ID   A0A3Q0RFM4_AMPCI        Unreviewed;       975 AA.
AC   A0A3Q0RFM4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Si:rp71-17i16.5 {ECO:0000313|Ensembl:ENSACIP00000008648.1};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000008648.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000008648.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   Ensembl; ENSACIT00000008907.1; ENSACIP00000008648.1; ENSACIG00000006322.1.
DR   GeneTree; ENSGT00940000165924; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.770; -; 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; IPR000341; PI3K_Ras-bd_dom.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR045580; PIK3CG_ABD.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10048:SF99; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT GAMMA ISOFORM; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF00794; PI3K_rbd; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   Pfam; PF19710; PIK3CG_ABD; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00144; PI3K_rbd; 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   SUPFAM; SSF54236; Ubiquitin-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; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          167..255
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          303..458
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          489..668
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          680..960
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          466..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   975 AA;  111816 MW;  50DE0E08DFD1B8A0 CRC64;
     MALNTEMKST KSKRAEWRAV ASSVDLLAQE QNCHPDPFAI LDPEKYTLLY ARGGDWYEAY
     DDCQVIRTLD IPWSHDDPRC LTARILVKPP VAVDPEEKEK QRQCLTYLIG HDLEKEASDR
     LGELTFTRRK LAAPRKQELK NRDNKLYATE PWITYASLPD DLQEWLNRDL PVTFHYMSRI
     SFSIKAELST TPELLLQVFE RVAKAQGVKC ESFDDLVLKV TGREEFLSGD YTLCDFLWVR
     QCLRXNQELH LSVVPMSQLA SEAVKFVDWP LVDGFSGXFS SHDDLRLXGK DLDDIFMISL
     WDCRRNFRVK LLGIDIPQLP SKCPQSVYVE ASILYGNKVL SSVCSFPKAF ADEVLWNEWL
     DFDFLLRDLP RGAKLGLTIN EMPDMQKGKG NVLYFVNLLL IDHRSVLSQG PHTLHMWSHP
     GLDDEAITYQ ADKLSSATNP DIADSMAISF LLDRYSFPVV VPNTISHSEC SDSPTPTKSE
     PQESCRTVPP PLPIKKSYLQ AKLPETVTLR SPSPTSDTRT AGLRRFREES IRYSSSLPHY
     LRSVDWMSRR VVEDVHWLLG NWNPEELDLT VALELLSMDY ADEIARRLAV QRLESLSNDD
     VLKYLLQLVQ TLKVEPYHDS FLARFLIQRA LRSKRIGHFF FWYVRSEVAG CPYFRQRMAV
     ILEAYLLGCG QAMLDSFTQQ VQAVEALRDA AVAIKXLYPD KTNLDSTSRK HHFSELICHN
     HIKICIMLVL MDSIWQEKSL DLNLIPYGCI STGQNIGMIE IVRNATTIAA VQRSLGGTTG
     AFKNNVLFEW LKSKCPLQEI HFKTVDRFVK SCAGYCVATY VLGIGDRHND NIMITEDGNL
     FHIDFGHILG NRKRFLGVSR ERAPFVLTPD FLYVMGRVSG RNRLYYQWFK DTCIKAYLSL
     RAHSHLLVTL FSLMMLTGIP ELSAAEDMRY LRVALQEEQS EADAREHFLQ QISECEKLGW
     SVQFNFWIHE NFGIK
//