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Database: UniProt
Entry: Q64HK9_CANDU
LinkDB: Q64HK9_CANDU
Original site: Q64HK9_CANDU 
ID   Q64HK9_CANDU            Unreviewed;       977 AA.
AC   Q64HK9;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
OS   Candida dubliniensis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=42374 {ECO:0000313|EMBL:AAU13915.1};
RN   [1] {ECO:0000313|EMBL:AAU13915.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=D1558 {ECO:0000313|EMBL:AAU13915.1};
RX   PubMed=15302834; DOI=10.1128/EC.3.4.1015-1027.2004;
RA   Pujol C., Daniels K.J., Lockhart S.R., Srikantha T., Radke J.B., Geiger J.,
RA   Soll D.R.;
RT   "The closely related species Candida albicans and Candida dubliniensis can
RT   mate.";
RL   Eukaryot. Cell 3:1015-1027(2004).
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; Evidence={ECO:0000256|ARBA:ARBA00001686};
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   EMBL; AY622606; AAU13915.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:CD36_51560; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05168; PI4Kc_III_beta; 1.
DR   Gene3D; 6.10.140.1260; -; 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; 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; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR049160; PI4KB-PIK1_PIK.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR   Pfam; PF11522; Pik1; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..125
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          679..960
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   977 AA;  110360 MW;  98EC3128B0F668DF CRC64;
     MSENTPEAPS KQLLERIQSS SFSLFNCIYE LKNHNDSIGI QHELVKKLYS FPYEDLQFFI
     PQFVQLLVTY DSNSMALEEF IITSSCRYPH FSLIVFWNLQ AYIFELKNEP ESRSFQAARN
     LVTKIQNIMF NTELSVVKAP EFRENLFPAL VLCGAVASSA LLPSFKNYCL PMIKAQGKQQ
     KSLVFKLANF QKSLTKNLTL KNQRMSADIP KESHSDDETV VSSSIKPSLS RSASVPRRST
     KKASLSFSSD ESEAYTTDDD DNKTSIELEK EFYKMDLNGS LKGGSTKFLE TEENLHVNTA
     IKSKKRLSTL TSKVMASSWD SMDGYNVNSQ SLPDLSKADS RDLIPFLSST ESETSLLYNN
     NAIANDLQKX TLQQPKFMPG FDNDYLTKIL QVNYAKNETQ FIMALQNISI RLSQVPKEAR
     LSALRAELSI INDTLLPSEI DIPQLLPVTS NRNKKYHKIL KLNVNEASVL NSAERVPFLL
     FIEYLSDEID FNPTTEYNQR IIARKNIVGA TNTSVKKMNS FSEVPDGNFS KENNLESHIT
     ETVTSAICNE STEEADLSEM PIARRTAVSS DSFSPEMLVT PTVTEQSKLS GFPSLNSKEV
     STKVLADQMR IAAVMLQQLD SSGKANSEQS FLIKNRIVES MIALQDQFDS FDFEKLSQLQ
     SDQPSAGERK LENDFKLGED WNTKKQRIKK SSAYGHLKNW DLCSVIAKNG DDLPQEAFAC
     QLISMISNIW KKNQVPVWTK RMKILITSAN TGLVETITNA MSIHSIKKSF TEHSIKSGEN
     DKGKIFTLLD YFHSVFGSEN SVSFRTAQQN FAKSLAAYSI ICYVLQIKDR HNGNIMVDRD
     GHIIHIDFGF LLSNSPGSVG FEAAPFKLTV EYVELLGGVD SEIYSQFVHL CKQCFKSLRD
     NSEEIIEIVE LMQRDSTLPC FNNGENTSVL LRQRLQLQLN DEDTDQFVEN FLIGKSLGSM
     YTRLYDQFQM ITQGIYS
//
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