGPGIPDLDRALSDGYTSGDGLGMGL---GGSR 113
Cdd:TIGR01925  38 TDIKTAVSEAVTNAIIHGyeenCEGVVYISATIEDHE---VYITVRDEGIGIENLEEAREPLYTSKPELERSGmgfTVME 114

                          90       100
                  ....*....|....*....|.
gi 1747870817 114 RLVHDFEVDSTPGSGTTVRVT 134
Cdd:TIGR01925 115 NFMDDVSVDSEKEKGTKIIMK 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 ...
 18-135 1.72e-34

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: 116.32  E-value: 1.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  18 DLAWVRQHVRQAATLVGFGLVDQTKLVTAASELARNTLVHGGGGVMETsRVTAADGTAGLRLVFSDEGPGIPDLDRALSD 97
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLL-EVVAEGGRVALEILAVDQGPGIADVDEALRD 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1747870817  98 GYTSGDGLGMGLGGSRRLVHDFEVDSTPGSGTTVRVTS 135
Cdd:cd16934    80 GFSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVARK 117
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
10-137 7.80e-18

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 74.18  E-value: 7.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  10 RLPIRSDM-DLAWVRQHVRQAATLVGFGLVDQTKLVTAASELARNTLVHGGGGVMETS-RVTAADGTAGLRLVFSDEGPG 87
Cdd:COG2172     1 SLSLPADLeDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDPDGPvEVELELDPDGLEIEVRDEGPG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1747870817  88 IPDLDraLSDGYTSGDGLGMGLGGSRRLVHDFEVDSTPGsGTTVRVTSWV 137
Cdd:COG2172    81 FDPED--LPDPYSTLAEGGRGLFLIRRLMDEVEYESDPG-GTTVRLVKRL 127
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 39-134 1.57e-06

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 44.18  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817   39 DQTKLVTAASELARNTLVHGGGGVmeTSRVTAADGTAGLRLVFSDEGPGIP--DLDRALSDGYTSGDGLGMGLGG----- 111
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEGG--RITVTLERDGDHVEITVEDNGPGIPpeDLEKIFEPFFRTDKRSRKIGGTglgls 79

                           90       100
                   ....*....|....*....|....*...
gi 1747870817  112 -SRRLVHDF----EVDSTPGSGTTVRVT 134
Cdd:smart00387  80 iVKKLVELHggeiSVESEPGGGTTFTIT 107
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 39-134 9.56e-06

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: 41.97  E-value: 9.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  39 DQTKLVTAASELARNTLVHGGGGvmETSRVTAADGtAGLRLVFSDEGPGIP--DLDRALSDGYTSGDGLGMGL----GGS 112
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKA--GEITVTLSEG-GELTLTVEDNGIGIPpeDLPRIFEPFSTADKRGGGGTglglSIV 78

                          90       100
                  ....*....|....*....|....*.
gi 1747870817 113 RRLVH----DFEVDSTPGSGTTVRVT 134
Cdd:pfam02518  79 RKLVEllggTITVESEPGGGTTVTLT 104
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
37-134 3.22e-05

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 42.20  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  37 LVDQTKLVTAASELARNTLVHGGGGvmETSRVTAADGTAGLRLVFSDEGPGIP--DLDRALSDGYTSGDGLGMGLG---- 110
Cdd:COG0642   218 RGDPDRLRQVLLNLLSNAIKYTPEG--GTVTVSVRREGDRVRISVEDTGPGIPpeDLERIFEPFFRTDPSRRGGGTglgl 295

                          90       100
                  ....*....|....*....|....*....
gi 1747870817 111 -GSRRLVH----DFEVDSTPGSGTTVRVT 134
Cdd:COG0642   296 aIVKRIVElhggTIEVESEPGKGTTFTVT 324
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
38-134 1.40e-04

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 40.28  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  38 VDQTKLVTAASELARNTLVHGGGGVmeTSRVTAADGTAGLRLVFSDEGPGIP--DLDRALSDGYTSGDGLGMGLGG---- 111
Cdd:COG2205   128 ADPELLEQVLANLLDNAIKYSPPGG--TITISARREGDGVRISVSDNGPGIPeeELERIFERFYRGDNSRGEGGTGlgla 205

                          90       100
                  ....*....|....*....|....*...
gi 1747870817 112 -SRRLVH----DFEVDSTPGSGTTVRVT 134
Cdd:COG2205   206 iVKRIVEahggTIWVESEPGGGTTFTVT 233
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
 41-134 2.12e-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: 38.75  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  41 TKLVTAASELARNTLVHG----GGGVMETSRVTAADGtagLRLVFSDEGPGIPDLDRALSDGYTSGDGLGMGL---GGSR 113
Cdd:TIGR01925  38 TDIKTAVSEAVTNAIIHGyeenCEGVVYISATIEDHE---VYITVRDEGIGIENLEEAREPLYTSKPELERSGmgfTVME 114

                          90       100
                  ....*....|....*....|.
gi 1747870817 114 RLVHDFEVDSTPGSGTTVRVT 134
Cdd:TIGR01925 115 NFMDDVSVDSEKEKGTKIIMK 135
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 76-134 1.29e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 36.11  E-value: 1.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1747870817  76 GLRLVFSDEGPGIP--DLDRALSDGYTSGDGLGMGLGG----------SRRLVHDFEVDSTPGSGTTVRVT 134
Cdd:cd16948    37 GVVLSIKDFGIGIPeeDLPRVFDKGFTGENGRNFQESTgmglylvkklCDKLGHKIDVESEVGEGTTFTIT 107
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 43-134 4.05e-03

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 34.55  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747870817  43 LVTAASELARNTLVHGGGGVMETS-RVTAADGTAGLRLVFSDEGPGIPDLDRALSDgytsgdglgMGLGGS-------RR 114
Cdd:cd16936     1 VELAVSEAVTNAVRHAYRHDGPGPvRLELDLDPDRLRVEVTDSGPGFDPLRPADPD---------AGLREGgrglaliRA 71

                          90       100
                  ....*....|....*....|
gi 1747870817 115 LVHDFEVDSTPGsGTTVRVT 134
Cdd:cd16936    72 LMDEVGYRRTPG-GKTVWLE 90
 
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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