ID A0A1V9YTQ9_9STRA Unreviewed; 736 AA.
AC A0A1V9YTQ9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Phosphatidylinositol kinase (PIK-G2) {ECO:0000313|EMBL:OQR89020.1};
DE Flags: Fragment;
GN ORFNames=THRCLA_09963 {ECO:0000313|EMBL:OQR89020.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR89020.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQR89020.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR89020.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR89020.1}.
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DR EMBL; JNBS01002899; OQR89020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9YTQ9; -.
DR OrthoDB; 52727at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd15760; FYVE_scVPS27p_like; 1.
DR CDD; cd00821; PH; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; PTHR47794; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR PANTHER; PTHR47794:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OQR89020.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Transferase {ECO:0000313|EMBL:OQR89020.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 75..177
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 229..281
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 716..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 736
FT /evidence="ECO:0000313|EMBL:OQR89020.1"
SQ SEQUENCE 736 AA; 83230 MW; 4539CB4FC4B32950 CRC64;
MADEPKARPG SVPVLHTLLL DDPLVISRNS APAALIEELP SPASSPSVYS VSPSNFTASE
QLASNLVGST TEITSFGLCG FLNMRENGPG IHRMRRYYCR LIGVLFYRFF SKEQSRDLSN
AHMEAEVQKI EEWDGKGMMH LYRNAFRLTT SHGVFNVAAD SEKEKALWKQ YVNEAIEAAQ
LQMRDAALLA HSQSLLAASP GGLTLFRSNK EKEKPPKFKG QPTCAHPKCT VRFDNTKRQH
HCRNCGDSLC SDHSYHFAPL PHLPTLSGPQ RQCTRCFRVH RFTQLLRCIL QVFVKNRHQR
NSPRSTTLRH SRMATEDVAI LQTVKEAINE PDFGVSDAIQ ALHLHRKDSD EVYRVIVQKL
LSLSATHMPD FEFFLPQLFH LWASTEYELY IVKWTLLLRL LMTAAMYHVR LATSIHWLMR
ATIDDACGWG FGQSELNIPE YLKNRFAPCK LALFNLHMLV YQNDGQHNFK FQPDEDLRTM
PIQTDLIQTY FDRLLALQQY DEGQNAVTPD FVPSSTHFFP VSTPSNGSVR SNSALLLGPL
YAAVASCVLP PSWNFDTGNR VRLSPRLPSL EQSVFSTQLR FIDRLGKLAE ALRGVTPVSR
KEALPDQLAQ LTLPEYAYYP LGTCDEPLRR FVSICIKEGT VFTTKARAPT LIWFEVENMQ
NVPETLWLTP AQATYSHVEN EAPPQTLQTA LNHDEIGQVL RHDNIMSSLH TIEALQPLND
DEEDDESVDG TDALPP
//
