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Database: UniProt
Entry: I1M0S1_SOYBN
LinkDB: I1M0S1_SOYBN
Original site: I1M0S1_SOYBN 
ID   I1M0S1_SOYBN            Unreviewed;       752 AA.
AC   I1M0S1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
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   Name=100775866 {ECO:0000313|EnsemblPlants:KRH20721};
GN   ORFNames=GLYMA_13G196700 {ECO:0000313|EMBL:KRH20721.1};
OS   Glycine max (Soybean) (Glycine hispida).
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=3847 {ECO:0000313|EMBL:KRH20721.1};
RN   [1] {ECO:0000313|EMBL:KRH20721.1, ECO:0000313|EnsemblPlants:KRH20721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH20721};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH20721.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH20721}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH20721};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH20721.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH20721.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) 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; CM000846; KRH20721.1; -; Genomic_DNA.
DR   RefSeq; XP_003542821.1; XM_003542773.3.
DR   AlphaFoldDB; I1M0S1; -.
DR   SMR; I1M0S1; -.
DR   STRING; 3847.I1M0S1; -.
DR   PaxDb; 3847-GLYMA13G26670-1; -.
DR   EnsemblPlants; KRH20721; KRH20721; GLYMA_13G196700.
DR   GeneID; 100775866; -.
DR   Gramene; KRH20721; KRH20721; GLYMA_13G196700.
DR   KEGG; gmx:100775866; -.
DR   eggNOG; KOG0229; Eukaryota.
DR   HOGENOM; CLU_004312_6_4_1; -.
DR   InParanoid; I1M0S1; -.
DR   OMA; FYIGEWC; -.
DR   OrthoDB; 340426at2759; -.
DR   Proteomes; UP000008827; Chromosome 13.
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; 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:SF113; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE 6; 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; 2.
DR   SMART; SM00698; MORN; 7.
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:UP000008827};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037274}.
FT   DOMAIN          353..749
FT                   /note="PIPK"
FT                   /evidence="ECO:0000259|PROSITE:PS51455"
FT   REGION          295..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  85284 MW;  4164CAD86E5B201E CRC64;
     MNKELTSFVK AWEAAVRKSA GPKRRANSIF TPMSVAHVDD DDDATRNVVG EVEKILPNGD
     FYTGQWLDNN GPHGQGKYLW TDGCMYVGEW QKGGIMGKGR FSWPSGATYE GDFKGGYMDG
     KGTFIGSSGD TYKGCWVMEL RHGQGTQSYP NGDFYDGEWR KGLQNGHGRY QWKNGNHYIG
     QWRNGLFHGN GTMMWSNGNR YDGCWEEGLP KGNGTFRWGG DGSFYVGVWS KDPKEQNGTY
     YPSGSCAGHL EWDPQELFSL DLVECSVCGL EKVAIYPSHK SLNMLEGDNK MCKKGTDGTG
     RTRRMSVDAR ISNYSSEDGS YSSYNGSRSS QVDNSIPRVP HLRLKAPKRQ GETISQGHKN
     YELMLNLQLG IRHAVGRPAP STSLDLKSSA FDPKEKVWTK FPPEGSKHTP PHQSCEFRWK
     DYCPVVFRAL RKLFKVDPAD YMLSLCGNDA LRELSSPGKS GSFFYLTNDD RYMIKTMKKS
     EVKVFLRMLP GYYKHVRAFE NTLVTKFFGL HCVKLTGTAQ KKVRFVIMGN LFCSQYPIHR
     RFDLKGSTFG RTTDKPESEI EPTTTLKDLD LNYIFRLRKS WFQEFCRQVD RDCDFLEHER
     IMDYSMLVGL HFRGMSCGDN VTPSGHSPGP QTPTGHGNFD DGAPRLSGVD VDHLVVDPNR
     WIQLGISMPA RAEMTVRKSC DTPQLVGEPT GELYEIIIFF GIIDILQDYD ISKKLEHAYK
     SFQYDPTSIS AVDPRLYSKR FRDFIFRVFV ED
//
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