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
//