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Database: UniProt
Entry: A0A0J9XF02_GEOCN
LinkDB: A0A0J9XF02_GEOCN
Original site: A0A0J9XF02_GEOCN 
ID   A0A0J9XF02_GEOCN        Unreviewed;      1919 AA.
AC   A0A0J9XF02;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN   ORFNames=BN980_GECA13s00802g {ECO:0000313|EMBL:CDO55957.1};
OS   Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Geotrichum.
OX   NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO55957.1, ECO:0000313|Proteomes:UP000242525};
RN   [1] {ECO:0000313|EMBL:CDO55957.1, ECO:0000313|Proteomes:UP000242525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO55957.1,
RC   ECO:0000313|Proteomes:UP000242525};
RA   Casaregola S.;
RL   Submitted (MAR-2014) 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; CCBN010000013; CDO55957.1; -; Genomic_DNA.
DR   STRING; 1173061.A0A0J9XF02; -.
DR   OrthoDB; 147843at2759; -.
DR   Proteomes; UP000242525; 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; 1.
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, ECO:0000313|EMBL:CDO55957.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1338..1528
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          1625..1903
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          1629..1652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1919 AA;  215376 MW;  2A38C24FA91A4234 CRC64;
     MDDFGISRKG RGIRAQALER LSRLSASDPK KAESLDKLTG ALTYSDNSLN GSTTAISAKE
     LEILLALARS ASFIQDSTQA LKLTRLLGRY LCENPSQKIA NSATNREVRP SPWQVSSKCL
     TRAILNLGYK FQTDNDIFTE SQSILSRYLD ITFSAFLTAE TFDNQASFFP LLFSVQGFLE
     AITDKITIVP YSFIQKLLIK SREVFTTEFL LALETTIAKT SSNLSREEYA AALLSIRTAR
     SSDFIWSYYA ESYSRFNKPL GAMQFSSYLC DLALAVSSKI IDTSELPSAN LIDRLLSVEK
     LAKLTEQQYD ILDLVTDYAV DQITSLDEGA DYIELASPEK IDLAYATKAS ALQVIGVAVY
     FKHFSVEEAV KLVISSISHE YGMSNNLLSV TVFKLASLLC LFHDEIGGVV IKYFSHFITL
     PGVNASLVQK CAETLVFGLK TLSQDVVVST IYTFINLLSV DHDAVSPPIP AKGYHDQASG
     SAVGTEDTPS PDSYSTALYR NAITAVVTIA SKYGDPQIAG LASTVLNQKL NSSLVLDREV
     ALGMADLVMF VNEKEFRTIW KSFTFLLNNS FKSKDNESGD LISEVLYKLS TNLDRNHYLY
     DSYLAELLQA IVNRGDVHEL EHHRPHVEIS ATANEISIFL APLATLLPGL YEAPYETADN
     EINDLFRNAW FNMVVHGFSK NSDLTAKYKN ELEIIARSTP PLVSEVSTNK IESELELNTV
     LQRGSSHHNV NNQKEIMESI TSSNIFDFRN IQYPKLMFLS ATVLLESLRA NTGNCSKSLL
     YFGDPGIRNG ETRRYMAFIT MDVVKAYITN VIKGGIPYFA IDKVAAQLKE MFVFCCHRVK
     SIQDMAFECC NILIGSVPSA LCQKISLFAL LDLLTLLWSS CIDADTDEYE PRSIFHTKNT
     NIRLELSDSY DHRRESLQRL LVKAKEWVTV ALETMNFDVK NLLTSYLNDM NSSRPLNDVA
     LGFTFALEMG GSVSGSDREL AAISKASNIS TDTSSGFLSQ FIWSREIRAL PNFATSQEAI
     ALYDKEAVEI RQKLDTLFVN INSHAHGTSH VHFTEAKSLI FKASGFFTHK SEGRNIARLC
     VKIPFRVFTE SSIQFGITLW LWAINENPSL KPLILSEVSQ LWEWSVGECH GIYTRRHDLV
     DAADAKMEYS PSNKAEINHD AALASREFSC HQQLMRFLSS AFKSSIYESS HLLKMFTRLL
     TVGLEGLNHA SFHPLARPAR FELIQFSLDV LEVHTRLSSS NVVHSLKDLI ISSALTWFSQ
     PSQWPFGGNK LKLRADVDLL SKIAVTLKSM YISTNSKSQA FVATKRDLLL YFMADELAKM
     TAWLDPLQTG PNFRDNLGKK LIPSFTVSVN VLNNAWDIDP VLAVYLVERF KSNDLASRLE
     ALIGKSPLKV VSVPEALPYF LRARNSRKVD ASVDHQLVYW ASVSPIDSIN LFLPSYHADS
     LLLQYAMRSL KSHDVDITFF YVPQLVQSLR YDVSGYVEQY ILETAQISQL FAHQIIWNIL
     ANLFKGDDLP ENTAEDSVNP ILERVIKRMT SAFKDEDREF YEREFTFFNT VTGISRSLMP
     YLRKTKAEKK AKIDEEIAKI VVDEGVYLPS NPDGDVIDID RKSGRPLQSH AKTPFMATFK
     IRREVRDLGE GENSAAGAVS ANDNDDDEED GERTKTIEVW QSAIFKVGDD CRQDVLALQI
     ISVFRSIFNS YGLDLYVFPY RVTATAPGCG VIDVLPNSIS RDMLGREAVN GLYEYYTTKH
     GGEDSIQFQR ARNNFVKSLA AYSVISYLIQ FKDRHNGNIM YDDQGHILHI DFGFCFDIVP
     GGVKFEAAPF KLTHEMVAVM GGSTTTQAYR WFEELCVKAF LACRPHSETI IKVVLPMLDS
     GLPCFKGEST IKRLRNRFVL DKTEREAALH FRGLIKKSFE SVYTKGYDEF QRITNGIPY
//
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