MULTISPECIES: bifunctional protein-serine/threonine

LOCUS       WP_004342954             531 aa            linear   BCT 20-NOV-2023
            kinase/phosphatase [Pseudomonas].
ACCESSION   WP_004342954
VERSION     WP_004342954.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Bork,P., Brown,N.P., Hegyi,H. and Schultz,J.
  TITLE     The protein phosphatase 2C (PP2C) superfamily: detection of
            bacterial homologues
  JOURNAL   Protein Sci 5 (7), 1421-1425 (1996)
   PUBMED   8819174
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Cohen,P.
  TITLE     The structure and regulation of protein phosphatases
  JOURNAL   Annu Rev Biochem 58, 453-508 (1989)
   PUBMED   2549856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..531
                     /product="bifunctional protein-serine/threonine
                     kinase/phosphatase"
                     /EC_number="2.7.11.-"
                     /EC_number="3.1.3.-"
                     /EC_number="3.1.3.16"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004722 - protein serine/threonine
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=58811
     Region          7..211
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
     Region          231..>506
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mvtpapalaa skghllaiad gvsqcadggl aarsslqala ldyyatpetw aivqsldrll
       61 laqnrwlqan gggqpllttl talvlrgtry tlahvgdcra ylwrdgellr qtsdhvweqp
      121 hmqhvltral gldqhlvvdy legdlepgsq wllvsdgvwa tlgdsgirsi lrnaeepqrs
      181 aealvraahl agsqdnasal lvrveavpag slgdalaqlg hwplppplkp dqlfegwrvr
      241 qllgesrqsl lyrvedgqgq pwllktlpaa raddplatqa llleewflrr vqgrhfpelh
      301 glaqrqhlyy lmrehpgetl aerlrnhgpl slpewlglan qllrglgqlh rrnllhrdlk
      361 penlhlgrdg elrlldfgla wcpglsredp hllpgtpsyl apecfsgtsp svrqdlyatg
      421 vclyqaltgr ypygeieafq hprfgrpvpp sryrpdlpaw iddlllrava cdpaqrfeta
      481 eewllslqqg ealpaaatrp llereplqtw raiallslaa nlalllvwlk g