ID   KAPC_ASCSU              Reviewed;         337 AA.
AC   P49673;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=cAMP-dependent protein kinase catalytic subunit;
DE            Short=PKA C;
DE            EC=2.7.11.11;
GN   Name=CAPK;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7556139; DOI=10.1111/j.1432-1033.1995.tb20788.x;
RA   Jung S., Hoffmann R., Rodriguez P.H., Mutzel R., Hofer H.W.;
RT   "The catalytic subunit of cAMP-dependent protein kinase from Ascaris suum.
RT   The cloning and structure of a novel subtype of protein kinase A.";
RL   Eur. J. Biochem. 232:111-117(1995).
CC   -!- FUNCTION: Phosphorylates phosphofructokinase to activate it.
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   -!- SUBUNIT: Composed of two regulatory chains and two catalytic chains.
CC       {ECO:0000250}.
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; X69806; CAA49464.1; -; mRNA.
DR   PIR; S66515; S66515.
DR   AlphaFoldDB; P49673; -.
DR   SMR; P49673; -.
DR   EnsemblMetazoa; AgR002_g486_t01; AgR002_g486_t01; AgR002_g486.
DR   BRENDA; 2.7.11.11; 474.
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   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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00133; S_TK_X; 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   2: Evidence at transcript level;
KW   ATP-binding; cAMP; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..337
FT                   /note="cAMP-dependent protein kinase catalytic subunit"
FT                   /id="PRO_0000086066"
FT   DOMAIN          29..283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          284..337
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         35..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   337 AA;  39172 MW;  5D031EC3AF403E5D CRC64;
     MENREQEEIE PCVSITIDPN NNKLNVDDFD RICTIGTGSF GRVYLVQHRA SEQYFALKKM
     AIREVVSMRQ TEHVHSEKRL LSRLSHPFIV KMYCASWDKY NLYMLFEYLA GGELFSYLRA
     SRTFSNSMAR FYAAEIVCAL QYLHSKNIAY RDLKPENLML NKEGHLKMTD FGFAKEVIDR
     TWTMCGTPEY LAPEVIGNKG HDTAVDWWSL GVLIYEMMIG IPPFRGKTLD EIYEKIILGK
     LRFTRSFDLF AKDLVKKLLQ VDRTQRLGNQ KDGAADVMNH KWFTDIDWDD VQNMKLTPPI
     IPTLYSNGDT GNFDSYDECS DDEIAAPQHE LELFEDW