ID A0A087X5A9_POEFO Unreviewed; 1070 AA.
AC A0A087X5A9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Si:rp71-17i16.5 {ECO:0000313|Ensembl:ENSPFOP00000000962.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000000962.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000000962.2}
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 EMBL; AYCK01026769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01026770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01026771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087X5A9; -.
DR STRING; 48698.ENSPFOP00000000962; -.
DR Ensembl; ENSPFOT00000000964.2; ENSPFOP00000000962.2; ENSPFOG00000000898.2.
DR eggNOG; KOG0904; Eukaryota.
DR GeneTree; ENSGT00940000165924; -.
DR OMA; QEIHYNT; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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; 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:UP000028760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 192..280
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 328..509
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 518..702
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 773..1055
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 411..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 122267 MW; 95E7B2C3B21900F0 CRC64;
MRTQGGSANN LKFICEFRPD EDNSVNGDFE SVTVILPAQC SISQLRLRIC MKAQEQNCHP
DPFAILDPEK YILLYARGDD WYEAHDDCQI IRTLDIPWSH DDSPCLVAHI VAKPLVAGDS
EQKKNQQECL TYLIGHDLDN EASDRLGELT FTRRKLASPR RLELRNRDKV LYATEPWVTQ
APIPNELEEW LNRKLCLTLH YMSKISFSIQ VDLKATPDVL LEVFRRVMAD QRVEYNSSEE
LVLKVSGREE FLSGENCLCD FLWVRQCLKA NQDLHLSVVP VSQLAADTVR FVDWPLVDGF
SGQFSSHDDL SLLGKDLDDI FMISLWDCNR KFRVKLLGFD IPQLPNKPPQ SVYVEASILY
GGKVLCSVSS LPKLFGDEVL WNEWLEFDIL LRDLPRGVKL SFTINTCASD VSPTTKDPKP
GLSRDSKVSL NKHTDTQKGK TKILYFVNLL LIDHRSVLSQ GPYTLHMWSY PDLEDGAITY
QADKLSSATN PHIDESMAIS FLLDRYSFPV VLPNTFSHND GSGSPTSDLF PDKSTSSTQC
TSPITDSLSP HGKRDYLKRF REESVQYGSN LPHFLRNINW LDRRVVEDVH WLLGLWDPGE
LDVHVALELL SMDFPDEIVR KLAVRRLESL PNDDVLKYLL QLVQTLKVEP YHDSFLARYL
IQRALRSKRI GHFFFWYVRS EVAGCPYFRQ RMAVILEAYL LGCGQAMINI FTQQVQAVEA
LQEVAMIIKR LYPDKTDLPS SAPLKLQELL RSSNLPNEFL LPFDPRIKVG TILLDKCKVM
ASKKKPLWLE FSPMPSPTSS TPVGIIFKEG DDLRQDMLVI QTLVVMESIW QEQSLDLNLI
PYGCISTGHN IGMIEIVRNA ATIAAVQRSH GGTTAAFRND ALFEWLRSKC PLQEIHYKTV
ERFVKSCAGY CVATYVLGIG DRHNDNIMIT DQGNLFHIDF GHILGNRKHF LGVSRERAPF
VLTPDFLYVM GRLRGRNSLY FQRFRDTCSQ AYLLLRSHSR LLVTLFSLML LTGIPELSAA
EDMRYLREAL QEDQTEAEAK EHFLQRIAEC EQLGWTVQAN WWIHMVAGIR
//
