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Conserved domains on  [gi|586184698|gb|EWP90549|]
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serine-protein kinase rsbW [Staphylococcus aureus M1204]

Protein Classification

ATP-binding protein( domain architecture ID 10012135)

ATPase similar to histidine kinase domains

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
 1-159 8.98e-94

serine-protein kinase RsbW; Provisional


:

Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 268.33  E-value: 8.98e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   1 MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIK 80
Cdd:PRK04069   1 MMEKFDKIEMKIPAKAEYVSIIRLTLSGVANRMGFSYDDIEDMKIAVSEACTNAVQHAYKEDEV-GEIHIRFEIYEDRLE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586184698  81 IVISDKGDSFDYETTKSKIGPYDKDENIDFLREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS 159
Cdd:PRK04069  80 IVVADNGVSFDYETLKSKLGPYDISKPIEDLREGGLGLFLIETLMDDVTVYKDSGVTVSMTKYINREQVENNGERISTS 158
 
Name Accession Description Interval E-value
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
 1-159 8.98e-94

serine-protein kinase RsbW; Provisional


Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 268.33  E-value: 8.98e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   1 MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIK 80
Cdd:PRK04069   1 MMEKFDKIEMKIPAKAEYVSIIRLTLSGVANRMGFSYDDIEDMKIAVSEACTNAVQHAYKEDEV-GEIHIRFEIYEDRLE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586184698  81 IVISDKGDSFDYETTKSKIGPYDKDENIDFLREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS 159
Cdd:PRK04069  80 IVVADNGVSFDYETLKSKLGPYDISKPIEDLREGGLGLFLIETLMDDVTVYKDSGVTVSMTKYINREQVENNGERISTS 158
rsbW_low_gc TIGR01924
serine-protein kinase RsbW; This model describes the anti-sigma B factor also known as ...
 1-158 2.80e-89

serine-protein kinase RsbW; This model describes the anti-sigma B factor also known as serine-protein kinase RsbW. Sigma B controls the general stress regulon in B subtilis and is activated by cell stresses such as stationary phase and heat shock. RsbW binds to sigma B and prevents formation of the transcription complex at the promoter. RsbV (anti-anti-sigma factor) binds to RsbW to inhibit association with sigma B, however RsbW can phosphorylate RsbV, causing disassociation of the RsbV/RsbW complex. Low ATP level or environmental stress causes the dephosphorylation of RsbV.


Pssm-ID: 273879 [Multi-domain]  Cd Length: 159  Bit Score: 257.03  E-value: 2.80e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698    1 MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIK 80
Cdd:TIGR01924   1 MRVHQDTIEMTVPAKPEYVGLIRLTLSGIASRAGYTYDDIEDLKIAVSEACTNAVKHAYKEGEN-GEIGISFHIYEDRLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   81 IVISDKGDSFDYETTKSKIGPYDKDENIDFLREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNG--ERVEI 158
Cdd:TIGR01924  80 IIVSDQGDSFDMDTFKQSLGPYDGSEPIDDLREGGLGLFLIETLMDEVEVYEDSGVTVAMTKYLNREQVDNNVdiKATET 159
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
9-144 2.08e-39

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 129.65  E-value: 2.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   9 EMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIKIVISDKGD 88
Cdd:COG2172    1 SLSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDPD-GPVEVELELDPDGLEIEVRDEGP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 586184698  89 SFDyettkskigPYDKDENIDFLREGGLGLFLIESLMDEVTVY-KESGVTISMTKYI 144
Cdd:COG2172   80 GFD---------PEDLPDPYSTLAEGGRGLFLIRRLMDEVEYEsDPGGTTVRLVKRL 127
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
12-142 4.61e-31

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 108.53  E-value: 4.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   12 VPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIKIVISDKGDSFD 91
Cdd:pfam13581   1 FPADPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHAYREGPE-GPVEVRLTSDGGGLVVTVADSGPPFD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 586184698   92 YETtkskIGPYDKDENIDFLREGGLGLFLIESLMDEVTVYKES-GVTISMTK 142
Cdd:pfam13581  80 PLT----LPPPDLEEPDEDRKEGGRGLALIRGLMDDVEYTRGGeGNTVRMRK 127
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 43-142 3.62e-24

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: 89.63  E-value: 3.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698  43 AKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIKIVISDKGDSFDYettkskIGPYDKDENidfLREGGLGLFLIE 122
Cdd:cd16936    1 VELAVSEAVTNAVRHAYRHDGP-GPVRLELDLDPDRLRVEVTDSGPGFDP------LRPADPDAG---LREGGRGLALIR 70

                         90       100
                 ....*....|....*....|.
gi 586184698 123 SLMDEVTV-YKESGVTISMTK 142
Cdd:cd16936   71 ALMDEVGYrRTPGGKTVWLEL 91
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 46-141 3.30e-03

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 35.32  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698    46 AVSEAVTNAVKHAYKEnnnvGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKDENIDFLREG-GLGLFLIESL 124
Cdd:smart00387   9 VLSNLLDNAIKYTPEG----GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIGGtGLGLSIVKKL 84

                           90       100
                   ....*....|....*....|...
gi 586184698   125 MD--EVTVYKES----GVTISMT 141
Cdd:smart00387  85 VElhGGEISVESepggGTTFTIT 107
 
Name Accession Description Interval E-value
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
 1-159 8.98e-94

serine-protein kinase RsbW; Provisional


Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 268.33  E-value: 8.98e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   1 MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIK 80
Cdd:PRK04069   1 MMEKFDKIEMKIPAKAEYVSIIRLTLSGVANRMGFSYDDIEDMKIAVSEACTNAVQHAYKEDEV-GEIHIRFEIYEDRLE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586184698  81 IVISDKGDSFDYETTKSKIGPYDKDENIDFLREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS 159
Cdd:PRK04069  80 IVVADNGVSFDYETLKSKLGPYDISKPIEDLREGGLGLFLIETLMDDVTVYKDSGVTVSMTKYINREQVENNGERISTS 158
rsbW_low_gc TIGR01924
serine-protein kinase RsbW; This model describes the anti-sigma B factor also known as ...
 1-158 2.80e-89

serine-protein kinase RsbW; This model describes the anti-sigma B factor also known as serine-protein kinase RsbW. Sigma B controls the general stress regulon in B subtilis and is activated by cell stresses such as stationary phase and heat shock. RsbW binds to sigma B and prevents formation of the transcription complex at the promoter. RsbV (anti-anti-sigma factor) binds to RsbW to inhibit association with sigma B, however RsbW can phosphorylate RsbV, causing disassociation of the RsbV/RsbW complex. Low ATP level or environmental stress causes the dephosphorylation of RsbV.


Pssm-ID: 273879 [Multi-domain]  Cd Length: 159  Bit Score: 257.03  E-value: 2.80e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698    1 MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIK 80
Cdd:TIGR01924   1 MRVHQDTIEMTVPAKPEYVGLIRLTLSGIASRAGYTYDDIEDLKIAVSEACTNAVKHAYKEGEN-GEIGISFHIYEDRLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   81 IVISDKGDSFDYETTKSKIGPYDKDENIDFLREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNG--ERVEI 158
Cdd:TIGR01924  80 IIVSDQGDSFDMDTFKQSLGPYDGSEPIDDLREGGLGLFLIETLMDEVEVYEDSGVTVAMTKYLNREQVDNNVdiKATET 159
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
9-144 2.08e-39

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 129.65  E-value: 2.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   9 EMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIKIVISDKGD 88
Cdd:COG2172    1 SLSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDPD-GPVEVELELDPDGLEIEVRDEGP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 586184698  89 SFDyettkskigPYDKDENIDFLREGGLGLFLIESLMDEVTVY-KESGVTISMTKYI 144
Cdd:COG2172   80 GFD---------PEDLPDPYSTLAEGGRGLFLIRRLMDEVEYEsDPGGTTVRLVKRL 127
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
12-142 4.61e-31

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 108.53  E-value: 4.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   12 VPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIKIVISDKGDSFD 91
Cdd:pfam13581   1 FPADPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHAYREGPE-GPVEVRLTSDGGGLVVTVADSGPPFD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 586184698   92 YETtkskIGPYDKDENIDFLREGGLGLFLIESLMDEVTVYKES-GVTISMTK 142
Cdd:pfam13581  80 PLT----LPPPDLEEPDEDRKEGGRGLALIRGLMDDVEYTRGGeGNTVRMRK 127
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 43-142 3.62e-24

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: 89.63  E-value: 3.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698  43 AKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIKIVISDKGDSFDYettkskIGPYDKDENidfLREGGLGLFLIE 122
Cdd:cd16936    1 VELAVSEAVTNAVRHAYRHDGP-GPVRLELDLDPDRLRVEVTDSGPGFDP------LRPADPDAG---LREGGRGLALIR 70

                         90       100
                 ....*....|....*....|.
gi 586184698 123 SLMDEVTV-YKESGVTISMTK 142
Cdd:cd16936   71 ALMDEVGYrRTPGGKTVWLEL 91
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
 8-142 3.85e-14

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: 65.25  E-value: 3.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   8 IEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIKIVISDKG 87
Cdd:cd16942    4 MHLQFSARSENESFARVTVAAFVAQLDPTIDELTEIKTVVSEAVTNAIIHGYNNDPN-GIVSISVIIEDGVVHLTVRDEG 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586184698  88 DSF-DYE-------TTKSKigpydkdenidfLREGGLGLFLIESLMDEVTVYKE--SGVTISMTK 142
Cdd:cd16942   83 VGIpDIEearqplfTTKPE------------LERSGMGFTIMENFMDEVIVESEvnKGTTVYLKK 135
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
 5-142 3.14e-13

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: 63.02  E-value: 3.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698    5 EDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNvGIINIYFEILEDKIKIVIS 84
Cdd:TIGR01925   2 KNKMHLEFLAKSENESFARVTVASFIAQLDPTMEELTDIKTAVSEAVTNAIIHGYEENCE-GVVYISATIEDHEVYITVR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586184698   85 DKGDSF-DYETTKSKIGPYDKDenidfLREGGLGLFLIESLMDEVTVY--KESGVTISMTK 142
Cdd:TIGR01925  81 DEGIGIeNLEEAREPLYTSKPE-----LERSGMGFTVMENFMDDVSVDseKEKGTKIIMKK 136
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
 22-141 2.52e-11

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 60.69  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698  22 IRLTLSGvfsragatyDDIE-DAKIAVS------EAVTNAVKHAYKENNNvGIINIYFEILEDKIKIVISDKGDSFdyet 94
Cdd:COG3920  381 IRIELDG---------PDVElPADAAVPlglilnELVTNALKHAFLSGEG-GRIRVSWRREDGRLRLTVSDNGVGL---- 446

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 586184698  95 tkskigpydkDENIDFLREGGLGLFLIESLMD----EVTVYKESGVTISMT 141
Cdd:COG3920  447 ----------PEDVDPPARKGLGLRLIRALVRqlggTLELDRPEGTRVRIT 487
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
46-98 7.02e-05

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 41.53  E-value: 7.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 586184698  46 AVSEAVTNAVKHAykennNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSK 98
Cdd:COG4585  166 IVQEALTNALKHA-----GATRVTVTLEVDDGELTLTVRDDGVGFDPEAAPGG 213
LytS COG3275
Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];
51-100 8.14e-05

Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];


Pssm-ID: 442506 [Multi-domain]  Cd Length: 352  Bit Score: 41.39  E-value: 8.14e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 586184698  51 VTNAVKHAYKENNNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIG 100
Cdd:COG3275  262 VENAIKHGISSKEGGGTISISIEVEGDRLVIEVENNGVGIQPKKKKKGSG 311
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 38-141 2.08e-04

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: 38.50  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698   38 DDIEDAKIAVSEAVTNAVKHAYKENnnvgiiNIYFEI-LEDKIKIVISDKGDSFDYETTKSKIGPYDKDENIDFlREGGL 116
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAG------EITVTLsEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGG-GGTGL 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 586184698  117 GLFLIESLMD----EVTVYKES--GVTISMT 141
Cdd:pfam02518  74 GLSIVRKLVEllggTITVESEPggGTTVTLT 104
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 47-118 1.01e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 36.38  E-value: 1.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586184698  47 VSEAVTNAVKHAykennNVGIINIYFEILEDKIKIVISDKGDSFDYETTKskigpydkdenidflREGGLGL 118
Cdd:cd16917    5 VQEALTNALKHA-----GASRVRVTLSYTADELTLTVVDDGVGFDGPAPP---------------GGGGFGL 56
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 47-124 1.25e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 37.01  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586184698  47 VSEAVTNAVKHAYKENNNvGIINIYFEILEDKIKIVISDKGDSFdyettkskigpydkDENIDFLREGGLGLFLIESL 124
Cdd:cd16951   44 VNELLQNALKHAFSDREG-GTITIRSVVDGDYLRITVIDDGVGL--------------PQDEDWPNKGSLGLQIVRSL 106
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 46-141 3.30e-03

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 35.32  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586184698    46 AVSEAVTNAVKHAYKEnnnvGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKDENIDFLREG-GLGLFLIESL 124
Cdd:smart00387   9 VLSNLLDNAIKYTPEG----GRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIGGtGLGLSIVKKL 84

                           90       100
                   ....*....|....*....|...
gi 586184698   125 MD--EVTVYKES----GVTISMT 141
Cdd:smart00387  85 VElhGGEISVESepggGTTFTIT 107
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
49-100 7.02e-03

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 35.72  E-value: 7.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 586184698  49 EAVTNAVKHAykennNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIG 100
Cdd:PRK11644 417 EGLNNIVKHA-----DASAVTLQGWQQDERLMLVIEDDGSGLPPGSGQQGFG 463
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
53-118 7.24e-03

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 35.76  E-value: 7.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586184698  53 NAVKHAYKENNNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKDEnidflREGGLGL 118
Cdd:COG2972  347 NAIEHGIEPKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKG-----EGRGIGL 407
 
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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