ID A0A3S0ZZT5_ELYCH Unreviewed; 1046 AA.
AC A0A3S0ZZT5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EGW08_005111 {ECO:0000313|EMBL:RUS87111.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS87111.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS87111.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS87111.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS87111.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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:RUS87111.1}.
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DR EMBL; RQTK01000119; RUS87111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0ZZT5; -.
DR STRING; 188477.A0A3S0ZZT5; -.
DR Proteomes; UP000271974; 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 CDD; cd05165; PI3Kc_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; IPR003113; PI3K_ABD.
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:SF111; PHOSPHATIDYLINOSITOL 3-KINASE AGE-1; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF02192; PI3K_p85B; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00143; PI3K_p85B; 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; PS51544; PI3K_ABD; 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:UP000271974};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..103
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 189..290
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 330..477
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 501..678
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 746..1031
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1046 AA; 122079 MW; 15B4B56CE4D76FB4 CRC64;
MPPSSGELWE HYLMPQHVQV DCLLPTGVLI TLPCARDDTL ESIKKELWQE ARRYPLFYKL
MEPESYIFLA ITQDAMREEF YDETRRLCDL RLFQPILKVM EPKGNRDEKM VNYEISMLIG
VPVNEFNNNK ELEVITFRRN ILKACKDVVD QRDESGDHIR ALYTYPPEID SEVDLPQHLL
DRLKTFSDET SVIICVWVVN DDNNRTKYTV KVPHMAVPSD VIAETIRRRS RFMNMSRENA
ERCIEEYRHM YVLKVCGCDQ FLLAERPISQ YRYIRECLAK ESLPQLMLHT KENVYATLPE
TNFTWPTYMQ RGIQALAEIN KQQTTCIFDV DAPLRVKINC ATYVNIKESC KIYVRACIYH
GTEPMCEAKN TELVDSYNPR WDQWLDFLRV PDTPRSARLC LSICSESKRR NRRVHYALAW
GNLQLFDFNK RHLHGRYMLH LWSMPQGMDD LLNPIGITGS NPNKECPCLE IEFDNFGHPL
AYPSEDQFHQ LALQAMQREE ASAKEQPCET ELAMLEEITE KDPLSDISEQ DKILLWKFRE
HCLSRPKALP KLLSAVKWND RENVAQLYLL LDRWPLIPVE VALELLDCSF TDLRVREFAV
NSLDKGLGDD KLAQYLLQLV QAIKYEPYHD NPITKFLLKR SLMSQKIGNV FFWHLKSEMH
QTSIRQRFGL ILEAYCRGCG PYLKNLARQV EALDKLWKLS EMLKHEVNAD EHQKYLHMQL
QQPDYREALQ NLHSPLNTAH ILGELNLEDC CVKTSKKLPL WLVWSNPDTM ADMGDFYYRI
MFKNGDDLRQ DMLTLQVIGL MDSIWKNEGL DLRLIPYGCL STGKDVGLIE VVKNAKTITA
IQSKGGALSS IQIDSSQLHK WIKEQNPDRY DHAIDVFKRS CAGYCVATFV LGIGDRHPEN
IMVTSEGQVF HIDFGHFLDH KKKKFGINRE RVPFVLTEDF QRVIARGADK PSKHKGFKEF
QELCGQAYLI LRKHANLIIT LFTMMLQCGI PELQSLDDIG YIRKTLAVEK VEERALEYFQ
NQFHSAYGDS WTTKVDWFFH NMKFKH
//
