ID D2V885_NAEGR Unreviewed; 1262 AA.
AC D2V885;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC47134.1};
GN ORFNames=NAEGRDRAFT_65065 {ECO:0000313|EMBL:EFC47134.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC47134.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC47134.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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DR EMBL; GG738856; EFC47134.1; -; Genomic_DNA.
DR RefSeq; XP_002679878.1; XM_002679832.1.
DR AlphaFoldDB; D2V885; -.
DR STRING; 5762.D2V885; -.
DR EnsemblProtists; EFC47134; EFC47134; NAEGRDRAFT_65065.
DR GeneID; 8861179; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_65065; -.
DR eggNOG; KOG0229; Eukaryota.
DR InParanoid; D2V885; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IEA:InterPro.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00139; PIPKc; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR23086:SF8; PHOSPHATIDYLINOSITOL 5-PHOSPHATE 4-KINASE, ISOFORM A; 1.
DR PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF01504; PIP5K; 1.
DR Pfam; PF13181; TPR_8; 3.
DR SMART; SM00330; PIPKc; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00781}.
FT DOMAIN 226..581
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REPEAT 1060..1093
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 1220..1245
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1262 AA; 145508 MW; 2F0B70366F9E5F76 CRC64;
MISDKSLTSN LITDRKRRYQ HSKKAEGGSS SSDSLCSSEN SNKRRSSASE TNIGEIILDG
VSNERTTPRS LVDPLPPPST TTALVQSEIS SQAGESFNED LLTCYDESGS EIDEEDEEWN
DYDSIPMSDS QANLVDDDSQ EAQKKKNAVK VPKINLQQTT RMDRFDSTSF VTDRFTETSR
TDEQKTSRAS RGNSLEFRKR LNSLLKKENK TDMYMTNMQE LIENSQNKLG EEVNSSDKDY
EIMKIINRGT DRLIHKISLD EDDQEIKDLE SEYSTDEVYI FRDIGAEFKV FCPSVFQHLR
KLFKVSEFDF KKQMGCHTGN YSRVGTPGKS GAFFFITKST GYLLKSVTEE ELATALEMLP
NYHKHVQKNP YTLLSNFYLL FEITLKQTKY RFIVMNNVFF TPLTIHRKYD LKGSTAGRVA
SESERKKKSP ILKDKDINQG DVKLNLTLKQ NFYRRLENDI IFLQENDIMD YSLLLGIHNH
EQRSSEENRM VSKFRLPQPD DTSFSGRQKN YCSSLDGKEI YFLGIIDILQ RYNSRKQVEK
VVKSGMQSLK AKIRNVTKEK VSVEKPFKYG QRFENFLKIL CSTVSLKDFK PGTPKSYNQR
KDISEEFYHI LIRESPKDFK AFFFRGLFYH NPRVGDMVNA VSDYTKSIKL NPQYSNVSSY
LFRSLLYLTA ANSILEKRGD EIRYAKYANF AFKDLMKLIE MNQYCADAYL LRGVLWMYKF
KYHLLFGKST QEEKIGTVKE SGLAQFYYKK NFAVFSGIDI ASITDLYTCL GDANSKVANN
FAMIRNLGSI RKIIDGVKEN ERVLFYPRNG KISINIRSET LVLNYRLGND NSSISTAKSS
KSIEDSENEV EKEKQEFIRS ILEYVHHQDE QLYKLAERDL LKSIQINPSL HDPYGFQKMS
QRLDLEYYNA YIQLATLYLD LDRPDDAEKI LSESVKKAEK KSHASYFMRG NIYACKYLAL
DDRPETKDKA KEYLTLAIED YNKCLSLDPN CYKAWYNMAS LYKSENPEKA EECYTKCIEI
SEGFYFAIHS RALLYKNVLL QKEKAIIDFT QCITLDPLNT TCYILRANTY LDMNNLQSAE
MDFKQAIHVD PNCSSAYYEL AKLNMNNEEK LNNISSFTLQ DSEIANDLLL LNSLSNNTNE
DGDENIIELS DEENENSENI DDGEDEVLED EEEEYLESET ELLRSLMTAC RIGDVNEVKR
CISTNRVDIN QHDPKSIYGT PIMRAISDGH IEVVKVLLNG GADISRLGWD KDAVSFFKLN
EF
//
