ID A0A0V0QGP0_PSEPJ Unreviewed; 818 AA.
AC A0A0V0QGP0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=phosphatidylinositol 3-kinase {ECO:0000256|ARBA:ARBA00012073};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
GN ORFNames=PPERSA_01254 {ECO:0000313|EMBL:KRX01351.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX01351.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX01351.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX01351.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE-ProRule:PRU00880}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX01351.1}.
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DR EMBL; LDAU01000170; KRX01351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QGP0; -.
DR EnsemblProtists; KRX01351; KRX01351; PPERSA_01254.
DR InParanoid; A0A0V0QGP0; -.
DR OMA; LIPRWES; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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 ATP-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 29..177
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 247..446
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 499..802
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT COILED 470..497
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 818 AA; 95570 MW; 0A4309D1D98280B7 CRC64;
MEDNIYLKGQ YIPHHSLDQL KIKFQLVQLR DEKKSLAQYL DNFVSQSDTY ANLYVEAQLI
NNLELINPPQ QHQLGKKLLI QEDIIFNFYY KDLSYNSLIA ITLWTTNKKY SKNKPLGSTT
ITLFDSDLKL RQGKFHLYIW PETQPDISYN SKTCGLIQDE NIQEIKNTVQ KIGYYLNKTS
ATEHENQIIN SLNLKLHYTS QKVPAAFLEI EFPKFPIPIL YEDKRQDKDD FIQTLSFPPR
GKIQVQNTTL ADCIVSSDFD FENNFNDPAQ EQFNLLDVDE NNAKDLKPSV QQDQENKDAL
IYFLNSIQWT NAREKEECRN LLQQWSPCDY WDAVHLLSAF FCANDIYNKE ASKPFEDMME
IRRYAVDQLK KIPQHNVNFI LLQLVQALRY ENLDSVQSSP LAQFLIELGT QNIHIASQLL
WILNVETDVI NVKDNKQAKQ SKEEQERINQ WYNLILLDFQ ESIKIKNPQI NQILKNQKEY
RDILKELSQQ MKKEGKEPVP EQTLVFKSAM APLKTTWKVK NQDTNEEQKL EFIYKTGDDL
RLDQLILQVF QFMENIFKDI NLDFKLTPYK VLACSKSDGF MEFVPDTVTL QSITTDQKKY
KHTLVTFFEK ISNDPNLKYH KDMQNQANVV KNTEITKSQK QKDDSKQNPL IHKEVMENYI
LSCAGYCVIT YILGIGDRHL ENIMMQNTGK MLHIDFGFIL GQDPKRGSSP LKLTADMVNG
MGGKLSNNYQ IFKLKCVNTY KYLRKYCKAI VTLFYLMIDS GMPFINKTAI EKMSQKFCLE
ETDGNAERHF LNILEESENS LMDRVNDKFH IYAGLIKN
//
