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Database: UniProt
Entry: R7U1H6_CAPTE
LinkDB: R7U1H6_CAPTE
Original site: R7U1H6_CAPTE 
ID   R7U1H6_CAPTE            Unreviewed;      1057 AA.
AC   R7U1H6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CAPTEDRAFT_183615 {ECO:0000313|EMBL:ELT99799.1};
OS   Capitella teleta (Polychaete worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Capitellidae; Capitella.
OX   NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT99799.1};
RN   [1] {ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELT99799.1, ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT99799.1,
RC   ECO:0000313|Proteomes:UP000014760};
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:CapteP183615}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00879}.
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DR   EMBL; AMQN01009879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB306460; ELT99799.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7U1H6; -.
DR   STRING; 283909.R7U1H6; -.
DR   EnsemblMetazoa; CapteT183615; CapteP183615; CapteG183615.
DR   HOGENOM; CLU_002191_1_1_1; -.
DR   OMA; WSEWLNY; -.
DR   Proteomes; UP000014760; 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:UP000014760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          14..103
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          188..288
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          328..483
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          513..690
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          757..1042
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1057 AA;  122335 MW;  561ABBBBAB92C372 CRC64;
     MPPSSGELWG HHLMPSQVDV DCLLPNGIII SLPCYRDANL GTIKFELWKE AKKYPLFSQL
     SDASSYIFVS ITQDAEREEF YDETRRLCDL RLFQPILKVV EPKGNREEKM LNYDIGIAIG
     MSVNEFNDNK DLEIMTFRRR VLDVCKMAVE ERDSRGNLSQ ARYVYPPDIH HSAQLPPHIN
     ERIEKEGKGK IMICIWVVSA SDRQKYTVGV SHMATPEEVI AEAIRRRTRL MNMSPEQQRR
     CIVEYQDSYI LKVCGCELFL LEKYPVSQFK YMRTCISRSR IPQLMLMSKE GVFSSLPKNI
     FTIPAYVMKG VSAFQDINKQ NTTSLWNMDA MLKIKINSAM YVNVKEKGEI YVKTGIYHGT
     ESLCPIKDTA RVESSNPKWN QWLEYDLYLP DIPRCARLCL ALCCVSKKQK KKQVHYALAW
     GNINLLDFNN RLLCEKTTLR LWPVPQGQED MLNPIGVPGP CPNGDSPCVE IEFHRFGMPV
     SYPTEAQIDE YANWLSSRNR NQAHVQGSTT APPLMNEPLS KTEQDQLQEI IRRDPLSELS
     EQDKELLWKS RHACIPIPGS LPKLLQAVKW YSREDVVQVY VLLREWPIVS TETALELLYC
     TFTDLTVRRF AVKCLEEGLT DDQLSQFLLQ LVQVLKFEPY FDNYLTRFLL RRALLSQRIG
     HFFFWHLKSE MHQANIRQRF GLILEAYCRG CGAYLKSLCR QVEALDKLAK LSDSVKMERE
     ETQMKVLCSQ VQQADYMEAL QHFPSPLNNS YILGDLIIED CEVKHSKKKP LQLVWQNPDA
     MSELLFTDFK ILFKNGDDLR QDMLTLQVIG IMDSIWQGEG LDLRLIPYGC LATGPNMGMI
     EVVRNARTVL KILSQDIRSA MMVRTKELHS WIKEKNKGDR YQQAIELFTM SCAGYCVATF
     ILGIGDRHPS NIMVTEEGQV FHIDFGHFLD HRKKKFGINR ERVPFVLTED FIRVIARGQD
     NPIKSQEFAD FMELCGKAYL SLRKHSNVFI TLFTMMLSCG IPELQSLDDI GYLRKTFVVE
     KSEQEALEYF QKRFNEAYGG AWTTKLDWFF HWVKHGN
//
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