ID D8SKG0_SELML Unreviewed; 790 AA.
AC D8SKG0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=phosphatidylinositol 3-kinase {ECO:0000256|ARBA:ARBA00012073};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
GN ORFNames=SELMODRAFT_118849 {ECO:0000313|EMBL:EFJ15325.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ15325.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE-ProRule:PRU00880}.
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DR EMBL; GL377624; EFJ15325.1; -; Genomic_DNA.
DR RefSeq; XP_002983829.1; XM_002983783.1.
DR AlphaFoldDB; D8SKG0; -.
DR STRING; 88036.D8SKG0; -.
DR EnsemblPlants; EFJ15325; EFJ15325; SELMODRAFT_118849.
DR Gramene; EFJ15325; EFJ15325; SELMODRAFT_118849.
DR KEGG; smo:SELMODRAFT_118849; -.
DR eggNOG; KOG0906; Eukaryota.
DR HOGENOM; CLU_004869_0_0_1; -.
DR InParanoid; D8SKG0; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08397; C2_PI3K_class_III; 1.
DR CDD; cd00870; PI3Ka_III; 1.
DR CDD; cd00896; PI3Kc_III; 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; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR008290; PI3K_Vps34.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 2.
DR SMART; SM00142; PI3K_C2; 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 PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Kinase {ECO:0000256|PIRNR:PIRNR000587};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Transferase {ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 21..165
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 258..438
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 509..782
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 790 AA; 90008 MW; F13BAE97F2232FED CRC64;
MDQVFLSSDI NFPVTALVES LQGDLRSPPS SQEDLSPALY VECALYIDGS PFGLVTRTGL
AIEKPYKWNE AITLTGKYRD LSLNAQLAFT VWDVSNPLQE IAVGGSTLKL FNSKGQLKTG
KQRLRLWRGR VADGSAVSTT PGKVPEGERG EVERLDKLLS KYERGEIEHI DWLDNSALKA
IDKIMAEQKK SSTHFFLTVK LWSFGHAVEY QERAEALLSQ PPTSRTLCAL WDTEIGRENP
CEVKHFKLAR SISRLVIDPD LKPSSKEKRV LMQVCNSPPT QKLTSDDKML LWKFRFYLST
DKKALTKFLR CVDWNDAQEA KQATELMHKW EPVDIPDALE LLSADFESEE VRAYAVEALR
KKTTAEELQC YWLQLVQALQ FERCDKSPLA YFLVQKAVQI PDLANSFHWY VMKELAKATE
PSNKTKRFFS VHDLFETQML KKPMDYSGKP LLDQLHRQTE LVSKLCSITT AVKDVADKDE
KLRQLLSDLT SFEELPSPLD PKIIITGIVP RESSVFTSSR SPLVLTFRTV AGGSCKVMFK
KGDDLQQDQL VIQLITLMDQ LLKVENLDLQ LTPYRVLATN KDEGLLEFVT GSKNLQTILV
RHRSIINYFR QCHPDPEGQF GISAPCLETF VKSCAGYCVI TYILGVGDRQ AFLHLENLLI
RDDGRLFHVD FGFILGKDPK PFPPPMKLCK EMVDAMGGIN SEYYGKFKLY CCEAFNILRK
SSNLILNLFY LMSNSEVAIL KLQEKFQLSL DDEEAIQFFQ LLINESVNAL FPQVVDTMHR
WAQYWRYGKV
//
