ID   PIK1_CANAL              Reviewed;         977 AA.
AC   Q9UW20; O74714; Q59YW7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Phosphatidylinositol 4-kinase PIK1alpha;
DE            Short=PI4-kinase;
DE            Short=PtdIns-4-kinase;
DE            EC=2.7.1.67;
GN   Name=PIKALPHA; Synonyms=PIK1;
GN   OrderedLocusNames=C5_01765C_B {ECO:0000312|CGD:CAL0000202032};
GN   ORFNames=CaO19.10711;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=10455055; DOI=10.1126/science.285.5431.1271;
RA   Hull C.M., Johnson A.D.;
RT   "Identification of a mating type-like locus in the asexual pathogenic yeast
RT   Candida albicans.";
RL   Science 285:1271-1275(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gamo F.J., Garcia-Bustos J.F.;
RT   "Cloning and sequencing of a C. albicans phosphatidylinositol 4-kinase.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts on phosphatidylinositol (PI) in the first committed step
CC       in the production of the second messenger inositol 1,4,5,-
CC       trisphosphate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC         1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC         H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC         EC=2.7.1.67;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: The C.albicans mating-type-like (MTL) locus contains, in
CC       addition to the genes for the regulatory proteins (MTLA1, MTLA2,
CC       MTLALPHA1 and MTLALPHA2), a and alpha idiomorphs of a
CC       phosphatidylinositol kinase (PIKA and PIKALPHA), a poly(A) polymerase
CC       (PAPA and PAPALPHA) and an oxysterol binding protein-like protein (OBPA
CC       and OBPALPHA). PIKALPHA is not represented in the genomic sequence of
CC       strain SC5314 because that haploid assembly includes the mating type a
CC       allele of this locus. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF167163; AAD51410.1; -; Genomic_DNA.
DR   EMBL; AJ011588; CAA09718.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9UW20; -.
DR   PRIDE; Q9UW20; -.
DR   CGD; CAL0000202032; PIKALPHA.
DR   eggNOG; KOG0903; Eukaryota.
DR   HOGENOM; CLU_002446_2_0_1; -.
DR   InParanoid; Q9UW20; -.
DR   OMA; QPCFNAG; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IGI:CGD.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IGI:CGD.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR021601; Phosphatidylino_kinase_fungi.
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; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048; PTHR10048; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF11522; Pik1; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 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   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Transferase.
FT   CHAIN           1..977
FT                   /note="Phosphatidylinositol 4-kinase PIK1alpha"
FT                   /id="PRO_0000088832"
FT   DOMAIN          1..125
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT   DOMAIN          679..960
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          205..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..691
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          826..834
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          845..869
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   COMPBIAS        216..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        87
FT                   /note="R -> G (in Ref. 2; CAA09718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        582
FT                   /note="S -> A (in Ref. 2; CAA09718)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   977 AA;  110699 MW;  C7899B61AC352AA4 CRC64;
     MSADITETPN KQLLEQIRSP SFSLFNCIYE LKNHTDSIGI QHELVKKLYS FPYEDLQFFI
     PQFVQLLVTY DSESMALEEF IITYSSRYPH FSLIVFWNLQ AYIFELKNEP ESRSFQAVRN
     LITKIQNIMF NADQQTVKAP EFRENFLPAL VLCGAVASSV LLPSFKSYCL PMIKAQGKQQ
     KSLVFKLVNF QKSLTKNLTL KNQRMSADIP KGSHSDDETA TSSSIKPSLS RSASVPRRNT
     KKTSLSFSSD ESEAYTTDDD DNKTSIELEK DFYKIDLDGL SKEKSANFLE PEENLNVNTA
     IKSKKRLSTL TSKVMTQPWN GIDGYNVNSQ SLPDLSKAEG RDLIPFISST ESETSLLYHN
     NSISNDLQKN IPRQQKFSPG FDNVYLTKLL QVNYAKNETQ FIMALQNISI RLSQVPKEAR
     LSALRAELSI INDTLLPSEI DIPQLLPITS NRNKKYHKIL KLNVNEASVL NSAERVPFLL
     FIEYLSDEID FNPTTEYNQR IIARKKMNGA TSMTVKKINS FSEVADGNFE KENKIKSSTP
     ETVSNIIYNE NTEEADLSEM PLDRKTTVSS DSFSPEMLVT PSITEQSKLS NFPSLNTKEV
     STKVLADQMR IAAVMLQQLD SSGKANSEQS FLIKNRIVES MIALQDQFDS FDFEKLSQLQ
     SDEPSAGERK LENDFKLGED WNTKKQRIKK SSAYGHLKNW DLCSVIAKNG DDLPQEAFAC
     QLISMISNIW KKNNIPVWTK RMKILITSAN TGLVETITNA MSIHSIKKSF TEHSIKSGEN
     SKGKIFTLLD YFHSVFGSPN STSFRTAQQN FAKSLAAYSI ICYVLQIKDR HNGNIMVDGD
     GHIIHIDFGF LLSNSPGSVG FEAAPFKLTV EYVELLGGVD SEIYSQFVYL CKQCFKSLRD
     NSEEIIEIVE LMQKDSTLPC FNNGENTSVL LKQRLQLQLN DEDTDQFVEN FLIGKSLGSM
     YTRLYDQFQM ITQGIYS