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Database: UniProt
Entry: A0A1V9ZZ88_9STRA
LinkDB: A0A1V9ZZ88_9STRA
Original site: A0A1V9ZZ88_9STRA 
ID   A0A1V9ZZ88_9STRA        Unreviewed;       755 AA.
AC   A0A1V9ZZ88;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Phospholipase A-2-activating protein {ECO:0000313|EMBL:OQS03279.1};
GN   ORFNames=THRCLA_04424 {ECO:0000313|EMBL:OQS03279.1};
OS   Thraustotheca clavata.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Thraustotheca.
OX   NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS03279.1, ECO:0000313|Proteomes:UP000243217};
RN   [1] {ECO:0000313|EMBL:OQS03279.1, ECO:0000313|Proteomes:UP000243217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS03279.1,
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:OQS03279.1}.
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DR   EMBL; JNBS01000943; OQS03279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9ZZ88; -.
DR   STRING; 74557.A0A1V9ZZ88; -.
DR   OrthoDB; 276070at2759; -.
DR   Proteomes; UP000243217; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.10.20.870; PFU (PLAA family ubiquitin binding), C-terminal domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015155; PFU.
DR   InterPro; IPR038122; PFU_sf.
DR   InterPro; IPR013535; PUL_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19849; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR19849:SF0; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR   Pfam; PF09070; PFU; 1.
DR   Pfam; PF08324; PUL; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS51394; PFU; 1.
DR   PROSITE; PS51396; PUL; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          11..41
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          101..136
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          239..273
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          379..473
FT                   /note="PFU"
FT                   /evidence="ECO:0000259|PROSITE:PS51394"
FT   DOMAIN          488..752
FT                   /note="PUL"
FT                   /evidence="ECO:0000259|PROSITE:PS51396"
SQ   SEQUENCE   755 AA;  80890 MW;  2CBE9ABA96240353 CRC64;
     MTSEYNVQRA LHGHGGAIRA ICQVDDFLIT GSMDAAIYVW NSSSAIVQSI FDHNHWVTAL
     IPLSSVHAKR LGASGFVSGS MDTRLRVYLK TSNEFTCAMV LEGHSSGVIS LAWLADSVLL
     SGSWDGTCRG WDLQTGICNF VLPNHENGVC VLGLSNDTVI TGSTGRQEGN QVVDAVIRVW
     QPSNGVYAVK STLNEHQGPI RQLVQVPEIG FASCSNDGSI KLWTTHGDVV MSCSHPFNHE
     GKPGFVLGLT YLPNTQQLVS ASEDCSVRIW SLDGSCLQTI SHPQGLWCAA ALGNGVDFAT
     GGDDKVARVF STQATMETSA AEIISFQEEV AAAATARQRG PSSVDIAKLP DYNHRGAKVG
     PSDGFIQMFR KGNSAWACQW SGPSQTWLDI GEVTGTGSGG IVDGKSFDIV IPVEIETPNG
     LQKLEIGYNQ GQNPFQVAQA FIDKHFLQQH YLKQIADFIT QQSGSYHAPV LGETSTTSSS
     APLPFLSTYF PVKTYASFDS TKVAKLHSTV VQFNSAVPPN AALSNAELET LTSLITTLTQ
     TSFYHSSQVS STEVNVVLKM VELWPAANVF PALDLCRLLG LHPIGAQVLS AKASWLLERC
     VAFGSSISAD VPNPTRMLAW RVLVNYCVHS CLRATLVASP SVDSGLLQAA NGAKGNKTLA
     VSIATLILNL STAIFNNEQQ TTDALIQVIH SMLPQPLDED TFSRLILSIG TLGLASSQLW
     SKLPTLNAIK ERASAVNSSA TIFAIIDDIA KASKQ
//
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