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Database: UniProt
Entry: A0A024G8S9_9STRA
LinkDB: A0A024G8S9_9STRA
Original site: A0A024G8S9_9STRA 
ID   A0A024G8S9_9STRA        Unreviewed;      1256 AA.
AC   A0A024G8S9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=PIPK domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN9_037040 {ECO:0000313|EMBL:CCI42920.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI42920.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI42920.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI42920.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:CCI42920.1}.
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DR   EMBL; CAIX01000041; CCI42920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024G8S9; -.
DR   STRING; 65357.A0A024G8S9; -.
DR   InParanoid; A0A024G8S9; -.
DR   OrthoDB; 5481504at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:InterPro.
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; cd00821; PH; 1.
DR   CDD; cd17300; PIPKc_PIKfyve; 1.
DR   Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR   Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR044769; PIKfyve_PIPKc.
DR   InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR   InterPro; IPR027484; PInositol-4-P-5-kinase_N.
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; PF00169; PH; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51455; PIPK; 1.
PE   4: Predicted;
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:UP000053237};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00781}.
FT   DOMAIN          250..348
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          785..1127
FT                   /note="PIPK"
FT                   /evidence="ECO:0000259|PROSITE:PS51455"
FT   REGION          775..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1218..1256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1229..1249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1256 AA;  144855 MW;  788A3FFEEB9D4BD9 CRC64;
     MCNEIESVVE EVYEIQTFQP FRGWTFERFS DQFGKTFITL TEAAHTLLRE DQCNRHELDL
     NVCANLMNRA KPHTSPTLLD LERSNYGYGS ENHKLNYYEI GCLPNHDWMW SHAWMLDYEF
     LHGEWSYGTS IHGMNRRLAE GTNRAKKSLV DFLRRRRWIR TRIRKPCLEM EESSEHLNEN
     SSNQITVHVN EPEYSMSLSQ NGQYKVKKDS KRHLEKRFYH VFRNAMLAHL NLQSSYRLSN
     INRVEFDADA VEMEGWLGIR GTISRSWKLR YCVLRFDTNS LICLRDRTLF IQVNEIPIDR
     HTSVLLEDSG LNTQHQFSII YGEHKIRLNA TTHASRTAWL EAISGLIVRS RASFVAVEDS
     DSNHSLISKT RRRVRSRITS ELDSNHSDGT VSALSYPSVS SSDLYSEIRQ SKHVHRKKRV
     WRPYTLICSA MSDKRETDSA FRLQYVQKFK STFEKKMKLA STFLNANLNV LEKNMIAISV
     KFSSSYCNHT TEQSMEVVSH LRRDIEKSLE QFYVDGHAKL RADRASVLLC NRLGRDLYLE
     TKRLNDLIVN YAVPATMVTE KKKTPNAPVP RIPTDWFDPA QPKPMLKRCS LSDSTDVTSE
     RAALSDDEME RRRALKTCKS FSEKISHLDF GCTKPKIDNA NPNSQLRYTC LFDSDTTSFD
     RPQRFRSATT TSQPLNTTRS DGSNGTTGCS IFASYEALPD CLSEGQLELP SGINNYVVPI
     WEKDLGSLIA FALCSDAYMR ELEAQFRNCF DIRDELSAEE IDEASRLYYE RRENPKGTKQ
     QIQFGEEEGA PELGSESDTS LSSEHEVSKK DRWLAYMAAM KRNDFQHADI EFAYEDRTAQ
     TKRGVRCIVY FAAQFHALRA LIAPGNFEFL NSILKSMRWD ASGGKSGAFF SLTHDKRYVL
     KGISLTEFNM FHHLAPHYFK YMEQSIHQKT RIVMSRIVGL YKLCRSRRHS KHTTYVVVME
     SMTYGFPPAQ LYDLKGILRR RCNTMEPLAE DGLSIFTKSS DRDQLSLNSS SQLIEVDAVG
     QRVLLDGNLY GSIPIPVRQS DLINCEAAIQ NDTTFLCRAG VVDYSILLML NEKERVMVVG
     LIDYIHQFDF LKKMESTSKA SIMFRNPTII NPNAYQRRFV NAMHRYLVGI DCDMLKTRKS
     ANSTQRTQTN DYRTTLRHTI QLASQTEGDE QCDKNQSIAV DKVKGGRHKH AANKVPRLSN
     SLMDRFIWQN IQKVISRSSS MPSLGRDNTK SRMKQDLRWY SHREEFSSSS EYELGS
//
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