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Database: UniProt
Entry: B9V0G9_9ORYZ
LinkDB: B9V0G9_9ORYZ
Original site: B9V0G9_9ORYZ 
ID   B9V0G9_9ORYZ            Unreviewed;      1222 AA.
AC   B9V0G9;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN   ORFNames=OA_CBa062H21-3 {ECO:0000313|EMBL:ACM17540.1};
OS   Oryza australiensis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4532 {ECO:0000313|EMBL:ACM17540.1};
RN   [1] {ECO:0000313|EMBL:ACM17540.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19098269; DOI=10.1105/tpc.108.063727;
RA   Ammiraju J.S., Lu F., Sanyal A., Yu Y., Song X., Jiang N., Pontaroli A.C.,
RA   Rambo T., Currie J., Collura K., Talag J., Fan C., Goicoechea J.L.,
RA   Zuccolo A., Chen J., Bennetzen J.L., Chen M., Jackson S., Wing R.A.;
RT   "Dynamic evolution of oryza genomes is revealed by comparative genomic
RT   analysis of a genus-wide vertical data set.";
RL   Plant Cell 20:3191-3209(2008).
RN   [2] {ECO:0000313|EMBL:ACM17540.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ammiraju J.S.S., Lu F., Sanyal A., Song X., Jiang N., Pontaroli A.C.,
RA   Rambo T., Currie J., Kollura K., Talag J., Fan C., Goicoechea J.L.,
RA   Zuccolo A., Bennetzen J.L., Chen M., Jackson S., Wing R.A.;
RL   Submitted (SEP-2008) 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};
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DR   EMBL; FJ266020; ACM17540.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9V0G9; -.
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: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, ECO:0000313|EMBL:ACM17540.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..157
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          939..1207
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          13..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          822..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..844
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1222 AA;  137478 MW;  473AC52512BC95BA CRC64;
     MVRLLGLRSL SFGPEESPRE ITVAGGGGGG GGGGGGDAAA HPVGSSGWLV RFFDSAFFCE
     WIAVSYLYKH DHQGVRDYLC NRMYTLPLPG LEAYLFQVCY MMVHKPSPSL DRFVIDTCSK
     SLRIALKVHW LLAAELELED TDDLDGIDRV QEQCQAAATV QGEWPPLVRP APPSPIASPR
     GNPMLSRIRS SKQRLLSLAS SPSLGLSPPA GASNAAAADD VGGSGGKQPT TPLSEDNKLL
     KRLSIGPKVR DAASFFRRSV DKDDEQDKEG FFKRLLRDSK DKEEEDGDKE GFFKRLLSKE
     KENEEEEGDR DGFFRRLLRD SKDEDMELTP SSEGLLKRLF RDKEDRQGDD EEKEGFFRRI
     FKDKNEERRE SLHGRHGDEE RVGKSLEEDD KEGFFRKIFK DKNEERKDGG HSKQQDDKEK
     TAGNIEEDKR DGFFRQLFKE KNEEKKEGIT PNKKEEDDKG HRTMDEDNFF RRLFKDKNEE
     KKGAAHDKND DDKCEEGDKE NFFRKLFKDK HEERRSDGLD KHDDDGKGTS GIDDEENSEF
     LSFRRLFRVH PEEAKSGHIE SSQPNSISEG SPGSESFFKR LFRDRDRSLE DSELFGSKLL
     KEARHQLSEK NPAPTGNGDK QSGKPPLPNN AIAELRKGCY YASLELVQSL CDTSYGLVDI
     FPMEDRKIAL RESLTEINSQ IASTEKNGGV CFPMGKGIYR VVHIPEDEAV LLNSREKAPY
     LICVEVLKAE APSHSKGSSD VNKLSKGGIP LANGDVQLPK PPPWAYPLWS RHETQNYETD
     RMLKSTSQVI DQAMAQLWEA KVKFVNVSFS VEKLGRSRSI AISDSGHRSR QSTADSNEPS
     GDSQPIADQP IEWVKVTLSA VPGVNMDDVD DNEPTRKKDH RRVPSTIAIE EVKAAALKGE
     APPGLPLKGV GQNAQNIDSK ATDGGDPKPT DALAGELWAV KKERIRRSSV HGKLPGWDLR
     SVIVKSGDDC RQEHLAVQLV AHLYDIYQEA GLPLWLRPYE VIVTSAYTAL IETIPDTASI
     HSIKSRFPDI TSLRDYYVAK YEENSPNFKL AQRNFVESMA GYSILCYLLQ VKDRHNGNLL
     IDEEGHIIHI DFGFMLSNSP GGVNFESAPF KLTRELLEVM DSDAEGTPSE FFDYFKVLCI
     QGFLTCRKHA ERIILLVEML QDSGFPCFKG GPRTIQNLRK RFHLSLTEEQ CVSLVLSLIS
     SSMDAWRTRQ YDYYQRVLNG IL
//
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