ID A0A061GSN9_THECC Unreviewed; 1842 AA.
AC A0A061GSN9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN ORFNames=TCM_037451 {ECO:0000313|EMBL:EOY30134.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY30134.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY30134.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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DR EMBL; CM001887; EOY30134.1; -; Genomic_DNA.
DR EMBL; CM001887; EOY30137.1; -; Genomic_DNA.
DR STRING; 3641.A0A061GSN9; -.
DR EnsemblPlants; EOY30134; EOY30134; TCM_037451.
DR EnsemblPlants; EOY30137; EOY30137; TCM_037451.
DR Gramene; EOY30134; EOY30134; TCM_037451.
DR Gramene; EOY30137; EOY30137; TCM_037451.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_000480_3_1_1; -.
DR InParanoid; A0A061GSN9; -.
DR OMA; SWIPRRT; -.
DR Proteomes; UP000026915; Chromosome 9.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010256; P:endomembrane system organization; IEA:EnsemblPlants.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IEA:EnsemblPlants.
DR GO; GO:0007033; P:vacuole organization; IEA:EnsemblPlants.
DR CDD; cd03334; Fab1_TCP; 1.
DR CDD; cd15725; FYVE_PIKfyve_Fab1; 1.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR044769; PIKfyve_PIPKc.
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; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45748; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR PANTHER; PTHR45748:SF21; 1-PHOSPHATIDYLINOSITOL-3-PHOSPHATE 5-KINASE; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 36..102
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1472..1809
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 132..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1842 AA; 203732 MW; 5B0D2DEC4692D19D CRC64;
MGNPDNKLSD LVDIVKSWIP RRSEPPNVSR DFWMPDQSCR VCYECDSQFT VFNRRHHCRL
CGRVFCAKCT ANSVPAPSDV QRAGQEDSER IRVCNYCFKQ WEQWIAAVDT GTNAHSPGLS
PSPSATSLAS TKSSCTCNSS SSTVGSTPYS TGPYHRVNYN SGLSPRESSQ MNASATEQNN
KASGTSTNPS SAAVDSSSNH FGLCDNRSDD EDDDYGAYHS DSESRHYAHA EDYYGAINIG
SIDRVYGSDK VHPDGGNMDT KSLSGSPLPE NFNAQSVDGI KKFEEVNERE NADEGEVPAY
DVDGTDVEPV DFENNGLLWL PPEPEDEEDE RESALFDDDD DDEGASGEWG YLRSSNSFGS
GEYRSRDKSN EEHRRAMKNV VEGHFRALVA QLLQVENLPV GDEDGGDSWL DIITYLSWEA
ATLLKPDTSK GGGMDPGGYV KVKCIASGRR NESSVVKGVV CKKNVAHRRM TSKIDKPRFL
ILGGALEYQR ISSHLSSFDT LLQQEMDHLK MAVAKIDAHH PNVLLVEKSV SRHAQEYLLA
KDISLVLNIK RPLLERIARC TGAQIVPSID HLTSPKLGYC DVFHVEKFLE EHGSAGQGGK
KLTKTLMFFD GCPKPLGYTI LLKGANGDEL KKVKHVVQYG VFAAYHLALE TSFLADEGAT
LPELPLKSPI TVALPDKPAS IDRSISTIPG FTVPSSGKPM ASQPINELQK SNKVVISDRP
SSANVEPPCE SRGASSSCLS KGLHTQTTLK EYASSSIEAI TSLNSLSALR ENISSHGNVL
SLNHAFSKVN GIDPKESVQT KTASSEAVMD DGFISICQSL LEAPDQGGGS NHTDGNMLVA
NHLGVPQLAS SKRDTSNNNE EVGSSKEEFP PSPSDHQSIL VSLSTRCVWK GTVCERSHLF
RIKYYGNFDK PLGRFLRDHL FDQSFRCRSC EMPSEAHVHC YTHRQGSLTI SVRKLPELPL
PGQREGKIWM WHRCLRCPRA NKFPPATRRI VMSDAAWGLS FGKFLELSFS NHAAASRVAS
CGHSLHRDCL RFYGFGRRVA CFRYAAIDVH SVYLPPPKLE FNYDNQEWIQ SEANEVTNRA
EFLFREVYNA LQKMSEKLLG PGFQDGGIKS PEKRICIEEL EAMLQKDREE FQESLQEVLC
KEVKVGQPVI DILEINKLQR QILFLSYVWD QRLIHAFSSI VNNIQEVMSS SIPKLGLKPV
SSVEKLVEIN VSPKPSKALS SCDSALVQTK PDININQEGN TGEISEPGGD HREKGMDQDL
NSRNEAESSL SCSANTSEKS DSLESGKVVR RALSEGEFPI MANLSDTLEA AWTGESHPAS
VGPKENGYSV SDTVVVDLST AANSDMGNRT SDRGEVEVAC SPQSALPTKG PENMEKTMSW
ASMPFPNFYS LFNKNSSFNA QKLSISEYNP VYVSSLRELE RQSGARLLLP IGVNDTVVPV
YDDEPTSIIA YALVSSDYYS QMSELEKPKD AADSAVSSSL FDSVNLLLLN SFNDSSSDTF
RSFGSGDESI LSISGSYSSL VSDPLLDTKN FHARVSFTDD GPLGKVKHSV TCYYAKWFES
LRRTCCPSEL DFIRSLSRCK KWGAQGGKSN VFFAKTLDDR FIIKQVTKTE LESFIKFGPA
YFKYLSDSIS TRSPTCLAKI LGIYQVSSKY LKGGKESKMD VLVIENLLFR RNVTRLYDLK
GSSRSRYNPD TSGSNKVLLD QNLIEAMPTS PIFVGSKAKR LLERAVWNDT SFLALIDVMD
YSLLVGVDEE KHELVLGIID FMRQYTWDKH LETWVKISGI LGGPKNASPT VISPQQYKKR
FRKAMTAYFL MVPDQWSPPT IVPSRSQTEL CEENAQGDNS VE
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