ID A0A095ATT0_SCHHA Unreviewed; 816 AA.
AC A0A095ATT0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3 {ECO:0000256|ARBA:ARBA00019787, ECO:0000256|PIRNR:PIRNR000587};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073, ECO:0000256|PIRNR:PIRNR000587};
GN ORFNames=MS3_06240 {ECO:0000313|EMBL:KGB37876.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB37876.1};
RN [1] {ECO:0000313|EMBL:KGB37876.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
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.
CC {ECO:0000256|PIRNR:PIRNR000587}.
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DR EMBL; KL250940; KGB37876.1; -; Genomic_DNA.
DR RefSeq; XP_012797637.1; XM_012942183.1.
DR AlphaFoldDB; A0A095ATT0; -.
DR STRING; 6185.A0A095ATT0; -.
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; 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; 1.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 182..450
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 529..794
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 322..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 94644 MW; 9E929093AA7942F7 CRC64;
MTNDTSVDLF SRFNEAFDLP LPYNALYDYN GICFVLSSTY TDKKGMHEQL IAGANMKLYN
SKKVLNKKKV IESFDGSSKK MISILIDLFL TNRKHLRNEL LETPLDRHCM PDVEHAVDEA
KRASGRLFLS VKFEFSRSYP SVYMPVIFQR PFLPEQSELR ADRWNPVDEK YFKMTRNART
ADVDRARKPN KDILDRLKLV LDLPPGLNIS ESDGDLIWKY RFYLADKFPE TSLAKFILSV
RWEYTEQVNQ AVELLKQWPK IAPEHVLELF TRQFLHPAGR RFAVHRLEAA SDEELILYLY
QLVQALRYEN WHDIFSVQPK RNDRTSKRNV SDVTKEGNSQ EVKSTNLTSN RKMPSSFRTG
RGGALQNIER SREELIGWHS DLKKEWKEDL ASFLIRRAQL NFRIANYLYW FLRLEANSND
GEDDFWERDR VNPPDTQKMY KHVLNRLLHA FDAGSPTCQK WNIELLQQTQ FIQDLCRLLK
SVTNDLGNRS RKIELLRSKL DSEEYAHIRH IDKPFPLPLN PDIIVCGVQS STATLFKSFQ
RPALLTFIQP NGDTYRAILK HGDDLRQDQL VLQMIELMDV ILRKENFDLR LTPYKVLATS
NRHGLVQFVE SISLADILHR STLLAYLQLK APSPNSPMGV QKDVMETYIR SCAGYCVITY
LLGVGDRHME NLLLTADGHL FHIDFSFILG ADPKPMAPEV RLTRAMIDGM GGPNSNQFNE
FWKITFTAFL ILRRHANLFL TLFSLMSNTG IQSFNGQQNN ASEFLKEHFC VHQSEEKAVS
RLANRMTESI KAIVPDIMER IHTIVQVNNF YYVGNS
//
