ID   A0A316W9C2_9BASI        Unreviewed;       851 AA.
AC   A0A316W9C2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=IE81DRAFT_319542 {ECO:0000313|EMBL:PWN46154.1};
OS   Ceraceosorus guamensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN46154.1, ECO:0000313|Proteomes:UP000245783};
RN   [1] {ECO:0000313|EMBL:PWN46154.1, ECO:0000313|Proteomes:UP000245783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN46154.1,
RC   ECO:0000313|Proteomes:UP000245783};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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; KZ819352; PWN46154.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316W9C2; -.
DR   STRING; 1522189.A0A316W9C2; -.
DR   InParanoid; A0A316W9C2; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000245783; 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; PF00614; PLDc; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
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:UP000245783}.
FT   DOMAIN          179..206
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          628..655
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          708..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   851 AA;  96845 MW;  11083B013ACBD8F0 CRC64;
     MGVRDTLKKN LDPETFVDSV SKLGSGFAAM MNPNHRHDEA HEKEKDKILQ SIRDSHRFNS
     FAGVRSGNRA KWYSDGHDYF WALSELLDNA KETIFILDWW LTPELYLRRP PHLYEEWRLD
     RLLKRKAEQG VQVRIIVYKE VTETMTMSSA HTKHALEDLH PNIRVFRHPD HMPHGEITLF
     YSHHDKVVVV DAEYACVGGL DICFGRWDTQ SHPLSDCHPF AMLERTLFVG QDFNNARVMD
     FAKVDDFMNN QQSSLSLGRM PWHDVHVTFT GPSVLDVAYN FIERWNFVKE LKYGKGYSLI
     AFPHGAVPAS DVLEEHQEIA RHPHMERFHE YGERFMHPWH PERRKLQLSD GGSVGANATM
     DVQVVRSAAD WSSGILTEHS IQNALIELIQ TASHSIYIEN QFFITATQPG QVVNCVGAAI
     ANRIISAAKD GRRFKVVIVI PCIPCFAGEL QEAAGNRTIM QKQYESINRG GKSIMEVIKA
     AGYDPHEYIS FWNLRGIDRI PSGIVRETEQ ASGITYHQAQ VALARVYIGD AAYQDGRKKI
     AIKVPSSEPD APLDKDGKKK LSTVEEVEMP ATSQEALEIL RKFANGTPER ARGLQDSIAS
     AFLHGQPDIT QSQWQGSEEE EVNAWVTEET YVHSKLAIFD DRTVLIGSAN LNDRSQAGDR
     DSETAIVIED HDMFESKMDG KKYMASRFAA SFRRHLYRQH LGLVAPQECT PETAKDQPTP
     AQRPAPHPFP DPERKAQEEE WEQLVEDPLS PELEEIWRRQ ARTNTAIVDE LFQVVPSNRV
     RNWKDYDSFF VARGARTGHI AEPGKRSAQE VRQRLAGYKG SLVEFAYDFM DGDNFEKTDI
     TTSKALLDLY T
//