ID   KPK2_PLAFK              Reviewed;         510 AA.
AC   Q02595;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Probable serine/threonine-protein kinase 2;
DE            EC=2.7.11.1;
GN   Name=PK2;
OS   Plasmodium falciparum (isolate K1 / Thailand).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1378403; DOI=10.1111/j.1432-1033.1992.tb17051.x;
RA   Zhao Y., Kappes B., Yang J., Franklin R.M.;
RT   "Molecular cloning, stage-specific expression and cellular distribution of
RT   a putative protein kinase from Plasmodium falciparum.";
RL   Eur. J. Biochem. 207:305-313(1992).
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=2.7.11.1;
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=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Membrane.
CC   -!- DEVELOPMENTAL STAGE: Is highly expressed during the young trophozoite
CC       stage but gradually decreases in amount with further growth. No protein
CC       can be detected during the ring stage, only small amount is expressed
CC       during the schizont stage.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; X63648; CAA45179.1; -; mRNA.
DR   PIR; S23466; S23466.
DR   AlphaFoldDB; Q02595; -.
DR   SMR; Q02595; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Kinase; Membrane; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..510
FT                   /note="Probable serine/threonine-protein kinase 2"
FT                   /id="PRO_0000086165"
FT   DOMAIN          111..364
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          408..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        230
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         117..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   510 AA;  59006 MW;  0605C3A73C76F4B9 CRC64;
     MEKRYQQLFK GKRIDFPLAT GAASHVSLTY DEKKNPYLLC WTYIYQEKPE FTVPLKGCRI
     INNITEIGPC IHIITSNEEY QFQCRSKEEF DEMSQFFNML GYPILGFKNV YVLNKKIGKG
     SFSTAYIGTN ILYGNRVVVK EVDKSKVKES NVYTEIEVLR KVMHKYIIKL ISAYEQEGFV
     YLVLEYLKGG ELFEYLNNNG PYTEQVAKKA MKRVLIALEA LHSNGVVHRD LKMENLMLEN
     PNDPSSLKII DFGLASFLNS PSMNMRCGSP GYVAPEILKC ASYGTKVDIF SLGVILFNIL
     CGYPPFRGNN VKEIFKKNMR CHISFNTKHW INKSESVKEI ILWMCCKNPD DRCTALQALG
     HQWFLPKLTD MHMTANINEL KRNEAIVHKS NDQQDMCKKC KHFNNTQNDD IYNNNNNNNQ
     LDPNKNHKNN YNDYKNYFDT MLKIDDKYSE NLIKDKTSMD SISLNKKDYD AYLVHSNEHD
     TVVLHGKCQT TKNSSSLLSY KCSRRSPPQN