ID A0A059AKL2_EUCGR Unreviewed; 1027 AA.
AC A0A059AKL2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=EUGRSUZ_I00214 {ECO:0000313|EMBL:KCW54241.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW54241.1};
RN [1] {ECO:0000313|EMBL:KCW54241.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW54241.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000256|ARBA:ARBA00001686};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK198761; KCW54241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059AKL2; -.
DR STRING; 71139.A0A059AKL2; -.
DR EnsemblPlants; KCW54241; KCW54241; EUGRSUZ_I00214.
DR Gramene; KCW54241; KCW54241; EUGRSUZ_I00214.
DR eggNOG; KOG0903; Eukaryota.
DR InParanoid; A0A059AKL2; -.
DR OMA; AYPLWTV; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol 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; cd05168; PI4Kc_III_beta; 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; 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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR049160; PI4KB-PIK1_PIK.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; PS51545; PIK_HELICAL; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..142
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 741..1012
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 183..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1027 AA; 116092 MW; 800DB42DA1E6F326 CRC64;
MVRILGLTIG ESDDSPREIS TSRTLLASDS GEAGWLIRFF NSAFFCEWIA VSYLYKHNHT
GVRDYLCNRM YTLPLSGIES YLFQICYMMV HKPSPSLDKF VIDICSQSLK IALKVHWFLM
AELEDNDDND GIGRIQEKCQ TAATLTGEWA PFVRPQNATA SPGSNKNQVF SRILSSKQRL
LSLTSSPDDG KRRSFSFSPS SGNRLQEEIG QSTPEENNLF KKLIPGPKVR DALLFRKSVE
KDDEDSGKEG FFKKFLRDSR GEDEELTTSS EGFFKRVFRD SKGKDEELTS SSDNFFKKLF
RDSKSDSEDR SVSKSLEDYE KDGFFRKLFK EKSEDKKDGN DDEDRGTTEE RCSKSAEDDE
KEGFFKKLFR EKFEDKKEGN DKVEEGNAHI DEEEPSDSPG TENFFRKLFR DRDRSVEDSE
LFGSKKQNEK HPGSPKERDD KTNAKPPLPY KNASQFRKGT YHESLDFVQR LCETSYGLVD
IFPVEDRKTA LRESLAEINL HIAEAQESGG VCFPLGKGMY RVVHIPEDEA VLLNSREKAP
YLICAEVLKS EMPSNSKDTC GSQKLSKGGI PLANGDALLP TPPPWACPLR TTQEIYRNSA
DRMSFSAAQA IDQAMGHKSE AKMKFVNVKL SVEKMKHQAT GQKSGSSRQR EGEQTTDLEW
VRVVLTADPG ARMEDIQDQG SSRRKEHRRV PSTVAIEEVK AAAAKGEAPP GLPLKGAGQD
SSEAQPRAGG TLKAGDALAG ELWEFKRERI RKASDFGKLP GWDLRSIIVK SGDDCRQEHL
AVQLISHFYD IFQEAGLPLW LRPYEVLVTS SYTALIETIP DTASLHSIKS RYPNIASLRD
FFVAKYQENS PSFKLAQRNF VESMAGYSLV CYLLQVKDRH NGNLLLDEEG HIIHIDFGFM
LSNSPGGVNF ESAPFKLTRE LLEVMDSDAE GIPSEFFDYF KVLCIQGFLT CRKHAERIIL
LVEMLQDSGF PCFKGGPRTI QNLRKRFHLS LTEEHCVSLV LSLISSSLDA WRTRQYDYYQ
RVLNGIL
//
