ID A0A0D2DJI9_9EURO Unreviewed; 1953 AA.
AC A0A0D2DJI9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=PV06_06132 {ECO:0000313|EMBL:KIW42600.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW42600.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW42600.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW42600.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; KN847336; KIW42600.1; -; Genomic_DNA.
DR RefSeq; XP_016262816.1; XM_016407212.1.
DR STRING; 215243.A0A0D2DJI9; -.
DR GeneID; 27358206; -.
DR VEuPathDB; FungiDB:PV06_06132; -.
DR HOGENOM; CLU_000893_1_0_1; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05167; PI4Kc_III_alpha; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR045495; PI4K_N.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF15; PHOSPHATIDYLINOSITOL 4-KINASE ALPHA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19274; PI4K_N; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1373..1548
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1653..1937
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1953 AA; 219677 MW; D17C8C1A66673E62 CRC64;
MDLGYGGLRR QAFHKLAILT AQRSHHREAD FRRLTSSILP AKNQPNGVLD GVLRALTPTS
RTLITLRELD ILLALCGSAH NIHDPSHAER LVNQLSTYLP EAHAQLFAPS PFLHEIKPAP
WTALTFQLTQ ALLILGLRFP TLKVRVSECL KTYLSNWSQS AGALVSLGAE EHDEDNEGEA
QEVAAITVSL VGFLDAAALH ENFWSSYERV ELIRTLEESL SDKFLIRVET ASSAIRTSIS
AHMSSRDWKK YLKRFAAQGL PVGAMMLQKG FMKLVLACTS RMLCDEHTVE CGDVLDQYIA
GTHLGRSRDE DVTEDMIEYL VSIISDQIRV LEDGSDYLQL SSAWQQRLAF SVKAYALEAF
LHCMILDEDL ADPDDLFNWL EDSIGNQAQM ADINLADIAL KSLAIVAKHV PEEASNFARV
LLRFIVRGTS TSEAVAIAAQ SLSHILKMLS QDAVITTVYS LGNVLSSQTG AEKTHHPWAG
GEINGHHGSL SSASKLRTGS VFSLSLSGDE ETSLVCGNVA HAIVVIAREC KDPRITALVQ
TMMIQKVGRI SLPVDARIIE QSARLSIQGK ENEFKTLLRL YSRLHREALL QDNNLIFDAV
RNAEEYLAYN IGSRSPLFKI FATHLLERIL SKGDVVEGEF KQSAEVEQAA KEIAPLLKPL
SIIASRRPVS SQEGGFIEDP DILAMSREVW YNIAVHGITL QSRIGQQYYH ELRLLAMNSR
PLVDDDRAEL LESDVELNTV LRRGMSPQHT AEQRKNLIAA IPERDSDVRQ LSYQKVVFLN
AVFLVESLRA TSGSCAEILD YFTDPTTQTS HMGLCLTSIA NEVVKRYTSK VIVGGEMEFS
APYVSRQLAD ILSGCCHRSG KMQEVARTAT NHIISFAPSA LCQKAALFAL LELLSLMWSS
CLDADVDEYE WRPFLTSTRG KITIELSDDY AFRKRTLNTL YSDAKKWVAT VMGVAPLDVK
GLLQTYLSEF DDTGAYGHVS LGRSFALEMG SMIPPLDHRL SALDQKGDFT HINMASDFMA
QYTTRQEYRF TGIPDYQLGN VHIDNITGRR ASVGRQATDN TYVLSNVLLD LHKRTEHKTH
VQASEVKDVL RRAAALLCQS KKSQTTIVHH LVHIPFQIFT KESIKLGISL WLGVIHENPR
MEPRILMEAA QAWEKTIDRK EGIFNPSFRH HDPFYVKEEF APTDKAAIQR QAQNAHNTIS
PHFRLLQFFQ SHFNSIRLGS GNTQRNFVRM LERTLLGFIH IKGHPLLREM QFSLVHFALR
VLKTSTCISK LYMWKLRDLI LSVGLQWFSH PLSWSFGGNR LQLKAEVQIM QDVLVSLQSA
KQPVLATAVS RKDPQQKQDL LEALLQNEIT RLNVWLAPLG HAGHQTHSEA QIAVYSRTAW
LENPALAVQL VSRFPSEQLR RDVRFLLLNF TDKALNEPDA IDLLIGDKLP SDVSGQLKYL
LYWAPVNPMQ AVTYFLPAFG NHPFVLQYAM GALESHSVDV TFFYVPQIVQ SLRYDALGYV
ERYIIETGKF SQLFAHQIIW NMKANAYKDE DSQEPDSVKP TLDKVMDSLV SSFSGADRDF
YQREFAFFGE VTDISGKLKP FIKKPKPEKK AKIEEELRKI KVEVGVYLPS NPDGVVVGID
RKSGKPLQSH AKAPYMATFR IRKTRETPEN DPRSNAETAF KAIHVPRRGH SRQNTNEISD
LGLDDNPRTY EVWQSAIFKV GDDCRQDVLA LQMIAAFRGI FNSVGLDVYV FPYRVTATAP
GCGVIDVLPN SISRDMLGRE AVNGLHDYFI TKYGGEHSIR YQEARHEFVK SMAAYSVISY
LLQFKDRHNG NIMIDDKGHI LHIDFGFCFD IAPGGVKFER APFKLTPEMI AVMGGDDPNI
SQSYRWFEEL TIKAFLCSRQ YCEKLSHLVS LMLDSGLPCF KPETMRNFRN RFVLDKSDRE
AAEFMLGCIK KSAGNVSTKV YDEFQLLTNG IPY
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