ID A0A0V1I450_9BILA Unreviewed; 966 AA.
AC A0A0V1I450;
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 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 Name=pik3c3 {ECO:0000313|EMBL:KRZ17672.1};
GN ORFNames=T11_14565 {ECO:0000313|EMBL:KRZ17672.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ17672.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ17672.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ17672.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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, 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:KRZ17672.1}.
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DR EMBL; JYDP01000006; KRZ17672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1I450; -.
DR STRING; 268475.A0A0V1I450; -.
DR Proteomes; UP000055024; 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; 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; 2.
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; 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:UP000055024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 55..241
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 325..575
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 683..950
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 472..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 110458 MW; 969FDF8A6A917A42 CRC64;
MYDSCDGQEK QRSNNFHIEI ILDCHKTTLK LMLHLFMAPN TITSDRVNYV YSCDVHKPVK
FKIGCLEGLL PRFSLNDILR DPSAVDCLAL QEECQPNIYV ECQLYCLGKP VGLPIVTSSK
YFTTFYCWDE WITLPIKYSE LSRDAQLAFT IVDVHSNMKR HVIGGTSISL FSKRGILRRR
QYDLKVWPFQ SGDGTAANRT PGKLKVGAGC CSETVRLMKR SKRYFSGLME KVDWLDRITF
RQIERVCAQE KSLGKDLFLL VDFPVFHFGG NDFCMVYFEA DMDNSKLFNR CPTLTRFVDL
SLDLENVCEL KNYLLARSTR SVMADRDIKP NPTTRDQLAR VVNYPPNCEL NNEDKALIWK
FRHYLKSNGR ALVKFLQCVQ WQSPAELAQA EELLHEWAPM SVADTLELLS SKFQQPLVRE
YAVGRIRDSS PDVVHTYLMQ LVQALKFEEQ ERIRAGTDPT FVQNIQNQAP LQSNLATGDD
GPAPQSCSNR TTSVERSSEP SDKEMDSGVG CAQSEQLHPE NDGTDLASFL IRVACKDPTL
ANHLYWHLKT ERDCLHLEII SRESGGKASD KGSPATDEKQ QQLEWKLRAY RKLYSTMVDR
LLKALARGGT EAKRRRKLIK RQEQFVAHLL DIMGRVMRDS GPRNQKLAHL KKLLAAEDER
FNLHNMGGLP LPLDPGVKLQ SIVAEKATMF NSAMSPAKLT FKTIDGEEYT TIFKYGDDLR
QDQLVLQTIS LMDELLRREN LDLKLTPYKV IATGSSHGFV QFKESITLRE VVHKYGTIQE
FLRCQKPATE DALYGVHPEI MDNYVRSCAG YSVITFLLGV GDRHLHNLML CKNGCLFHID
FGYILGRDPK PLPPPIKLTK EMVEAMGGLR SIYWREFVKF MYTAFLLLRR HVNLFVNIFA
LMVQSSLPDI ASEPEKAVSK LQDRFFLRLS DEEAVYHLQH MIEVSINAKM AAIVDLMHDI
AQFLRK
//
