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Conserved domains on  [gi|545589550|ref|WP_021718252|]
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MULTISPECIES: anti-sigma regulatory factor [Phascolarctobacterium]

Protein Classification

ATP-binding protein( domain architecture ID 10005496)

ATP-binding protein with a histidine kinase-like ATPase domain, similar to serine/threonine-protein kinase BtrW, which phosphorylates and inactivates its specific antagonist protein BtrV and may function as a negative regulator of sigma-B activity

Gene Ontology:  GO:0005524|GO:0016787
PubMed:  16077112|12354223

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
17-141 1.07e-22

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


:

Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 86.51  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550  17 DFDRAGEASAGLKRLLQKIGVPADIIRRIAIGTYEAEMNVIIHAGGGQ------VDAEIFPEETVVYIADQGPGIPDIKL 90
Cdd:COG2172    7 DLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDpdgpveVELELDPDGLEIEVRDEGPGFDPEDL 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 545589550  91 AmqEGWSTAPDHvrqmgfgaGMGLPNMMKCSDDFDIQSTVGsGTNIKMKFK 141
Cdd:COG2172   87 P--DPYSTLAEG--------GRGLFLIRRLMDEVEYESDPG-GTTVRLVKR 126
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
17-141 1.07e-22

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 86.51  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550  17 DFDRAGEASAGLKRLLQKIGVPADIIRRIAIGTYEAEMNVIIHAGGGQ------VDAEIFPEETVVYIADQGPGIPDIKL 90
Cdd:COG2172    7 DLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDpdgpveVELELDPDGLEIEVRDEGPGFDPEDL 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 545589550  91 AmqEGWSTAPDHvrqmgfgaGMGLPNMMKCSDDFDIQSTVGsGTNIKMKFK 141
Cdd:COG2172   87 P--DPYSTLAEG--------GRGLFLIRRLMDEVEYESDPG-GTTVRLVKR 126
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 20-140 1.78e-15

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: 67.78  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550  20 RAGEASAGLKRLLQKIGVPADIIRRIAIGTYEAEMNVIIHAGGGQVDAEIFPEETVVYI----ADQGPGIPDIKLAMQEG 95
Cdd:cd16934    1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALeilaVDQGPGIADVDEALRDG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 545589550  96 WSTapdhvrqmGFGAGMGLPNMMKCSDDFDIQSTVGSGTNIKMKF 140
Cdd:cd16934   81 FST--------GGGLGLGLGGVRRLADEFDLHSAPGRGTVVVARK 117
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
17-140 1.22e-08

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 49.98  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550   17 DFDRAGEASAGLKRLLQKIGVPADIIRRIAIGTYEAEMNVIIHAGGG------QVDAEIFPEETVVYIADQGPGIPDIKL 90
Cdd:pfam13581   4 DPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHAYREgpegpvEVRLTSDGGGLVVTVADSGPPFDPLTL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 545589550   91 AMQEGwsTAPDHVRQMGfgaGMGLPNMMKCSDDFDIQSTvGSGTNIKMKF 140
Cdd:pfam13581  84 PPPDL--EEPDEDRKEG---GRGLALIRGLMDDVEYTRG-GEGNTVRMRK 127
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 55-141 1.34e-05

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 41.87  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550    55 NVIIHAGGG---QVDAEIFPEETVVYIADQGPGIP--DIKLAMQEGWSTAPDhVRQMGfGAGMGLPNMMKCSDDF----D 125
Cdd:smart00387  16 NAIKYTPEGgriTVTLERDGDHVEITVEDNGPGIPpeDLEKIFEPFFRTDKR-SRKIG-GTGLGLSIVKKLVELHggeiS 93

                           90
                   ....*....|....*.
gi 545589550   126 IQSTVGSGTNIKMKFK 141
Cdd:smart00387  94 VESEPGGGTTFTITLP 109
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
17-141 1.07e-22

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 86.51  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550  17 DFDRAGEASAGLKRLLQKIGVPADIIRRIAIGTYEAEMNVIIHAGGGQ------VDAEIFPEETVVYIADQGPGIPDIKL 90
Cdd:COG2172    7 DLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDpdgpveVELELDPDGLEIEVRDEGPGFDPEDL 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 545589550  91 AmqEGWSTAPDHvrqmgfgaGMGLPNMMKCSDDFDIQSTVGsGTNIKMKFK 141
Cdd:COG2172   87 P--DPYSTLAEG--------GRGLFLIRRLMDEVEYESDPG-GTTVRLVKR 126
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 20-140 1.78e-15

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: 67.78  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550  20 RAGEASAGLKRLLQKIGVPADIIRRIAIGTYEAEMNVIIHAGGGQVDAEIFPEETVVYI----ADQGPGIPDIKLAMQEG 95
Cdd:cd16934    1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALeilaVDQGPGIADVDEALRDG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 545589550  96 WSTapdhvrqmGFGAGMGLPNMMKCSDDFDIQSTVGSGTNIKMKF 140
Cdd:cd16934   81 FST--------GGGLGLGLGGVRRLADEFDLHSAPGRGTVVVARK 117
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
 51-139 4.95e-10

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: 54.08  E-value: 4.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550  51 EAEMNVIIHA----GGGQVDAEIFPEETVVYIA--DQGPGIPDIKLAMQEGWSTAPDHVRqmgfgAGMGLPNMMKCSDDF 124
Cdd:cd16942   45 EAVTNAIIHGynndPNGIVSISVIIEDGVVHLTvrDEGVGIPDIEEARQPLFTTKPELER-----SGMGFTIMENFMDEV 119

                         90
                 ....*....|....*
gi 545589550 125 DIQSTVGSGTNIKMK 139
Cdd:cd16942  120 IVESEVNKGTTVYLK 134
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
17-140 1.22e-08

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 49.98  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550   17 DFDRAGEASAGLKRLLQKIGVPADIIRRIAIGTYEAEMNVIIHAGGG------QVDAEIFPEETVVYIADQGPGIPDIKL 90
Cdd:pfam13581   4 DPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHAYREgpegpvEVRLTSDGGGLVVTVADSGPPFDPLTL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 545589550   91 AMQEGwsTAPDHVRQMGfgaGMGLPNMMKCSDDFDIQSTvGSGTNIKMKF 140
Cdd:pfam13581  84 PPPDL--EEPDEDRKEG---GRGLALIRGLMDDVEYTRG-GEGNTVRMRK 127
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 55-141 1.34e-05

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 41.87  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550    55 NVIIHAGGG---QVDAEIFPEETVVYIADQGPGIP--DIKLAMQEGWSTAPDhVRQMGfGAGMGLPNMMKCSDDF----D 125
Cdd:smart00387  16 NAIKYTPEGgriTVTLERDGDHVEITVEDNGPGIPpeDLEKIFEPFFRTDKR-SRKIG-GTGLGLSIVKKLVELHggeiS 93

                           90
                   ....*....|....*.
gi 545589550   126 IQSTVGSGTNIKMKFK 141
Cdd:smart00387  94 VESEPGGGTTFTITLP 109
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 44-140 5.85e-05

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: 39.56  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550  44 RIAIGtyEAEMNVIIHAGGG------QVDAEIFPEETVVYIADQGPGIPDIKLAmqegwstAPDHVRQMGfgaGMGLPNM 117
Cdd:cd16936    2 ELAVS--EAVTNAVRHAYRHdgpgpvRLELDLDPDRLRVEVTDSGPGFDPLRPA-------DPDAGLREG---GRGLALI 69

                         90       100
                 ....*....|....*....|...
gi 545589550 118 MKCSDDFDIQSTVGsGTNIKMKF 140
Cdd:cd16936   70 RALMDEVGYRRTPG-GKTVWLEL 91
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 55-141 8.06e-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: 39.66  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550   55 NVIIHAG-GGQVDAEIFPEETV-VYIADQGPGIPDIKLA-MQEGWSTAPDHvrqMGFGAGMGLPNMMKCSD----DFDIQ 127
Cdd:pfam02518  16 NALKHAAkAGEITVTLSEGGELtLTVEDNGIGIPPEDLPrIFEPFSTADKR---GGGGTGLGLSIVRKLVEllggTITVE 92

                          90
                  ....*....|....
gi 545589550  128 STVGSGTNIKMKFK 141
Cdd:pfam02518  93 SEPGGGTTVTLTLP 106
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 72-141 2.42e-03

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 36.16  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545589550  72 EETVVYIADQGPGIP--DIKLAMQEGWSTAPDHVRQMGF------------GAGMGLPnMMKC-----SDDFDIQSTVGS 132
Cdd:cd16929   82 EDLTIKISDRGGGIPreDLARLFSYMYSTAPQPSLDDFSdlisgtqpsplaGFGYGLP-MSRLyaeyfGGDLDLQSMEGY 160


                 ....*....
gi 545589550 133 GTNIKMKFK 141
Cdd:cd16929  161 GTDVYIYLK 169
 
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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