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Database: UniProt
Entry: D7KW77_ARALL
LinkDB: D7KW77_ARALL
Original site: D7KW77_ARALL 
ID   D7KW77_ARALL            Unreviewed;       769 AA.
AC   D7KW77;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase {ECO:0000256|PIRNR:PIRNR037274};
DE            EC=2.7.1.68 {ECO:0000256|PIRNR:PIRNR037274};
GN   ORFNames=ARALYDRAFT_475243 {ECO:0000313|EMBL:EFH62837.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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   EMBL; GL348714; EFH62837.1; -; Genomic_DNA.
DR   RefSeq; XP_002886578.1; XM_002886532.1.
DR   AlphaFoldDB; D7KW77; -.
DR   STRING; 81972.D7KW77; -.
DR   EnsemblPlants; fgenesh2_kg.2__373__AT1G60890.1; fgenesh2_kg.2__373__AT1G60890.1; fgenesh2_kg.2__373__AT1G60890.1.
DR   Gramene; fgenesh2_kg.2__373__AT1G60890.1; fgenesh2_kg.2__373__AT1G60890.1; fgenesh2_kg.2__373__AT1G60890.1.
DR   eggNOG; KOG0229; Eukaryota.
DR   HOGENOM; CLU_004312_6_4_1; -.
DR   OrthoDB; 340426at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
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:SF25; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE 8; 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:UP000008694};
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          266..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   769 AA;  87546 MW;  5E653941C86B0DE2 CRC64;
     METRPVEREF SNGDVYFGQL KGTLPHGKGK YAWPDGIVYE GDWEEGKISG RGKLMWSSGA
     KYEGDFSGGY LHGFGTLTLP DGSVYAGAWR MNVRHGLGRK EYCNSDVYDG SWREGLQDGS
     GSYSWYNGNR FIGNWKKGKM SGRGVMSWAN GDLFNGFWLN GLRHGSGVYK YADGGFYFGT
     WSRGLKDGSG VFYPAGSKHP SLKKWHRHFG YDDTGNFLLS HNSTTNIDDL RTSKAVSRSL
     SELTTTSGLT RTSERYPDDY WSTSDPPRDF LHHGPSSKSA RSVDSGQSEI RDKNPIVFER
     EYMQGVLIKE RIMSSIDMSH RARPLNLTKE VTVSTCVSFL GGKWNHYLML NLQLGIRYTV
     GKITPVPPRE VRASDFSERA RIMMFFPRNG SQYTPPHKSI DFDWKDYCPM VFRNLREMFK
     LDAADYMMSI CGDDGLREIS SPGKSGSIFY LSHDDRFVIK TLKRSELKVL LTMLPRYYEH
     VGNYENTLIT KFFGVHRIKL KWGKKVRFVV MGNMFCTELK IHRRYDLKGS TQGRYTEKNK
     IGEKTTMKDL DLAYEFHMDK LLREALFKQI ILDSSFLESL QILDYSLLLG LHFRAPDPLT
     DILEPPNEIS DQESDSVASV DVSLPREPAI PPKGLLMVTH EPNSVNTAPG PHIRGSTLRA
     FSVGEQEVDL ILPGTARLRV QLGVNMPAQA HHKLRQDKEE SGTVELFEVY DVVVYMGIID
     ILQEYNMKKK VEHTCKSMKY DPMTISAIEP TLYSKRFIDF LLKVFPEKA
//
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