ID Q4QAC9_LEIMA Unreviewed; 1089 AA.
AC Q4QAC9;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=phosphatidylinositol 3-kinase {ECO:0000256|ARBA:ARBA00012073};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
GN ORFNames=LMJF_24_2010 {ECO:0000313|EMBL:CAJ05324.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ05324.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ05324.1, 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:CAJ05324.1, 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. {ECO:0000256|PROSITE-
CC ProRule:PRU00880}.
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DR EMBL; FR796420; CAJ05324.1; -; Genomic_DNA.
DR RefSeq; XP_001683719.1; XM_001683667.1.
DR AlphaFoldDB; Q4QAC9; -.
DR STRING; 5664.Q4QAC9; -.
DR EnsemblProtists; CAJ05324; CAJ05324; LMJF_24_2010.
DR GeneID; 5652375; -.
DR KEGG; lma:LMJF_24_2010; -.
DR VEuPathDB; TriTrypDB:LmjF.24.2010; -.
DR VEuPathDB; TriTrypDB:LMJFC_240029000; -.
DR VEuPathDB; TriTrypDB:LMJLV39_240027800; -.
DR VEuPathDB; TriTrypDB:LMJSD75_240027100; -.
DR eggNOG; KOG0906; Eukaryota.
DR HOGENOM; CLU_004869_0_0_1; -.
DR InParanoid; Q4QAC9; -.
DR OMA; CVITFVL; -.
DR Proteomes; UP000000542; Chromosome 24.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; ISO:GeneDB.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISO:GeneDB.
DR GO; GO:0036092; P:phosphatidylinositol-3-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; cd00896; PI3Kc_III; 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; IPR035892; C2_domain_sf.
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; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR008290; PI3K_Vps34.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 4.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51547; C2_PI3K; 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:CAJ05324.1}.
FT DOMAIN 53..229
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 335..533
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 799..1073
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 612..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1089 AA; 119074 MW; D0BE1F3303108FB5 CRC64;
MTSTSAALIA SVLRQPRVGD DLQWMRYDAL FRTAQDYAAA EYLYRLRLCS LRLRSSLLSP
SLPCTDLVSE VAHLLPHYPV QITAQLVYMD EPLSPVVESA AVYASAAALL PSASPVGGDA
DTHAEMEVVY TFADEWLVFP LELCDVPLDA SCKLHLWHRD TRVAEAAFHV YSVAGELCVG
QRQLALSTGG GAPSDEQLWS TSTHAAELLA DFHRGMMPSI PWLDTLSIQQ LEAEHARHGN
AVVRKGSSQS AKDPCGAQTA ILTLYLPAAT TAVFFEPGVA RVSDDMKSLL QCGDAADNPC
DFTQRPFPDQ YTFFKEHNLC EAKAAITSKT QYFLSDSSAP PGPKERHQLA SLLRRPPIQL
DNVTGAVVTG AGAGGVGGVR LEETRLLWKY RHFICRDGKY FLPFMRCVDW ANTHSSERRA
ACALIHQWAR PAFEDVLACL SFYFDHVAPV RQYAVRLLRR EGDGRLCQLA FQLVQAVRYD
SAEAELANFL VERAVGCWEL CSTLHTLLSV EVALEKCRTS SAAGKASDDR HGGTTLFKPL
LRRLSERLTQ QCPHFVKRLR QQHAVHRVLQ LLSRQLQQSS LDRLGKTALG NKLIAKQACG
LRALFSSVHH GMPSRRNVNG SFGSSLMAHS SADVREEHSM SSARTGDSSE EADANGGDGV
SAVEASDVDS AAEDDVRRLR FPLLSPQSQG SAPQSSPSQS GAQQQCRSRH AAAVDVLDRY
GVTTLATHPG IPITGLLPDS LYIFKSAKLP MRLTFTALRP AGLAWGGGRG GEPLHGASPS
PCVWTPLAMQ PAPSQQRSGG LQGMNSSGGG ASTAVAAEEQ AEGFLGAGEG DTVPLAMMYK
YNDDIRQDQL IVQLIRLMND LLQQDGMQLY LTPYRVIATG PNEGLVEIVP QVTTFFSVQR
DVLKYLRVYN NTAELLRQAM DRYTRSFAGY CVITFVLGIG DRHLENILIT QDGRLLHIDF
GYVLGNDPKP FPPPMKINRE MVEVLGGPQS TGFTEFKLYC CSAYNTLRKH APLLLHILLL
GAHTEGMPQV TGEGGDPRVN LLKVQEKLRL DLTNAQATQY LQNVIADSVG SIFTNLWDVL
HAAAQATRG
//
