ID W9QWV8_9ROSA Unreviewed; 1101 AA.
AC W9QWV8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=L484_020718 {ECO:0000313|EMBL:EXB40983.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB40983.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-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};
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DR EMBL; KE343785; EXB40983.1; -; Genomic_DNA.
DR RefSeq; XP_010090858.1; XM_010092556.1.
DR AlphaFoldDB; W9QWV8; -.
DR STRING; 981085.W9QWV8; -.
DR GeneID; 21403604; -.
DR KEGG; mnt:21403604; -.
DR eggNOG; KOG0903; Eukaryota.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000030645; Unassembled WGS sequence.
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 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, ECO:0000313|EMBL:EXB40983.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..142
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 818..1086
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 184..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 124618 MW; 429BCB844B95A469 CRC64;
MVRLLGLTRG ETYESPREIT SSRANSSSDS GDNGWLIRFF DSAFFCEWIA VSYLYKHEHS
GVRDYLCNRM YTLPLSGIES YLFQICYMMV HKPSPSLDKF VIDICSKSLK IALKVHWFLL
AELEDSDDNE GISRIQEKCQ IAATLMGEWP PLIRPQSESS SPGSKSQVLN RILSSKQRLL
SLTTSPPAQK SLSFSPSSGG VAQEEGGPMS PDENKIFKRF IPSPKVRDAL LFRKSGEKDD
EDSEKDGFFK RLLRDSKGED EGGSKIRELF RKSSEKEEDD SEKDGFFRRL LRDSRGDDEE
LTTSSEGFFK RLFRDSKSDT EDKSTSKSVE EEEKEGFFKK LFKDKFDDKK HVTGRYEDEE
VVHLEEKSSK STEDEEKEGF FRKFFRDKFE DRRDGNDKAD EGSANGEEED PSDFSLFRKL
FRVHPEEAKN NAANENNSGG LFESSPGTEN FFRKLFRDRD RSVEDSELFG LKHKEKRPGS
PRQRDEKSYV KPPLPSNTAS QFRKGAYHES LDFVLSLCET SYGLVDIFPI EDRKSALRES
LAEINQHLSE AQKSGGIGFP MGKGMYRVVH IPEDEAVLLN SREKAPYLIC VEVLKSETPS
NPRDSSSPQK LSRGGIPLAN GDALLPKPPP WAYPLWTVQE VYRNSNDRMS SSTALAIDQA
MTHMSEARVK FVNVKLSVEK QYHSHSEDIE ISDSQSAIDS TGTKSFHSVS KSCQSGENRA
HPSKPAHGCD LKWVRVVLTA DPGVRMEDIE DQGPRRRREH RRVPSTVAIE EVKAAAAKGE
APPGLPLKGA GQDSSDAQPR VNGATPKASD ALSGELWEVK KERIRKASVY GKLPGWDLRS
VIVKSGDDCR QEHLAVQLIS HFYDIFQEAG LPLWLRPYEV LVTSSYTALI ETIPDTASLH
SIKSRYPNIS SLRDFFVAKY QENSPSFKLA QRNFVESMAG YSLVCYLLQV KDRHNGNLLM
DEEGHIIHID FGFMLSNSPG GVNFESAPFK LTRELLEVMD SDAEGVPSEF FDYFKVLCIQ
GFLTCRKHAE RIILLVEMLQ DSGFPCFKGG PRTIQNLRKR FHLSLTEEQC VSLVLSLISS
SLDAWRTRQY DYYQRVLNGI L
//
