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Database: UniProt
Entry: A0A0B2RET9_GLYSO
LinkDB: A0A0B2RET9_GLYSO
Original site: A0A0B2RET9_GLYSO 
ID   A0A0B2RET9_GLYSO        Unreviewed;       790 AA.
AC   A0A0B2RET9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase {ECO:0000256|PIRNR:PIRNR037274};
DE            EC=2.7.1.68 {ECO:0000256|PIRNR:PIRNR037274};
GN   ORFNames=glysoja_025858 {ECO:0000313|EMBL:KHN30367.1};
OS   Glycine soja (Wild soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN30367.1};
RN   [1] {ECO:0000313|EMBL:KHN30367.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Root {ECO:0000313|EMBL:KHN30367.1};
RA   Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT   "Identification of a novel salt tolerance gene in wild soybean by whole-
RT   genome sequencing.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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; KN651818; KHN30367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2RET9; -.
DR   Proteomes; UP000053555; 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; 3.
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:SF115; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE; 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; 8.
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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037274}.
FT   DOMAIN          397..786
FT                   /note="PIPK"
FT                   /evidence="ECO:0000259|PROSITE:PS51455"
FT   REGION          252..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..693
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  89809 MW;  D45391A8EF4E324C CRC64;
     MIGKDSGVMK AWEATMRKTH AVAKKRANSI FGTISLAHVV DEEENNNNDD YDDDNEENGK
     NETFDVYIEE KVLPNGDYYT GEWANNFPHG LGKYLWTDGC MYVGEWFKGK TKGKGRFSWP
     SGATYEGDFK SGFMDGNGTY TGCNGETYKG QWVMNLKHGH GFKSYANGDW YDGEWRKDLQ
     DGEGRYVWKD ESHYVGEWRN GTIWGKGSFV WAENGKVFEG FWEDGLPKGK GTFKWPNGSF
     YEGNFSKDGK DQNGTYHNSC ESSSDGEEGH SELWDPQELY SELNGYSVCP GEKVQVMPSH
     KRLAVWRSTK TGESAKNRRI SLDGRVSIGL EKPSDRLQIW DGGESDASGA KTPTMGSDLD
     EDLMGLRVDD GGESLGQLQP IKAPKKSKRQ GETICKGHKN YELMLNLQLG IRHSVARPAP
     TASLDLKPSA FDPKEKVWTR FPPEGSKYTP PHPSCDFKWK DYCPVVFRTL RKLFKVDPAD
     YMLSICGNEA LRELSSPGKS GSFFYLTNDD RYMIKTMKKA EVKVLLRMLP SYYNNFRDHQ
     NTLLTKYYGL HCVKLNGPIQ KKVRFIIMGN LFCSEYITHR RYDLKGSSLG RFSDKPETDI
     SETTILKDLD LNFIFRLEKS RFEEFCRQVD KDCELLEQEG IMDYSLLLGI YFKDISPDGE
     IIPLQSRTPV GDSENEANPH TSCEDTDQPP SDPSSVCSII LGMNMPAKVE RTVRRSGCEL
     QLVGEPIGEF YNGVLTFGII DILQDYDISK KLEHAYKSIQ YDPTSISAVD PIQYSRRFRD
     FIFRIFTEDS
//
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