ID   A0A1A8VW71_9APIC        Unreviewed;       894 AA.
AC   A0A1A8VW71;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Phosphatidylinositol 3-and 4-kinase, putative {ECO:0000313|EMBL:SBS83083.1};
GN   ORFNames=POVCU2_0018830 {ECO:0000313|EMBL:SBS83083.1};
OS   Plasmodium ovale curtisi.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=864141 {ECO:0000313|EMBL:SBS83083.1, ECO:0000313|Proteomes:UP000078560};
RN   [1] {ECO:0000313|Proteomes:UP000078560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Naeem Raeece;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00008941}.
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DR   EMBL; FLQU01000247; SBS83083.1; -; Genomic_DNA.
DR   Proteomes; UP000078560; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR044571; P4KG1-8.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   PANTHER; PTHR45800; PHOSPHATIDYLINOSITOL 4-KINASE GAMMA; 1.
DR   PANTHER; PTHR45800:SF11; PI3K_PI4K CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:SBS83083.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078560};
KW   Transferase {ECO:0000313|EMBL:SBS83083.1}.
FT   DOMAIN          177..399
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00454"
FT   REGION          479..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..658
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..764
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..797
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   894 AA;  102382 MW;  6B41F14ABA42F3BC CRC64;
     MGSNSLPMSQ QMYFSTHNAL RINEENDVIN TLFYEINGNR HISLYIFPFY DVQMLKRLLI
     KKLDLPRGIK VNDIIIFYKG IKLPNYRVIS TYLDNTNRRV GGDVGVGIGI GSEKKKXXXX
     VNKLYWAIKD TNPNASIRVI DNKSYPPFFE NILNDIKLAF KKNISPKLTM DGTGGTYLLF
     NGKKKVCSVF KPLDEEAFAP FNPRGYEGKM YQEGFRSGVL SGEGASREIA AYILDSNYNN
     FSNVPCTIMV EACNPYFNNK SKLKYVDKEN NLKWKCGSLQ EFIDSKESVG NYDYKQFSIR
     DIHKIAILDI RVMNLDRNDG NILVSPLKSL KDSCNQFLYR NNKSFSTNDE DILKRIVTID
     KKPSRDAEKI RNKLLIREDC IRTMRVCTRL LQIGARMHLN LHEIAKISTR KNIDEESILE
     RLVKDSIVQA YQMMDSTSLM STNRLGYILD LAEIKMNKKK KPCKTKTIEI IDDKVKGECA
     NDPKKESTTK RKDVSNLSKE KPGHISSDKN KKEEHFNASS MNCFKDVREE VSQKGMENTN
     DELVKGIQGI DDGRRKSIHG DISNSCDKMK NFMGMEDGKG KCEHSPIPNY VNRLEKGKVD
     DASGALYISS KSKPSERTHC ASAGYGELYK ACGVSAARQN ENREKCKNGD DGESSENCEK
     SKSSSNSLSN KSEYTLVTAS SSSNNDERRQ HSVNNSAPPE DDGKEEHCNV DIDDTKNVGE
     EKKEETQIRG KQSEIMENKL EERTKEKNNP QRVVALSDEK RFHDIDYDEE DEEEENDDDD
     DDDDDDDDDD DDDDDDDVTF KKPSGTIKRI SECTGTAYRN MEINKINSIW MIRDKNNKII
     NVKWENKMFE KLFFETFENY VKKYINDYHP EWKAYPYNGA NIPCTKHAYL SSIE
//