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Database: UniProt
Entry: I1C1Q3_RHIO9
LinkDB: I1C1Q3_RHIO9
Original site: I1C1Q3_RHIO9 
ID   I1C1Q3_RHIO9            Unreviewed;       684 AA.
AC   I1C1Q3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Phosphatidylinositol 3-kinase VPS34 {ECO:0000256|PIRNR:PIRNR000587};
DE            EC=2.7.1.137 {ECO:0000256|PIRNR:PIRNR000587};
GN   ORFNames=RO3G_07088 {ECO:0000313|EMBL:EIE82383.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE82383.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE82383.1, ECO:0000313|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000313|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
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|PIRNR:PIRNR000587};
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   EMBL; CH476736; EIE82383.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1C1Q3; -.
DR   STRING; 246409.I1C1Q3; -.
DR   VEuPathDB; FungiDB:RO3G_07088; -.
DR   eggNOG; KOG0906; Eukaryota.
DR   InParanoid; I1C1Q3; -.
DR   OMA; LHKFAQY; -.
DR   OrthoDB; 10350at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
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; cd00870; PI3Ka_III; 1.
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; 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; 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; 2.
DR   SMART; SM00145; PI3Ka; 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   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:UP000009138};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT   DOMAIN          142..323
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          399..668
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   684 AA;  79006 MW;  7BBE6107F10B6D0C CRC64;
     MFGLMLKQME NKVQQHQLVK RYDCGDIRPV EWLDNLAFRQ IEKIHKEVSA NLTELALYVD
     LPKFDFPVVY GEMEYKLPDP FIEDASITEQ QQLVTAMNGT IHSELSDTTN YSLVLDPDLH
     RDNPVEAKHR RLVRSHRSGP LDRDLKPNPK IRDELNSIMS YPPTQTLTSE EKDLIWKFRF
     YLTRDKRALT KFLKCVVWTD ATEVRQAVDL LPLWVDIDVD DALELLGKEF QNRSVRSYAV
     NQLKKADDDD LLLYLLQLVQ ALKFEHYNDK GVDNDSSLER FLINRSHNNP VLGNYFHWYV
     MVECEDPAVH KMYAKVTYDY FNALMEVQGG HIRRGELREQ GTLIQKLSQV STEIRSMKEA
     RAKKVERLRA VLADPKGQLH SFPALPLPLD PTKKVCGIIP EKSGVFNSNL QPLRITFVCE
     DKSEYPIIFK TGDDLRQDQL VIQIILLMDK LMQKENLDLK LTPYKVLATG SEHGLMQFIP
     SMSLAGVLNE HQNNLLSFFR QHHPSSEPGN VYGIDPRVME TYIRSCAGYC VITYLLGVGD
     RHLDNLLLSP DGHLFHVDFG FILGRDPKPF PPPMKLCKEM IEAMGGANSP YYMNFQQYCY
     TAFTTLRRNA NLILNLFALM VDANIPDIKI EPDKAVLKVQ EKFRLDLSEE AAISYFRGLI
     SESVNALFPQ IMETVHKWAQ YWRR
//
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