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Database: UniProt
Entry: A0A0V0R7F9_PSEPJ
LinkDB: A0A0V0R7F9_PSEPJ
Original site: A0A0V0R7F9_PSEPJ 
ID   A0A0V0R7F9_PSEPJ        Unreviewed;      1575 AA.
AC   A0A0V0R7F9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=PPERSA_10535 {ECO:0000313|EMBL:KRX10436.1};
OS   Pseudocohnilembus persalinus (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC   Pseudocohnilembus.
OX   NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX10436.1, ECO:0000313|Proteomes:UP000054937};
RN   [1] {ECO:0000313|EMBL:KRX10436.1, ECO:0000313|Proteomes:UP000054937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36N120E {ECO:0000313|EMBL:KRX10436.1};
RX   PubMed=26486372; DOI=10.1038/srep15470;
RA   Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA   Miao W.;
RT   "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT   persalinus provides insight into its virulence through horizontal gene
RT   transfer.";
RL   Sci. Rep. 5:15470-15470(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX10436.1}.
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DR   EMBL; LDAU01000028; KRX10436.1; -; Genomic_DNA.
DR   EnsemblProtists; KRX10436; KRX10436; PPERSA_10535.
DR   InParanoid; A0A0V0R7F9; -.
DR   OMA; CIERMES; -.
DR   OrthoDB; 5481504at2759; -.
DR   Proteomes; UP000054937; 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: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; 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:UP000054937};
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          22..97
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          880..1196
FT                   /note="PIPK"
FT                   /evidence="ECO:0000259|PROSITE:PS51455"
FT   REGION          657..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1287..1311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1335..1371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1388..1423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1448..1495
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1575 AA;  185228 MW;  76F614CD5EDCAE2A CRC64;
     MSRYQEIQPE KFLMPKEKWQ PDEGSKNCFD CNASFNLFRR RHHCRKCGRI FCDSLIKEKN
     VNSFIFVRCS DNFIIGKYFN SDNKKIRFCK ECYRQASEFI QDLLGIDIQE SEDKIQSKSK
     FNDNNNKKNS ENQNSFQNNQ VSIASQQQNE CRNNQNDFQK FQRSFEHDKE DNQLDFVSKK
     ELEDMVMKKI RFLTDYLLGK NICSEKWKNY LFKFLQKSVQ AIIIDSTKHS DKRDICDYVK
     VKKLLLKQDR KNFINYTQGI VCRNNVCNKK MRKNFENPKI LIIASPIEYP AQDTNLENII
     KNERKFIKKV VDQILSLNPD VVFVGASVCK LAIDQLFLNN VTLVYKIKPS ILTKIAKATR
     SKIITELDRL GQIGNHKPLG TCRSLNFTQE QEISKHKDPT LMVLEAHNTY GGVSILIGGQ
     SMEELKKVKR LIQEVLRLGR HLWLEKNMIY TNIQLLNSYR QLDKNRRIDE ICSYGNFSMF
     TDEFLSLEEF IETKKMKYTR INFVRGQIEN FNDIKSKEEL ENYIAQRGNN FNDSKVPYFV
     EICDTVNKDL NFTNHNQDIS LAKYIIKKVD DLQNRCDICK RPKYNHVYIF YHGDTFVRIQ
     AEDKYGLQNQ QKWGVQGNQI QDKQKNVDLF KKKQSELETY FECEKCETVS SLNRLLGQGP
     SNASQSQSQN SNSKRASKVQ SQQGAEQFSG QRISSKKESI ISIVDESGHM QGKHNSHRFK
     IGDLEKSINQ LGNGNLLLDD SGFDFQKYEF IPVFEKEPMS YISWAHNSAQ YMQDVYLKEN
     FNEYEYVFQK EQKMESLNGQ GFSIQKSDFE DDQKLKEFLE QKLNMDYENK QEYNSLETYK
     IDIPLKKKIV FSAIKSQGQQ KVNPELQILK QQIDDLDQEQ QQNLSNSQFT PLQQKPLTLE
     KQISEEILTS NMNNVNMEKK LNSEQQLYLG NIQKKQGGQY EKIGNVTIYF PVQFEALRMC
     NNISLNRFIQ SCLSSSGFET QGGKQNADFF KSADDLIITK VINQAEFKHF KKIALSYFHH
     MYIHRFESKP SLLAKIYGML HVKIQNRDLY MVIMENLFFG IPAKEPYISV YDLKGSETNR
     FLKSVSSTLL DTNYKIDRNS EPLPVNKESY VIIDRALQRD CKFLASADVV DYSLLMIIDK
     KNMSLKMGLI DYLRDFDWAS DIENKYKYLK TLGNVPTIVQ PKKYKSRFLE EFLKRYIVEV
     NFKKDSLQTK KQGEKNMLCE KSLTEIIKQQ DELIKQEIQN KNLISQNQES MEELAEKIQK
     INREQQEKIL SQLREIEMKK RNEIEQEKRR YQEEQQQRLL HHKSKQESHH RENQILENNQ
     QQQIIQDDIQ MGKIQQNGQG NTDNQSKQKR QSEKSVEMVI DQNDDQQLIN SRNNIEKDVI
     INNKNYKNDN INNDDNNGNN NNSQFNQNDL TNINNKSDKN DVQNNFDIKA QNGSIYDKND
     KKQNDDTLQN LELNELDEQQ QLEQFDLQML KQKSLQELED ENEAEQEKIE KMKNASLMKQ
     IDEEYDSSSI SQKDYSDKGY NIENFQQQVE YDSIKQISEN LRKQNLEENY GSNLALQAIQ
     EEEINENIDE LKQKV
//
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