Conserved Protein Domain Family
HisKA

?
cd00082: HisKA 
Click on image for an interactive view with Cn3D
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.
Statistics
?
PSSM-Id: 119399
View PSSM: cd00082
Aligned: 463 rows
Threshold Bit Score: 30.2584
Threshold Setting Gi: 6226671
Created: 1-Nov-2000
Updated: 17-Jan-2013
Structure
?
Program:
Drawing:
Aligned Rows:
 
phosphorylationdimer interface
Conserved site include 1 residue -Click on image for an interactive view with Cn3D
Feature 1:phosphorylation site [posttranslational modification site]
Evidence:
  • Comment:site of trans-autophosphorylation and phosphate transfer reaction
  • Comment:phosphate is transfered to Asp of a downstream response regulator

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
Feature 1                    #                                                       
1JOY_A         9 ADDRTLLMAGVSHDLRTPLTRIRLATEMMSeq---------dGYLAESINKDIEECNAIIEQFIDYLX 67
gi 15600079  241 YQRLQQFSADLAHEIRTPIGSLMGHGQVALrqprs---neeyQALIASNQEELERIARMVESILFLAR 305
gi 12484567  239 VQQLSQFSDDLAHELRAPLTNLMGKAQLTLsrqrp---pdeyKAVLESNTEELERLARIVSDMLFLAQ 303
gi 6578850   281 LATLGRFSAQMAHDLKNPIAAMKGAAQYLKeehargrswdgqGEFLDLLLEQVERLDRVVDTYQRLAR 348
gi 2500767   233 FERLSQFADDLAHELRTPINALLGQNQVTLsqtrs---iaeyQKTIAGNIEELENISRLTENILFLAR 297
gi 15794694  310 LAALGQLTANLAHEIRNPMSAIRHANDLLRenmeagaadpfnAKLCKIIDGNVCRIDKMLEDISSLNK 377
gi 2443475   378 LASMGRLVASVAHQIRNPLAAISQAAELLDdpg------eggEPLRPEGRGVETRLLRIIRDNVRRLD 439
gi 3851181   310 LAALGQLTANLAHEIRNPMSAIRHADGGTLfvdev--adlplSMQVKLLRAIQEKAVRRIGDATEQPV 375
gi 55977759  240 FVRLSQFSSNLAHDMRTPLTNLLAEAQVALskprt---adeyRDVIESSIDEYQRLSRMIEDMLFLAR 304
gi 110282957 233 YQKLSRFSADLAHDLRTPLNNLIGHAEVALsrdrt---gpeyVALVEESLVEYQRLARMIDAMLFLAR 297

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap