ID A0A0D3HJG7_9ORYZ Unreviewed; 1264 AA.
AC A0A0D3HJG7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART11G06300.2};
RN [1] {ECO:0000313|EnsemblPlants:OBART11G06300.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART11G06300.2};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART11G06300.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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};
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DR AlphaFoldDB; A0A0D3HJG7; -.
DR STRING; 65489.A0A0D3HJG7; -.
DR PaxDb; 65489-OBART11G06300-2; -.
DR EnsemblPlants; OBART11G06300.2; OBART11G06300.2; OBART11G06300.
DR Gramene; OBART11G06300.2; OBART11G06300.2; OBART11G06300.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_002446_4_1_1; -.
DR Proteomes; UP000026960; 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: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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..150
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 933..1201
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 154..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1264 AA; 142590 MW; C5726FE7029D2CA3 CRC64;
MVRLLGLRSL SFGPEESPRE ITVAGGGGGD AAAHPVGSSG WLVRFFDSAF FCEWIAVSYL
YKHDHQGVRD YLCNRMYTLP LPGLEAYLFQ VCYMMVHKPS PSLDRFVIDT CSKSLRIALK
VHWLLAAELE LEDTDDLDGI DRVQEQCQAA ATVQGEWPPL VRPAPPSPIA SPRGNPMLSR
IRSSKQRLLS LASSPSLGLS PPAGASNAAA AEDVGGSGVK QPATPSSEDN KLLKRLSIGP
KVRDAASFFR RSVEKDDEQD KEGFFKRLLR DSKDKEEEDG DKEGFFKRLL SKEKENEEEE
GDRDGFFRRL LRDSKDEDME LTPSSEGLLK RLFRDKEDRQ GDDEEKEGFF RRIFKDKNEE
RRESLHGRHG DEERVGKSLE DDDKEGFFRK IFKDKNEERK DGGHSKQQDD KEKTAGNIED
DKRDGFFRQL FKEKNEEKKE GTTPNKKEED DKGHRTMDDE NFFRRLFKDK NEEKKGAAHD
RNDDDKCEEG DKENFFRKLF KDKHEERRSD GLDKHDDDGK GTSGIDDEEN SEFLSFRRLF
RVHPEDAKSG HIESSQPNGI SEGSPGSESF FKRLFRDRDR SLEDSELFGS KLLKEARHQL
PEVKNSVPTG NGDKQSGKPP LPNNAIAELR KGCYYASLEL VQSLCDTSYG LVDIFPMEDR
KIALRESLTE INSQIASTEK NGGVCFPMGK GIYRVVHIPE DEAVLLNSRE KAPYLICVEV
LKAEAPSHSK GSSDVNKLSK GGIPLANGDV QLPKPPPWAY PLWSRHETQN YETDRMLKST
SQVIDQAMAQ LWEAKVKFVN VSFSVEKLGR SRSVAISDSG HRSRQSTADS NEPSGDSQPI
ADQPIEWVKV TLSAVPGVNM DDVDDNEPTR KKDHRRVPST IAIEEVKAAA LKGEAPPGLP
LKGVGQNAQN IDSKATDGGD PKPTDALAGE LWAVKRERIR RSSVHGKLPG WDLRSVIVKS
GDDCRQEHLA VQLVAHLYDI YQEAGLPLWL RPYEVIVTSA YTALIETIPD TASIHSIKSR
FPDITSLRDY YVAKYEENSP NFKLAQRNFV ESMAGYSILC YLLQVKDRHN GNLLIDEEGH
IIHIDFGFML SNSPGGVNFE SAPFKLTREL LEVMDSDAEG TPSEFFDYFK VLCIQGFLTC
RKHAERIILL VEMLQDSGFP CFKGGPRTIQ NLRKRFHLSL TEEQCVSLVL SLISSSMDAW
RTRQYDYYQR ELLAPSKNQF AYIIVKISGI AQVSLGLTSQ VQPPWFLRAK HAFVFCISHT
WSPL
//
