ID   A0A1E1LMG9_9HELO        Unreviewed;       896 AA.
AC   A0A1E1LMG9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=RCO7_08689 {ECO:0000313|EMBL:CZT11707.1};
OS   Rhynchosporium commune.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Ploettnerulaceae; Rhynchosporium.
OX   NCBI_TaxID=914237 {ECO:0000313|EMBL:CZT11707.1, ECO:0000313|Proteomes:UP000178129};
RN   [1] {ECO:0000313|EMBL:CZT11707.1, ECO:0000313|Proteomes:UP000178129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UK7 {ECO:0000313|EMBL:CZT11707.1,
RC   ECO:0000313|Proteomes:UP000178129};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009376};
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC       {ECO:0000256|PIRNR:PIRNR009376}.
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DR   EMBL; FJUW01000063; CZT11707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E1LMG9; -.
DR   STRING; 914237.A0A1E1LMG9; -.
DR   InParanoid; A0A1E1LMG9; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000178129; Unassembled WGS sequence.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR   CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR   CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF186; PHOSPHOLIPASE D; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 3.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Reference proteome {ECO:0000313|Proteomes:UP000178129}.
FT   DOMAIN          213..240
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          666..693
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          26..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   896 AA;  100728 MW;  1F44C436F095F877 CRC64;
     MSFFGSAKNA FDSFSSHVKD EIDKIQGDGQ SSAQTQSNTS NTSNVGQSQS AGGNRFDSFA
     PPRAGNEAKW YVDGCGYMWA VSVAIEEARE SIWILDWWLS GELYLRRPPT ENENYRVDRM
     LLAAAERGVK VNVIIYKEVS QILTLCSDHT KKALQLHPNI AVFRHPDHTP SGPVIQSELL
     ASIQNFSLKS LQLADIPADA FKALYGVNKD VVLYWAHHEK LCLVDGDIAF MGGLDLCFGR
     WDTNSHPLAD AHPTNINKAL FPGQDFNNAR VFDFEDVTNW EKNKLDRTKN SRMGWSDISI
     CLRGPVVQDL KAHFVQRWDF IYEEKYRVRK DPRFESLRFD ANGVPGGYYR ENGSNSISVS
     APRSLQIEGI SDSVERGFGQ QGGQHEHRFH LPGGHGSIFD RLRGTDVDNT GRSYSDTVSS
     GISIQLVRSC TQWSNGVAKE HSIANAYIDI IRNSEHFVYI ENQFFITATG DKQRPVKNQI
     GAAIVERIVR AYREGQRYKV IVCMPAVPAF AGDLHADDSL GTRAIMEYQY HSICRGGHSI
     MEEIEKAGVP DSKQYIRFYN LRNYDRINAG SAMARVYDAS GIEYEDARRE HDDIVGAGYN
     GRGEGTGAYY GRSNPAYEQY QEAGALVNDD SKYDSVAACS MDYGPSIKDI PWSGSEEAEF
     NAYVSEELYI HSKVLIADDK IVICGSANLN DRSQLGDHDS EIAVVIQDPT PVDSEMNHAP
     YQASRFASSL RRQLFRKHLG LLPHQDPTRP DENFLPISHA PNTYDWGSPA DILVRDVLSD
     EFNELWTRTA AVNTEIFTRA FHVVPADNVR NWEDYKEFFS KHFMSPSKEE DKVKLPSRYE
     YGHVVKEEFP GGVAELKDNL NRVRGSLVEM PLLFMDGVDF AKEGLTLNAL TDEVYT
//