ID A0A0D3DY21_BRAOL Unreviewed; 769 AA.
AC A0A0D3DY21;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase {ECO:0000256|PIRNR:PIRNR037274};
DE EC=2.7.1.68 {ECO:0000256|PIRNR:PIRNR037274};
GN Name=106307687 {ECO:0000313|EnsemblPlants:Bo8g109210.1};
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:Bo8g109210.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo8g109210.1, 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:Bo8g109210.1}
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_013600160.1; XM_013744706.1.
DR RefSeq; XP_013600161.1; XM_013744707.1.
DR AlphaFoldDB; A0A0D3DY21; -.
DR STRING; 109376.A0A0D3DY21; -.
DR EnsemblPlants; Bo8g109210.1; Bo8g109210.1; Bo8g109210.
DR GeneID; 106307687; -.
DR Gramene; Bo8g109210.1; Bo8g109210.1; Bo8g109210.
DR KEGG; boe:106307687; -.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_6_4_1; -.
DR OMA; KARTMMY; -.
DR OrthoDB; 340426at2759; -.
DR Proteomes; UP000032141; Chromosome C8.
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:SF131; 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; 8.
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 344..765
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 244..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 87424 MW; 40B167FEA265A0F3 CRC64;
MDTRPGEREF SNGDFYSGEL KGSLPHGKGK YEWSDGTIYQ GDWYEGKISG KGKLVWPSGA
KYEGDFSGGY LHGIGTMTSP DGSVYSGAWR MNVRHGLGRK EYVNSDLYDG SWKEGLQEGH
GSYSWTNGNR YIGNWKNGKM CGRGVMRWAN GDLFDGFWLN GFRHGSGVYK FVDGCLYYGA
WSHGLKDGKG VFYPAGSKHP SLKKWCRSLQ HDDTGKFVLS RSSSINVEEL RSLSTVTPSL
SVKTSVSGTS KTLSERFRDE NLRTSEPPPS DFTCHGPSSK SARSSGSGQR EGQDKNRVVY
EREYMQGVLI RETITSSVDR SHKIRPPNLP KQVRDRSFMT FLKGEHNYYL MLNLQLGIRY
TVGKITPVPR REVRASDFGK KARTMMYFPR DGSNFTPPHK SIDFSWKDYC PMVFRNLRAM
FKLDPADYMM SICGDDGLTE ICSPGKSGSI FYLSHDDRFV IKTLKKSELE VLLKMLPKYY
RHVGDHENTL ITKFFGVHRI KLKLGKKVRF VVMGNMFCTE LKIHRRYDLK GSTQGRITEK
TKIQEKTTLK DLDLAYEFHM DKLLREALFK QIYLDCAFLE SLHIIDYSLL LGVHFRAPEQ
LNDILEHPNE MSDQDSVSSV DVGMAQELSI PPKGLLLVTH EPNSVNTAPG PHIRGSTLRA
FSVGEKEVDL ILPGTARLRV QLGVNMPAQA HHKLDEDKEE SATIELFEVY DVVVYMGIID
ILQEYNAKKK VEHKCKSLRY DPMTISVTEP KVYSKRFVDF LHKVFPEET
//
