ID A0CSV0_PARTE Unreviewed; 1380 AA.
AC A0CSV0;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
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=GSPATT00010139001 {ECO:0000313|EMBL:CAK73867.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK73867.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK73867.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK73867.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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DR EMBL; CT868163; CAK73867.1; -; Genomic_DNA.
DR RefSeq; XP_001441264.1; XM_001441227.1.
DR STRING; 5888.A0CSV0; -.
DR EnsemblProtists; CAK73867; CAK73867; GSPATT00010139001.
DR GeneID; 5027049; -.
DR KEGG; ptm:GSPATT00010139001; -.
DR eggNOG; KOG0230; Eukaryota.
DR eggNOG; KOG1819; Eukaryota.
DR HOGENOM; CLU_255687_0_0_1; -.
DR InParanoid; A0CSV0; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 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:UP000000600};
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 15..81
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1064..1373
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
SQ SEQUENCE 1380 AA; 161225 MW; C3EABED183D656D3 CRC64;
MINQQLLQTT KWVQDRDAKA CKKCQNPFKA IFRRKHHCRN CGQLFCDSCS NYFMDKTNFK
NYQEIKKNKV RLCQDCYIDI NRKLRASGEV VEDKNSLTVL NSQQLRRHSK SFNVTDEKLP
ESAKQVYIVF RFIKTSPPPP LQLVPQIAID PQPRSQNCKL QIPDTITMGD DIEQKQKKFE
ERMISKVEEF VERRTLAYGI KEKWQGMMLQ FILNAIEYLK QAEILPLKNK ILLIRIKIIP
FIHYASTRYL RGVTITKNIA HKRMKTHHKS PSFLLLTGSL DLDIQNFDNV VKNHNKYLQQ
ALEQIDMLNP NIILIEKGIN NILLNEFLKR DITVSIQCST KQLQKVEVAV KARIQRAADV
FNKCCDKDCL GKSDTAFYES CDPDSIKQNQ TLYSRLDEKD KALLEAHLGK KNKDKTLLFI
HTPQYATSFQ ITLSGPKITE LIDVKKCFQE LCCICYSMSL ELSMILLDQK LKQDLEQNYK
QIDNQKSPMM NSGEISDFSI QSMTEHENQG FKVCKVRFHP AVISTIHDIQ KRNNDQSLEN
YIRQNIKNIN NKKISYFSQF CNFTKEVVKF YENEDFGLGH YISSKAIDTT TKYCSIKQIH
HVSIRYGPGA FVRCVVERKK QQNLQVKASV NLSKEIIKKE QSFLQMQYDE TSTQCEAVQG
DLDYKVHQQL NTNIITYIKC LNANCDRQLT KSFKLERSHL EFSFQKLIQY LIMSALKWKK
LNKTNWLVFE GELNEQGDQF DGCNHNQTER VFECNDFQVK LFTNLFDIYR IKHFQFNCQE
VKQHIEKCDQ EEIDKRRDTL ISHLQKLQQQ ILKNDKSVRS SYMTNSTLSF DKDPNPFIQA
PENSITLIGN FMEKLTQSPF PDFLALEQES MQLYSRIYSI EITDQLRISR IKNDNIISKQ
KTSQFSFVTN ESGPVIKNLS KKILKETTTT LSSINENSFP IQLLPTQQYT QSPESPSQEN
FNQFEDQSEI GFDKQYDNDQ NQQNSIKSFL LNWPKPAINF DQSNMQIKSF FDYIPIYNQN
DIGLVASALN HPKYYDLYEN KYRFTEFWEK IQDQSLQKEV EIEAAKILKD QLKNAVIEEF
QIKLSKFTAL MKKTSLNNLQ EVDEDEQAVI QNTAESPRRP SKSVTIQLYY PKQFECFRML
NGINIKQFIK SIASCSNWNS AGGKSGSTFY KSADNLFIFK AVKESEFSMF ESFAPKYFEH
LYSNIFNQRP SVLNKIYGMF TIKNSRGTSY LIAMENLFWG MEGELTVYDL KGSKAKRWNR
KNLKTLLDTN YIIDRNGEPL PIQEQDFNFL EIALEADSEF LLEVEVVDYS LLLIIDNQNH
QIKLSIIDYL QCYDFMKKME TKLKTAINFG AAPTIIKPAV YKERFIDAMK KYFMGIYSTL
//
