ID   KAPC_ENCCU              Reviewed;         322 AA.
AC   Q8SRK8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Probable cAMP-dependent protein kinase catalytic subunit;
DE            EC=2.7.11.11;
GN   OrderedLocusNames=ECU07_0520;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.11;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR   EMBL; AL590447; CAD25584.1; -; Genomic_DNA.
DR   RefSeq; NP_585980.1; NM_001041602.1.
DR   AlphaFoldDB; Q8SRK8; -.
DR   SMR; Q8SRK8; -.
DR   STRING; 284813.Q8SRK8; -.
DR   GeneID; 859409; -.
DR   KEGG; ecu:ECU07_0520; -.
DR   VEuPathDB; MicrosporidiaDB:ECU07_0520; -.
DR   HOGENOM; CLU_000288_63_5_1; -.
DR   InParanoid; Q8SRK8; -.
DR   OMA; WACGILC; -.
DR   OrthoDB; 963519at2759; -.
DR   Proteomes; UP000000819; Chromosome VII.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd05123; STKc_AGC; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045270; STKc_AGC.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..322
FT                   /note="Probable cAMP-dependent protein kinase catalytic
FT                   subunit"
FT                   /id="PRO_0000086070"
FT   DOMAIN          7..261
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          262..322
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   ACT_SITE        132
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         13..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   322 AA;  36415 MW;  A6548FF96A4B4DE5 CRC64;
     MLKIQDFEFV KVVGVGAFGK VHLVRLKSSP TSVFAMKMLD FGEILRQRLA DQLENEISIL
     KRIYGCPFVA KLYSTDFHGG KVGLIMEYVG GGELFYWLKK CGRFDEQMAR FYAAEIISAL
     RFIHGRGILY RDLKPENILI TSTGHIKLID FGFSVYESEN IYMISGTPEY MSPEKLRSED
     DGRASDYWGL GVMIYEMLCG DPPFYDSSAD AIYHKILESN VVFPHYVSPV ARCLITGLLD
     KNRATRLGTK GICEIMGHPF FKGIDWHEVE SRRIEPPFIP NPNTVLSSLA SSGELKGTDD
     AETVVLKPYK HIKHLYKVSK GL