ID H2AZ42_KAZAF Unreviewed; 874 AA.
AC H2AZ42;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Phosphatidylinositol 3-kinase VPS34 {ECO:0000256|ARBA:ARBA00041128, ECO:0000256|PIRNR:PIRNR000587};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073, ECO:0000256|PIRNR:PIRNR000587};
GN Name=KAFR0H01890 {ECO:0000313|EMBL:CCF59598.1};
GN ORFNames=KAFR_0H01890 {ECO:0000313|EMBL:CCF59598.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF59598.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF59598.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; HE650828; CCF59598.1; -; Genomic_DNA.
DR RefSeq; XP_003958733.1; XM_003958684.1.
DR AlphaFoldDB; H2AZ42; -.
DR STRING; 1071382.H2AZ42; -.
DR GeneID; 13887594; -.
DR KEGG; kaf:KAFR_0H01890; -.
DR eggNOG; KOG0906; Eukaryota.
DR HOGENOM; CLU_004869_0_0_1; -.
DR InParanoid; H2AZ42; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000005220; Chromosome 8.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08397; C2_PI3K_class_III; 1.
DR CDD; cd00870; PI3Ka_III; 1.
DR CDD; cd00896; PI3Kc_III; 1.
DR Gene3D; 2.60.40.150; C2 domain; 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; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 1.
DR SMART; SM00142; PI3K_C2; 1.
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 ATP-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 14..186
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 292..525
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 592..858
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 874 AA; 101285 MW; 4D009F66E8EE9A74 CRC64;
MSVNNVTFCL SQELDIPLRV KLRSLEGVKQ LSKPSEKILN PKLTQVESNL YHNSNFLVSV
QVFDNERHRN LTLPVFTPYI PFKNSRKWDY WVTLPIMIKQ LTLSSRLRII LWEYNGMKKV
AFYKLETCIF NYNDCSLKRG YESLKFDYEV PNTVTSIEDD EVQENLNKYL QGEIKKIDWL
DDITFKKLVE EREKRTWPRN TFVLNIEFPV FELLVIYTER MDENVQKNIS TLHNFESVTD
MTEHSKTSPD IKISLGDKYT STLKFYDPDQ FNSDPIEEKY RRLERTSKQS DLDKQVKPDT
KKRKYLNKII NYPPGTALTA HEKGSIWKYR YFLMTNKKAL TKLLRSTNLS EETERNEVLE
LMDSWAEIDI DDAIELLGPD FTNLSVRSYA VNRLKKASDK DLELYLLQLV QAVCFENLSV
LNDKTNSEFQ IVNTPASPNV VNSTMIQRYQ KLERSVQSSE DGQINDMTME ETTIVISPLA
EFLIKRALKN PRLGNFFYWY LKSECEDRPY LKQILDSFLD RLPSGQKVTL FEQIEFVTLL
SRCSEEIKKS KDTTTKKIEL LHSLLTTKIR HMLKNKPIPL PLNPDIFVCD ASPEQSTVFK
SSLSPLMISF KTTDNLPYQL MYKVGDDLRQ DQLVIQIIRL MDELLKSENV DLKLSPYLTL
ATGIQEGAIQ FVPSSTLASI LSNYHGILFY LKAHFPDDSQ ELGVQDLVME NFVKSCAGYS
VITYILGVGD RHLDNLLLTP DGHFFHADFG YILGQDPKPF PPLMKLPPQI IEAFGGAESS
NYDKFRSYCF VAYSILRRNA GLILNLFELM KQSNIPDIRV DPDGAILKVK ERFNLDISEE
EAIIHFQTLI NDSVNALLPI VIDRLHNLAQ YWRA
//
