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Database: UniProt
Entry: A0A0D3B671_BRAOL
LinkDB: A0A0D3B671_BRAOL
Original site: A0A0D3B671_BRAOL 
ID   A0A0D3B671_BRAOL        Unreviewed;       773 AA.
AC   A0A0D3B671;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase {ECO:0000256|PIRNR:PIRNR037274};
DE            EC=2.7.1.68 {ECO:0000256|PIRNR:PIRNR037274};
GN   Name=106333009 {ECO:0000313|EnsemblPlants:Bo3g035460.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo3g035460.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo3g035460.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo3g035460.1}
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 4-
CC         phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178,
CC         ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037274};
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DR   RefSeq; XP_013626948.1; XM_013771494.1.
DR   AlphaFoldDB; A0A0D3B671; -.
DR   STRING; 109376.A0A0D3B671; -.
DR   EnsemblPlants; Bo3g035460.1; Bo3g035460.1; Bo3g035460.
DR   GeneID; 106333009; -.
DR   Gramene; Bo3g035460.1; Bo3g035460.1; Bo3g035460.
DR   KEGG; boe:106333009; -.
DR   eggNOG; KOG0229; Eukaryota.
DR   HOGENOM; CLU_004312_6_4_1; -.
DR   OMA; FYEVVMI; -.
DR   OrthoDB; 340426at2759; -.
DR   Proteomes; UP000032141; Chromosome C3.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd17302; PIPKc_AtPIP5K_like; 1.
DR   Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR   Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 4.
DR   Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR017163; PIno-4-P-5_kinase_pln.
DR   InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR   InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR   InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR   InterPro; IPR023610; PInositol-4/5-P-5/4-kinase.
DR   PANTHER; PTHR23086:SF127; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE; 1.
DR   PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1.
DR   Pfam; PF02493; MORN; 8.
DR   Pfam; PF01504; PIP5K; 1.
DR   PIRSF; PIRSF037274; PIP5K_plant_prd; 1.
DR   SMART; SM00698; MORN; 7.
DR   SMART; SM00330; PIPKc; 1.
DR   SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   PROSITE; PS51455; PIPK; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR037274, ECO:0000256|PROSITE-
KW   ProRule:PRU00781};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037274};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037274, ECO:0000256|PROSITE-
KW   ProRule:PRU00781}; Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037274}.
FT   DOMAIN          377..769
FT                   /note="PIPK"
FT                   /evidence="ECO:0000259|PROSITE:PS51455"
FT   REGION          20..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  88463 MW;  AC55A492A3A415B1 CRC64;
     MSKEQSYVLK AWEVTVRKTQ QAKKRANSVF GTVSVSPHTD NDTSTDENDD ETSTNRSSLE
     EFYHAERVLP NGDYYTGQWY DSFPHGHGKY LWTDGCMYIG DWYNGKTMGN GKFGWPSGAT
     YEGEFKSGYM DGTGTYTGPS GDAYKGQWVM NLKHGHGVKS FANGDAYDGE WRRGLQEGHG
     RYQWSDGCHY TGEWKNGTIY GKGSFVWTNG NRYDGCWDEG FPRGNGTYKW DDGSFYVGNW
     SKDPEEMNGT YYPSGNEGNL EWDPKDLFDN LSEYTICSGE RVPMLPSQKK LSVWNSSKRI
     EKPRRVSVDG RVSVGVDRAF EKMNMWGNET GEEGTDLRKE LDAELMRLEA EGIRSLKSSP
     VPMKLPKAGR KQGETISKGH RNYDLMLNLQ LGIRHSVGRQ APVASLDLKP SAFDPKDKIW
     RRFPREGTKY TPPHQSTEFK WKDYCPLVFR SLRKLFKVDP ADYMLSICGD DALRELSSPG
     KSGSFFYLTN DDRYMIKTMK KSETKVLLRM LAAYYNHVRA FENSLVIRFF GLHCVRLNGP
     TQKKVRFVIM GNLFCSKYSV HRIFDLKGSS LGRTTDKPES EIDSNTILKD RDLSFIFRLQ
     KAWYQEFTRQ IDKDCEFLEQ ERIMDYSLLV GIHFRESSVA GDLIPSGAKT PIGESDEEAC
     HRLSRAEVDQ LLSDPSRWAS IRLGTNMPAR AERTVRKSSD SELELVGEPT GEFYEVVLIF
     GIIDILQDYD ISKKLEHAYK SIQYDPSSIS AVDPKQYSRR FRDFIFKAFT DDN
//
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