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Conserved domains on  [gi|518729220|ref|WP_019889334|]
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MULTISPECIES: anti-sigma regulatory factor [Streptomyces]

Protein Classification

ATP-binding protein( domain architecture ID 382)

ATP-binding protein containing histidine kinase-like ATPase domain, similar to Streptomyces subrutilus DNA gyrase an an essential bacterial enzyme that catalyzes the ATP-dependent negative super-coiling of double-stranded closed-circular DNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HATPase super family cl00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
 10-86 4.66e-16

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


The actual alignment was detected with superfamily member PRK04069:

Pssm-ID: 469604 [Multi-domain]  Cd Length: 161  Bit Score: 69.95  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518729220  10 TQDFVEVRLPAAGAYLSVLRTATAGLAARLDFTLDEIEDLRIAVDEACAILLQQA----VPGSVLSCvFRLVDDSLDVTV 85
Cdd:PRK04069   4 KFDKIEMKIPAKAEYVSIIRLTLSGVANRMGFSYDDIEDMKIAVSEACTNAVQHAykedEVGEIHIR-FEIYEDRLEIVV 82


                 .
gi 518729220  86 S 86
Cdd:PRK04069  83 A 83
 
Name Accession Description Interval E-value
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
 10-86 4.66e-16

serine-protein kinase RsbW; Provisional


Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 69.95  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518729220  10 TQDFVEVRLPAAGAYLSVLRTATAGLAARLDFTLDEIEDLRIAVDEACAILLQQA----VPGSVLSCvFRLVDDSLDVTV 85
Cdd:PRK04069   4 KFDKIEMKIPAKAEYVSIIRLTLSGVANRMGFSYDDIEDMKIAVSEACTNAVQHAykedEVGEIHIR-FEIYEDRLEIVV 82


                 .
gi 518729220  86 S 86
Cdd:PRK04069  83 A 83
rsbW_low_gc TIGR01924
serine-protein kinase RsbW; This model describes the anti-sigma B factor also known as ...
 11-86 3.28e-15

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: 67.90  E-value: 3.28e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518729220   11 QDFVEVRLPAAGAYLSVLRTATAGLAARLDFTLDEIEDLRIAVDEACAILLQQAVPGS---VLSCVFRLVDDSLDVTVS 86
Cdd:TIGR01924   5 QDTIEMTVPAKPEYVGLIRLTLSGIASRAGYTYDDIEDLKIAVSEACTNAVKHAYKEGengEIGISFHIYEDRLEIIVS 83
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
15-86 6.65e-08

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 47.99  E-value: 6.65e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518729220  15 EVRLPAAGAYLSVLRTATAGLAARLDFTLDEIEDLRIAVDEACAILLQ---QAVPGSVLSCVFRLVDDSLDVTVS 86
Cdd:COG2172    1 SLSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRhayGGDPDGPVEVELELDPDGLEIEVR 75
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
18-58 2.85e-03

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 35.34  E-value: 2.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 518729220   18 LPAAGAYLSVLRTATAGLAARLDFTLDEIEDLRIAVDEACA 58
Cdd:pfam13581   1 FPADPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACT 41
 
Name Accession Description Interval E-value
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
 10-86 4.66e-16

serine-protein kinase RsbW; Provisional


Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 69.95  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518729220  10 TQDFVEVRLPAAGAYLSVLRTATAGLAARLDFTLDEIEDLRIAVDEACAILLQQA----VPGSVLSCvFRLVDDSLDVTV 85
Cdd:PRK04069   4 KFDKIEMKIPAKAEYVSIIRLTLSGVANRMGFSYDDIEDMKIAVSEACTNAVQHAykedEVGEIHIR-FEIYEDRLEIVV 82


                 .
gi 518729220  86 S 86
Cdd:PRK04069  83 A 83
rsbW_low_gc TIGR01924
serine-protein kinase RsbW; This model describes the anti-sigma B factor also known as ...
 11-86 3.28e-15

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: 67.90  E-value: 3.28e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518729220   11 QDFVEVRLPAAGAYLSVLRTATAGLAARLDFTLDEIEDLRIAVDEACAILLQQAVPGS---VLSCVFRLVDDSLDVTVS 86
Cdd:TIGR01924   5 QDTIEMTVPAKPEYVGLIRLTLSGIASRAGYTYDDIEDLKIAVSEACTNAVKHAYKEGengEIGISFHIYEDRLEIIVS 83
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
15-86 6.65e-08

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 47.99  E-value: 6.65e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518729220  15 EVRLPAAGAYLSVLRTATAGLAARLDFTLDEIEDLRIAVDEACAILLQ---QAVPGSVLSCVFRLVDDSLDVTVS 86
Cdd:COG2172    1 SLSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRhayGGDPDGPVEVELELDPDGLEIEVR 75
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
18-58 2.85e-03

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 35.34  E-value: 2.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 518729220   18 LPAAGAYLSVLRTATAGLAARLDFTLDEIEDLRIAVDEACA 58
Cdd:pfam13581   1 FPADPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACT 41
 
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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