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Database: UniProt
Entry: R0IR32_9BRAS
LinkDB: R0IR32_9BRAS
Original site: R0IR32_9BRAS 
ID   R0IR32_9BRAS            Unreviewed;       770 AA.
AC   R0IR32;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase {ECO:0000256|PIRNR:PIRNR037274};
DE            EC=2.7.1.68 {ECO:0000256|PIRNR:PIRNR037274};
GN   ORFNames=CARUB_v10008368mg {ECO:0000313|EMBL:EOA39723.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA39723.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
RN   [2] {ECO:0000313|EMBL:EOA39723.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Schmutz J., Prochnik S., Nordborg M., Weigel D., Rokhsar D., Wright S.;
RT   "Genome sequencing of Capsella rubella.";
RL   Nat. Genet. 0:0-0(2013).
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; KB870805; EOA39723.1; -; Genomic_DNA.
DR   EMBL; KB870805; EOA39724.1; -; Genomic_DNA.
DR   RefSeq; XP_006306825.1; XM_006306763.1.
DR   RefSeq; XP_006306826.1; XM_006306764.1.
DR   AlphaFoldDB; R0IR32; -.
DR   STRING; 81985.R0IR32; -.
DR   GeneID; 17900441; -.
DR   KEGG; crb:17900441; -.
DR   eggNOG; KOG0229; Eukaryota.
DR   OrthoDB; 340426at2759; -.
DR   Proteomes; UP000029121; 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:SF104; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE 7; 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:UP000029121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037274}.
FT   DOMAIN          345..766
FT                   /note="PIPK"
FT                   /evidence="ECO:0000259|PROSITE:PS51455"
SQ   SEQUENCE   770 AA;  87950 MW;  B8B658E999E8F046 CRC64;
     MDMRSGDREF PNGDFYSGEV KGLLPHGKGK YVWSDGTTYE GDWDQGKISG KGKLIWSSGA
     KYEGDFSGGY LHGYGTMTSP DESVYCGTWR MNVRHGLGRK EYCNSDLYDG SWKEGLQDGR
     GSYSWTNGNR YIGSWKKGKM CERGVMRWAN GDLYDGFWLN GFRHGSGVYK FSDGCLYYGT
     WSRGLKDGKG VFYPAGSKQP SLKKWCRSLE YDDTGKFVLS RSASVNVEEL RSSKTVTRSL
     SVETSAGEMT NSGRISDRLT DDIWKSCDPP RDFTCHGPLS KSARFSRSGE SEGQDKNRIV
     YEREYMQGVL IRETIMSSVD RSHKIKPPHR PKEVRARSLL TFLRGEHNYY LMLNLQLGIR
     YTVGKITPVP RREVRASDFG KNARTKMFFP RDGSNFTPPH KSIDFSWKDY CPMVFRNLRE
     MFKLDAAEYM MSICGDDGLT EISSPGKSGS IFYLSHDDRF VIKTLKKSEL QVLLKMLPKY
     YEHVGDHENT LITKFFGVHR ITLKWGKKVR FVVMGNMFCT ELKIHRRYDL KGSSQGRFTE
     KIKIQEKTTL KDLDLAYEFH MDKLLREALF KQIYLDCSFL ESLNIIDYSL LLGLHFRAPG
     QLNDILEPPN AMSDQESVSS VDVGLTQEIY IPPKGLLLVT HEPNSVNTAP GPHIRGSTLR
     AFSVGEQEVD LILPGTARLR VQLGVNMPAQ AHHKLIEDKE ESATIELFEV YDVVVYMGII
     DILQEYNTKK KVEHTCKSLQ YDPMTISVTE PAIYSKRFVN FLHKVFPEER
//
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