ID A0A2U9BY22_SCOMX Unreviewed; 1078 AA.
AC A0A2U9BY22;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative phosphatidylinositol 4-5-bisphosphate 3-kinase catalytic subunit gamma {ECO:0000313|EMBL:AWP09207.1};
GN ORFNames=SMAX5B_002734 {ECO:0000313|EMBL:AWP09207.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP09207.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP09207.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; CP026253; AWP09207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BY22; -.
DR STRING; 52904.ENSSMAP00000006370; -.
DR Proteomes; UP000246464; Chromosome 11.
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, ECO:0000313|EMBL:AWP09207.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 220..308
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 356..517
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 531..710
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 781..1063
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 527..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1078 AA; 122534 MW; 174DAC980ECD3A07 CRC64;
MDFGLFLNQS DSLHAVDAPS EMLTLSSSEN NLKFICEFKP GSGPLPGSDD CNADMDCKSV
SVIIPAQCSI YQLRLRICMQ AQEKNCHPDP LTILDPERYT LLYARGDDWY EAYDDCQVIR
TLDIPWSRDD TGRLSAQIVV KPLVAIDSEE KKKQQQCLAY LIGHNLEKEA SDRLGELTFT
RRKLSSPRRQ ELKNRDDKLY ATEPWVTCAP IPTDLQDRLN RKLPVTLHYM NKISFSIQVD
FGATPDVLLK IFRRVLADQG LDDDTSDSLV LKVSGREEFL SGDYPLSDFH WVRQCLKTNQ
DLHLSVVPES QLVEETVQFV DWPLVDGFSG QFSSHCDLCL DGKDLDDIFM ISLWDCNRKL
RVKLLGFDIP NPPSKCPQAV YVEASILYGK KLLSSVSSVP KAFADEVLWN EWLEFDVLLR
DLPRGAKLGF TINASAGDIS PVTKDSGEGK VLYFVNLLLI DHRSVLSQGS HTLYMWTYPD
QEEEAITYQA DKLSSATNPD VTDSMAISFL LDRYSFPVVL PNSLNTPESY GSPTSSLSPT
KSTAFSHESS SSHFSPTSST NTPCLKRFRE ESVRYASNLP HYLRNVDWMK RRVVKDIHWL
LENWDPGDLD VTVALELLSM DFADERVRGL AVQRLESLSN DDVLKYLLQL VQTLKVEPYH
DSFLARYLIQ RALRSKRIGH FFFWYVRSEV AGCPYFRQRM AVILEAYLLG CGQAMIDSFT
QQVQAVEALQ EVAIMIKNLF PDKTDLLPTA PIRLQELLRN CNLPNEFLLP FDPRIKVGVI
LLDKCKVMAS KKKPLWLEFS PMPSPTSATP VGIIFKEGDD LRQDMLVIQT LMVMDSIWQE
KSLDLNLVPY GCISTGHNIG MIEIVRDAAT IAAVQRTHRG SAGAFRNDAV FEWLKSKCPL
QEIHYTTVER FVKSCAGYCV ATYVLGIGDR HNDNIMITDQ GNLFHIDFGH ILGNRKHFLG
VNRERVPFVL TPDFLYVMGR VRGRNSLYFQ RFRDTCTQAY LSLRSHSRLL VTLFSLMLLT
GIPELSAAED MRYLREALQE EQGEAAAREH FLQQIAECEQ LGWTVQANWW IHMVAGIK
//
