ID A0A0D9VV05_9ORYZ Unreviewed; 1784 AA.
AC A0A0D9VV05;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR03G17690.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR03G17690.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR03G17690.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR03G17690.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-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 EnsemblPlants; LPERR03G17690.1; LPERR03G17690.1; LPERR03G17690.
DR Gramene; LPERR03G17690.1; LPERR03G17690.1; LPERR03G17690.
DR Proteomes; UP000032180; Chromosome 3.
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:SF3; 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:UP000032180};
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 35..100
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1436..1755
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1784 AA; 200371 MW; 36D5F3632CA39331 CRC64;
MEADKTFADV VKLVTSWLPR RSNPDNVSRV FWMPDHSCRV CYDCDTQFTI FNRRHHCRRC
GRIFCGKCTT NSIPASSGPD RNIDEGDRIR LCNFCFKQWE QEKAAALKQV MPVLSPSLSE
ASLFSTKSTI TINSVSTTAG SYSTGHYQHV ARASSISPPK SSQDKVSHNM LDTHVHEKSM
VSTVSNKDET SSVQFGYYTN RSDDEEEECA AYCSDRHVPH QQHNDNYYGP DEFDELDSSY
NPTISQTVEE NVISKEVSPH AAQGFPSTLP VTKVEDEHDP DNNDEEDEME VGFFDDGDED
EPVADNEQCR IRSSSSFSSG EFRSRDRSSE EHKKVMKNVV DGHFRALISQ LLLVENISSH
EGDETGWLEI VTSVSWEAAN FLRPDTSQGG GMDPGGYVKV KCLACGHRSE STVVKGVVCK
KNVAHRRMTS RIEKPRLLLL GGGLEYHRVT HQLSSIDTLL QQETDHLKMA VAKIAAQKPN
LLLVEHSVSR YAQDLLLEKN ISLALNIKKP LLERISRCTN AHIVPSIDYL PSQKLGHCEL
FYVDKYVEHS VNSNNTAKKM PKTMMFFEGC PKPLGCTVLL KGGSLDELKK IKHVVQYGIF
AAYHLALETS FLADEGATLP ETPLKSPLTV ALPDNRSTAD GSISTVPGFR FNVSNNQQPT
DNFEHLAASS IRATDPDRSA VPPVSSECTT QSQTSCSHSS GTWPAIDGRL NNKTVDEIEK
ATAISDSAST SGVLMNHSYI YSALEKNWYS GDYHEYGSTR SDVKIMMTDL ANSNSSCHHG
TSEASTNITS FANLKDPFDG SVDLVKMGNV TNSNLVMVRP VPSPAAQNQE TNQGHEITSN
KEEIMASDHQ SILVSLSIRC VWKGTICQRS HMLRIKYYGN FDKPLGRFLR DCLFNQGFQC
NSCDKPPEAH VHCYTHQQGS LTISVRKLTE FVLPGERDGK IWMWHRCLKC PWSNGFPPTT
LRIVMSDAAW GLSLGKFLEL SFSNHAAASR VASCGHSLHR DCLRFYGFGK MVACFRYAPI
NVHSIHVPPH KLDFSHQPLD WIQKEANEVI DRAKTLFDEI SRALHQHSDK KAHTLNVDCS
NYIAYLECLL RKERLEFEGC LNKVLKKETQ NFQPDILEIN RLRRQLLFHS YLWDQRLIAA
AKSDRSRQEL YSFRPVDKEV IQSIDTVAEL NAIEKPQNKI SATEVSFKDH KFVEFLHESN
DGGTTPRVYQ CNICPNHDQQ IAISESDSIQ RGSKTPLYSS VSINADSVPL EPDLVARRTL
SEGQFPSLLD VSNALDAKWT GENDPVADST TMPDCVSSSE DSEEHVTDTT PSYASVLLNK
LGDSAEDQPN WLRMPFLQFY RSLNKQCSRS YRFDVLNEYT PVHVSFLRTV ERQVGPKFFF
PIGVNDTVVG VYDDEPTSII SYALASHEYH LQLSEELESD TTDNSLSVID SRSASVTESV
DETTSELLRS FVSADDNILS ISGSKNPPPS DPLAHRKVSH IKVNFGDEGP LGQVKYTVIC
YYAKKFDALR RICCPSERDF VRSLSRCKKW GAQGGKSNVF FAKSLDDRFI IKQVTKTELE
SFMKFAPEYF GYISESIVTG SPTCIAKILG IYQVKSLKGG KEMRMDVLVM ENLLFERHVT
RLYDLKGSTR SRYNADSNGS NKVLLDQNLL EAMPTSPIFV GNKAKRLLER AVWNDTAFLA
SIDVMDYSLL VGVDEKKHEL VMGIIDFMRQ YTWDKHLETW VKTSGILGGP KNVAPTVISP
KQYKKRFRKA MSTYFLVVPD QWSPTAVVPN KQLANYRNTP NKPR
//
