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Database: UniProt
Entry: E9AE04_LEIMA
LinkDB: E9AE04_LEIMA
Original site: E9AE04_LEIMA 
ID   E9AE04_LEIMA            Unreviewed;      2662 AA.
AC   E9AE04;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN   ORFNames=LMJF_29_1450 {ECO:0000313|EMBL:CBZ12483.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CBZ12483.1, ECO:0000313|Proteomes:UP000000542};
RN   [1] {ECO:0000313|EMBL:CBZ12483.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(2005).
RN   [2] {ECO:0000313|EMBL:CBZ12483.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   EMBL; FR796425; CBZ12483.1; -; Genomic_DNA.
DR   RefSeq; XP_003722225.1; XM_003722177.1.
DR   STRING; 5664.E9AE04; -.
DR   EnsemblProtists; CBZ12483; CBZ12483; LMJF_29_1450.
DR   GeneID; 12981006; -.
DR   KEGG; lma:LMJF_29_1450; -.
DR   VEuPathDB; TriTrypDB:LmjF.29.1450; -.
DR   VEuPathDB; TriTrypDB:LMJFC_290022700; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_290021300; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_290021800; -.
DR   eggNOG; KOG0902; Eukaryota.
DR   HOGENOM; CLU_230048_0_0_1; -.
DR   InParanoid; E9AE04; -.
DR   OMA; VKACIFK; -.
DR   Proteomes; UP000000542; Chromosome 29.
DR   GO; GO:0020016; C:ciliary pocket; ISO:GeneDB.
DR   GO; GO:0005737; C:cytoplasm; ISO:GeneDB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IBA:GO_Central.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBZ12483.1}.
FT   DOMAIN          2074..2256
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          2360..2646
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          60..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..630
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..896
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2662 AA;  290632 MW;  476E4F94D257CB28 CRC64;
     MNDIRLPCWI KSSPTLVMAS ALAQLLTDEL AETTSSATAG APRPPSEVCV LGGRERWPRH
     NFDEDISSSS SDDGGGVNLS DSAASECEGC YDSGRDAMRT GGGVGTGYLR MVDRLLELNS
     KELDSLPPPG ATATAATYSP PKAVTAPATP MPTAIAGSWH RGSAVLFTGQ NGGASMSTLG
     ASPDILRDPR VRTLLRLSRL NDVLTRAETA QRLISRRTAA AMVSFFAFAV SCRYSGLPVD
     RTKGFFTECS ALYTTLLSKL RSLRFGGGVN LEDFTASLVA CGLKLRDDED VEGDEKDGRG
     GTNEAGATGA VTAGISCSGR SNSSSAVASG AAAMGSCGGA GVRTPMQLSF GRDKNWGLVG
     FGHRALDAIF VRCIPSNIDE CVHDPVALGV LRGISLTHSQ QLFYLGPELV NHLHDLTDAF
     ATSGHRRALP YKRVLSVLLE AISCSRVIDY ERTNNWITAV IQERYVVRGL FQREELHAHI
     VTATLTMLIR QYQEMAKECA SKVVDLGSMP DFTEGDQLIE LVWKALQDTI GSWEDAVATA
     EKHPLTLFRH NIDIVVQHLL RTEVERLRCY YIITSATAAY HQSLVGMSAG TRTTGNQSGC
     PPAVPQLAPG REEQRGANRR GRDTLRGQDG STRRHSGAPA AAPYVPSAEE ESLRISICSN
     IIKLLLLPTS IMSALPRTEE AKQLRASLTE AAARVLSVVT AKEFNSRDDT SVMTTASGRA
     ATSAAPRSVS PISAAAATPR IRHADAGAAG TDLLAISRRQ AHFSNNFYRC VEELIHELIH
     TILQQSVPDD ATAVANRSVL GGVSDARLST PSTSDTNSDA ILRGMVAAVC IQYMCFTNQH
     LRSFAISEVM DAVVRLSARC GAEEAATATH GSLERKSSSK TARASGSDSN ESPAAAPQGT
     VVGAAAAAAD PEEKRKLATH VRARQLALCF DALSAILVPT VVVEGYHHVA EEQEERAGLA
     RSCTTTSARG NSKREELSRY GQLLCDTYVD SLREHLWGLG EGSVSHHKML TPVMAVAVKA
     FVNLVLRVHE RLRGMSSMAL ALVQEAEAAM EGSKKGTQRS AAAIARDRAR LLHAFNAERM
     SVVLLLRGVI QNMLSVAWPS SGVLYQDRAC SWERPLNNKT ASAVMAPIAL AVLSPFFRPL
     AMLLHLSTLF PARSLRQLCT HYQYARYLTL EDPSTSDQYV FYYYRRLSRA LVAVEVDDSG
     GSGAGSAEQI EFECWALFRS CWMMFSYYKY TAEALMAVRA GGMAPMESAN PATATAALAR
     APILSTKQCK LLCLIAASAA PLLRMCSSDV QQAMADIAVL LRYTLAGALH CPMVVADVTA
     KSGIVHASLY KSLKRLCGGR KECWKRLSTG ELMLLQCVAE LEILRAAAGS VAQLTLYRHF
     EVREFVASAA IPEALGHILS TACDHYIEAV RSMLPGVAFQ VTRTDLMQLV FLVSFAIGSV
     RESASKLLLC VVRSFPTYAA YASALPLLWC MLDLLEAGTA WQIESLCEHV RFPAVPAVAA
     DPHSVERQQH VLFVADVAKR WAAILQDEAP IALFETAIKF MVVQQQECGE QATTQAGRHH
     AGSRLAALAS QYRVEEAPPN LDDSAITVMR GAGAAGHVVK TEYAQTLLLH GRAQGAMQAS
     SWYASAEQMH STVVAQLWAA TRLCRRDLAS AVAQRLESNL LRPARALFVE TGYSVGTVLA
     PRAFTVADED AAAREEVGVT SVPLGAPARA ETAASFAAAV ALLAKGSGTP IVRRQLLQYL
     VQGAVQTFRS DVLYEAILCW KWLLSQNREA YLLPMLQELD TAFVWTAANR LGLFDGYCSS
     KNRQVQTGEV PIPHNTVSAR GQKGAGVPEE AAVYVADNVD SASPHKLLFS FLTDMYVEEG
     SPLCLSPEVL RQLYLVAAHI MQFAKVLSLR DDMFGETMRC FLVVGSIAQL LREANVRQLR
     AGLLTIVPFP AIGALRERWY KALLRWFTKM PPSWYYAKDP VLAREEAKVV SSLSQLLKEE
     ADLLTRTTLG FLDFSSGVQR ERGMPLVHHW ESLSVVRESV AAVRQAADGG EAGLRKLIAR
     EKLRLQGLLH LLRVLVEHEA LRLSVWRTPR RTLKIPNTTP SVGWAKLIEC ADHHNPAVVV
     SMVYRFSSIP AVRLAASQRV VAHPERYSNV AEAVDLYLTE DVLRAGAPRL FLFCSCTIIQ
     ALRLLDPRYA AYKAVNSYAI CSLLSQRSEN LIFYLPQLLQ LLATDESGSI EAFLVRMSAK
     STMFAHQLLW SLQTESEGSG ALAKKCQQVE RRVKAVFTPN EEAFYKSEFA FVDLMTSVSG
     EIMKFDKTER KAQLRLRLKD DIFHALPKLR HLYLPTDPNY RITDVIPHTA GAMQSAAKCP
     ILVQFTCVPR TAEDTLTPDD VDSAAADEHG HGAMNSHGSA VSRQVVKACI FKMGDDCRQD
     QISLQLIGLM QRILNSIGVP SFLYPYRVIT TGKSSGVIEC VPRSRSRNEI GKLVESNVAE
     FFVQTFGHPE SAGFRRAREN FVRSTAAYSV VSFILNIKDR HNGNIMIDAD GNLVHIDFGF
     LFDTSPGGDI NFESSPFKLT TEMVQLIGMD VSGESTLQSK TLARALVDEE NYIYFKTLVN
     RCYLAVRQYA REICVMVELM LRSGLPCFKP KKTIADLAQR LAVDKNEIEA ADYMRRLIHE
     SRQNFRTVLY DYYQKVAEGI EM
//
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