ID A0A0E0B0N7_9ORYZ Unreviewed; 1838 AA.
AC A0A0E0B0N7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM09G04120.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM09G04120.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM09G04120.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR STRING; 40148.A0A0E0B0N7; -.
DR EnsemblPlants; OGLUM09G04120.1; OGLUM09G04120.1; OGLUM09G04120.
DR Gramene; OGLUM09G04120.1; OGLUM09G04120.1; OGLUM09G04120.
DR eggNOG; KOG0230; Eukaryota.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_000480_4_0_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
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: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; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR039429; SHMT-like_dom.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR PANTHER; PTHR45748; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR PANTHER; PTHR45748:SF8; 1-PHOSPHATIDYLINOSITOL-3-PHOSPHATE 5-KINASE; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01504; PIP5K; 1.
DR Pfam; PF00464; SHMT; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00781};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00781}.
FT DOMAIN 1338..1655
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1146..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1838 AA; 206037 MW; F399B5ECD0F49B6C CRC64;
MDGVDDGLIC STSCYKMCGH ADKSSIIDGE IGWPSMEISP CSTPYGTPLF SRESSCSSFA
SCFSSLDDYL VETDSKEEIE VLDTGQLHPS ILFSDESMEQ RKADSVQVEE YQVSHSAVVN
DDSSISIPTN QNNSSGQLQL EIHLDATNEK SVPSNAILDA NVTDPHQEVI SNGGLIEACY
GVPVDDIDLK QSNILDGEEI TSLPMADNEM TPLDDQIMDQ IDDMKEISSI VYNSTISAEQ
HVNSGSEFEK GNESSDNLYP LVMPSFDTDP HIWLPPDPVN KDDDTDIVAN NDDNSDNNGN
WVQSSFNISF DAKRNKTSCE DQLLKAMSEV MNGQFKILVT RFLAAEGLSL SDGEADKNWL
DIVASLSWRA ALLVKPDANV GNAMDPCMYV KVKCIASGSI EQSEVINGLL FKKSAAHKQM
RANMKNPRLL LLQGVVGHSS AGLLSMDSMK QENDHLEKIL SDVIIKCKPD AILVEKAVSR
NVNEYIHKQG VTVVSDMNIR RLERIARCTG SPILLLQNVL ATPNLIKQCE SLHFEKFIEE
HNITGGGKRS AKTLLFLEGF RKPLGCTILL KGSTSEELKK VKRVLHFTVF AAYHLILETS
FFADQRLFAT GKNAMEKGNC LKTDPQLLVP CTAAPSSKFC SDIAQNSDPT QQALNSLASD
GEYVNQDDFV DPEKSVCMHD SKIETSREYA DRKLDDSNNI QSYSSLPVPD PSRNLIGDIS
LDFAKLTSCD DFAGSTSGAP SNNGVLQMNG ADGKDCLEAI SDGISTETRT SLDSQNMLIS
MSSQHIRNQA ICEQSHLSRI TYYGYFDTSL GRYLQDSLLN EKHSCLSCGE PPEAHMYSYT
HHNGTLTVLV KSLPLDVTLS GKDQGRIWMW TRCLRCNGKP TQRVIISSSA RNLSFGKFLE
LSFSTHSAAK KLSTCGRLLH RDCLRFFGMR PKVAMFRYSS VEIYSAFKPP LTLEFHNPNK
RECLEVEFNN VLRKWRVLFS EAENKVQILK SGDSSQALGE NTKASVHDEL FLEVNRILAQ
EKNEFEVYPK TFDLLVKSGT SAHGILGLNW LHQLLLLGIY IWDVRLQHIL QYCKANAASS
DSTIHIKTPE NKPKNYEITS VHGDTLCLTN VGMERLEERI DTCHSFDSSF GGMILENEQL
TEKSVIQEPG SHVSPDHGED GGSHEVDKYA HISDSFCLEK SIDLPVKNEL PELVRGNEMY
PVAKPSKCFH VFLNLLDFSN DARKWIWGSF SHLEKEYKKE LQGGFLDKFH LINKYIPTFS
SLAQLKSQMD MVQFIVGPGG SILSIVEEEA SSMIAYALLI SEQQGMYSEA AIVKDEVIAG
RKIDKVTPIN SIGDTPVPSA ILSPNDSLEQ DHNLSRNVSS LSSEESTSGF YDSFLSALKD
LHPEFCLNNE KLTLKSKYTV LCIYAKQFYD LRKICCPSEI AYISSISRCK EWNAQGGKSK
AFFSKSMDDR FIIKQIKKTE FDSFLKFGLE YFKHFGVSQA SVNPTCLAKI LGIYQVKEIR
NGKETRTNFM VMENFLFGRN IIRRYDLKGA LFSRYVLDSK NPENVLLDQN FIEDMRAMPI
YIEGKTKNLL ERAIWNDTAF LSRMTVMDYS LFVGVDKQKK ELVFGIIDYL RQYTWDKQLE
SWVKTSLFVP KNLSPTVISP KEYKIRFRAF MSQSVTGLLP KDCISWGLSC LLVVMSAVDT
RYCTLSGKLS STSIFIEKLS YKVNPQIGYV NKLEERAKIS TPRFSYVVGA HTPERDFTRM
RIIADKCGAV LMCDPTHISG LVTTTECRSP FDHCDVVTSI NKNLTSPRGG TVFFRRGKKL
RGLFFFLKGM KMNCEFEDRI NFVVFHSIQL CQDRRTPW
//
