ID A0A0D3BB95_BRAOL Unreviewed; 1761 AA.
AC A0A0D3BB95;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN Name=106334573 {ECO:0000313|EnsemblPlants:Bo3g066070.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo3g066070.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo3g066070.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo3g066070.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_013628325.1; XM_013772871.1.
DR RefSeq; XP_013628326.1; XM_013772872.1.
DR RefSeq; XP_013628327.1; XM_013772873.1.
DR STRING; 109376.A0A0D3BB95; -.
DR EnsemblPlants; Bo3g066070.1; Bo3g066070.1; Bo3g066070.
DR GeneID; 106334573; -.
DR Gramene; Bo3g066070.1; Bo3g066070.1; Bo3g066070.
DR KEGG; boe:106334573; -.
DR eggNOG; KOG0230; Eukaryota.
DR HOGENOM; CLU_000480_4_0_1; -.
DR OMA; QEKVVEW; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000032141; Chromosome C3.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd03334; Fab1_TCP; 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:SF7; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000032141};
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 40..106
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1402..1728
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 112..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1068..1099
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 117..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..343
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1761 AA; 196685 MW; E995A58E35A021B2 CRC64;
MDTRDSSSNK TLSEIVGLVK SWIPWRSEPA TVSRDFWMPD QSCRVCYECD CQFTLINRRH
HCRLCGRVFC GKCTANSIPL AGSDLRAPRE EWERIRVCNY CFRQWEEQGD GGAHVSNVPE
LSTSPSESSL LSSKTSTTAN SSSFALGSMP GPAVPYQRAQ RGSDVSLHGV SSMEAGTTRK
GKETSRRNSF IATDVQDPSR FASNRSDDEY DEYGVYQTDI DTSHSPQANQ YYGPMEYEET
SIGGDGPCKH LSGETSDQKS LSGSPLIHHC LESLIGEGAE QFQKKDEHDG RDESEAPSPP
DDQVAEPVDF ENNGLLWVPP DPENEEDERE SPLYDEEDNE GEASGEWGYL RPSASFGSGE
YRSEDRTSEE HKKAMKNVVD GHFRALLAQL LQVENIPVSD EEGKESWLEI ITSLSWEAAN
LLKPDMSKSG GMDPGGYVKV KCLASGFRHD SMVVKGVVCK KNVAHRRMRA KIENARLLIL
GGGLEYQRVS NQLSSFDTLL QQEKDHLKMA VAKIHAERPN ILLVEKSVSR FAQEYLLAKD
VSLVLNIKRP LLDRIARCTG AQIIPSVDHL SSQKLGYCEN FRVDRFLEEH GSAGQAGKKV
VKTLMYFEGC PRPLGFTILL RGANEEELKK VKHVVQYGVF AAYHLALETS FLADEGASPE
LPLNSPITVA LPDKSMSIER SISTVPGFMV SAYEKSPTML TGSEPQRANS VPASELLSTT
ANVSIQKDIN PLIPNGSGWQ GREGTPGFTF SRYNVPLNLP DRLIAGRNAD FSERSALADK
SNPTDILDSS LHSSGQGVVP QSSQSSKSVV VENQDNGTEF MAIQQQNSET PKEPQSQKEE
FPPAPSDHQS ILVSLSSRSV WKGTVCERSH LFRIKYYGSF DKPLGRFLRD HLFDQGYRCR
SCEMPSEAHV HCYTHRQGSL TISVKKLQDC LLPGEKEGKI WMWHRCLRCP RPDGFPPATL
RVVMSDAAWG LSFGKFLELS FSNHAAASRV ACCGHSLHRD CLRFYGFGNM VACFRYATID
VNSVYLPPSV LSFNYDNQDW IQRETDEVVE RAELLFSEVL NAISQIAAKG FRRRIGELEE
LLQREKAEFE DNIQKMMLQR EVKEGQPQVD ILELYRLRRQ LIFQSYMWDH RLINASSLSK
IECSDENEKV PLAKSQTLPE MNAGTNSLLS GSEVDQNPDG GSTDDTKVQK EADTNLDMNP
EKEDGGEVSP SKTLPDSSEP LESKLDVRRT QSDGEIVTKN LSATLDAAWI GERQTSGEIP
TNTKILLPPS NSSTFPPIDL PEQQNEFKVA YPVSPALPSK DYESSEDSVS WLGVPFLNFY
RSINKNFLLS SQKLDTFGEH SPVYISSFRE AELRGGPRLL LPVGINDIVV PVYDDEPTSM
IAYALTSPEY QRQISVEGES LVSYTSELNI PRPVDDTIFD PSRSTSSVDE NILSMSSSRS
LDPLSYTKAL HARVSYGEDG TLGKVKYTVT CYYAKRFEAL RGICIPSELE YIRSLSRCKK
WGAQGGKSNV FFAKTLDDRF IIKQVTKTEL ESFIKFAPAY FKYLSESIST KSPTCLAKIL
GIYQVATKQL KSGKETKMDV LIMENLLFGR TVKRLYDLKG SSRARYNPDA SGSNKVLLDQ
NLIEAMPTSP IFVGNKAKRL LERAVWNDTA FLALGDVMDY SLLVGVDEEK NELVLGIIDF
LRQYTWDKHL ESWVKFTGIL GGPKNEAPTV ISPKQYKRRF RKAMTTYFLM VPDQWSPPNV
IANNSRSDQP EETSQAGTQA E
//
