ID   A0A3Q3W0P5_MOLML        Unreviewed;       946 AA.
AC   A0A3Q3W0P5;
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=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMOP00000001904.1};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000001904.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000001904.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   AlphaFoldDB; A0A3Q3W0P5; -.
DR   STRING; 94237.ENSMMOP00000001904; -.
DR   Ensembl; ENSMMOT00000001939.1; ENSMMOP00000001904.1; ENSMMOG00000001597.1.
DR   OMA; SKSLWTI; -.
DR   Proteomes; UP000261620; 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   CDD; cd08398; C2_PI3K_class_I_alpha; 1.
DR   CDD; cd00872; PI3Ka_I; 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; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10048:SF107; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT ALPHA 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   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; PS00915; PI3_4_KINASE_1; 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   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          65..167
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          208..365
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          395..572
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          643..929
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   946 AA;  110079 MW;  A97E557198E67F68 CRC64;
     MPVCEFDLVK DPEVQDFRRN ILNVCKDSVE LRDANGPHSR ALYVYPPNVE SSQELPKHIN
     SKLDKGQIIV VIWVIVSPNN DKQKYTLKIN HDCVPEQVIA EAIRKKTRSM LLSPEQLKMC
     VQEYQGKYIL KVCGCDEYLL EKYPISQYKY IRSCIMLGRM PNLMLMAKDS LYTQLPTDNF
     VMPSYSRRIS TATSYMNGEA AAKPLWTING TLRIRILCAT YVNVNIRDID KIYVRTGIYH
     GGEQMCDNVN TQRVPCSNPR WNEWLTYDMY IPDIPRAARL CLSICSVKGR KGAKEEHCPL
     AWGNINLFDY THTLVANKMA LNLWPVPHGL EDLLNAIGVT GSNPNKETPC LELEFDHFSS
     SVKYPDMNAV EDHANWTISR ELGFNYALSG QSNRVARDHA LTESDTEQLR QLSNRDPLSE
     ITEQEKDFLW RHRHYCMNIP EILPKILLAV KWNSRDEVAQ MYCLLKEWPS IRPEQAMELL
     DCNYPDPMVR RFAVRCLDKY LTDDKLSQYL IQLVQVLKYE QYLDNPLARF LLKKALTNQR
     IGHFFFWHLK SEMHNKTVSQ RFGLLLESYC RACGMYLKHL SRQVEAMEKL INLTDILKQE
     KKDETQKVQM RFLVDQMKRP DYMDALQNFT SPLNPAHQLG NLRLDECRIM SSAKRPLWLN
     WENPDIMSEL LFQNNEIIFK NGDDLRQDML TLQIIKIMEN IWQNQGLDLR MLPYGCLSLG
     DCVGLIEVVR SSHTIMQIQC KGGLKGALQF NSNTLHQWLK DKNKGEMYDM AVDLFTRSCA
     GYCVATFILG IGDRHNSNIM VKDDGQLFHI DFGHFLDHKK KKFGYKRERV PFVLTQDFLI
     VISKGSQECA KTKEFERFQE MCYKAYLAIR QHANLFINLF SMMLGSGMPE LQSFDDIAYI
     RKTLALEKTE QEALDYFMKQ MNDAHHGGWT TKMDWIFHTI RQHALN
//