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
//