ID A0A022PV00_ERYGU Unreviewed; 783 AA.
AC A0A022PV00;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase {ECO:0000256|PIRNR:PIRNR037274};
DE EC=2.7.1.68 {ECO:0000256|PIRNR:PIRNR037274};
GN ORFNames=MIMGU_mgv1a001627mg {ECO:0000313|EMBL:EYU18633.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU18633.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU18633.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(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; KI632325; EYU18633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022PV00; -.
DR STRING; 4155.A0A022PV00; -.
DR eggNOG; KOG0229; Eukaryota.
DR PhylomeDB; A0A022PV00; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
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; 2.
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:SF29; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE 4; 1.
DR PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1.
DR Pfam; PF02493; MORN; 7.
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; 1.
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:UP000030748};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037274}.
FT DOMAIN 390..779
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 88676 MW; 25168C38E68B0AC5 CRC64;
MKAWEATVRK TQAAAKKRAN TIFGTSYAVD PNIVAGAGAG EGEEENESDH HPNHEEDEFH
ASGEVYHAER FLPNGDYYTG YWADNFPHGQ GKYWWTDGCM YVGEWFRGKS MGRGIFSWPS
GAMYEGNFKS GFMDGEGTYT GAIGGTYRGA WVMNLKHGHG VKEYVNGDSY EGDWSRGSQE
GQGKYQWKNG NHYVGEWKNG KICGHGTMHW TNGNVYEGNW EDGLPKGNGT FKWPDGSFYV
GHWSSDPGEQ NGTYYPSGSL LEGGNLEWDP QEVFSKDLKE CKVCATEKVP IWPSQKKLAV
WRSSKGSDPS VRPRRMSVDG RIDAGVDKDL GGMRLSDGAA PSPWNVSAVD RAGNEGDDVF
VGLQCEGMMN LRGTPLRIPK MVKRQGETIS KGHRNYDLML NLQLGIRHSV GRPGPPPSLD
LKPSAFDPKE KFWTKFPPEG SKITPPHQSC EFKWKDYCPK VFRTLRMLFK VDAADYMLSI
CGNDALRELS SPGKSGSFFY LTNDDRYMIK TMKKAEVKVL LRMLNAYYNH VRAFENTLVT
KYYGLHCVKL NGQKVRFIIM GNLFCSEYMI HRRYDLKGST FGRLTDKPES EIDANTTLKD
LDLNFIFRLQ KTWFQEFRRQ VDRDCEFLEQ ERIMDYSLLV GLHFMEASND DITPSGSVTP
IDNGGSDEAV PRLSRADVDQ LLLDPAGWAS IRLGINMPAR VERTERNNDA AEFQLVGEPT
GEYYDVILFF GIIDILQDYD ITKKLEHAYK SIQYDPNSIS AVDPKQYSRR FRDYVLKAFA
EDT
//
