ID   A0A074YA05_AURPU        Unreviewed;       869 AA.
AC   A0A074YA05;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=M438DRAFT_346589 {ECO:0000313|EMBL:KEQ83666.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ83666.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ83666.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ83666.1,
RC   ECO:0000313|Proteomes:UP000030706};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584984; KEQ83666.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074YA05; -.
DR   STRING; 1043002.A0A074YA05; -.
DR   HOGENOM; CLU_000690_2_2_1; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000030706; 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:SF128; PHOSPHOLIPASE; 1.
DR   PANTHER; PTHR18896; 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:UP000030706}.
FT   DOMAIN          227..254
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          655..682
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   869 AA;  99835 MW;  D5F48089A8E0A558 CRC64;
     MGLIGKTSHV DSSAEQTRDS TDAEHKSAGD HIKHPFSDLR QKLKETSLYD IKVKAVHAKH
     KIGKWQNLIN PNHRHDEEHE KATDEKRTKI GEGHRFQSFA PERDGNKIKW YIDGRDYFHA
     VSVALERAKE TIYIEDWWLS PELFLRRPPF TTQDWRLDHI LKRAAERGVQ IYIVVYKEVN
     QALTCNSAHT KRALRALCPE GTPGHGNIHV MRHPDHNVFE NAGDMTFYWA HHEKFIVIDF
     DLAFIGGLDL CFGRWDQMQH PLADAHPSGV ENEVFPGQDF NNNRIMDFQD VKDWKSNELS
     KADYGRMPWH DVAMGVIGPC VYDIAEHFQL RWNFVKRDKY KRDDRFDWLT LEGREGEDED
     LIAVQRPKHP VGEYIHHPIS PMNVKTGRPD PSNVQGSVHA QIVRSSADWS SGILTEHSIQ
     NAYCEIIRNA QHFVYIENQF FITSTGEEQA PIHNLIGRAI VDACVRAGKE GRKFRVIIVI
     PAIPGFAGDL RDNAAAGTRA IMDYQYKSIN RGEHSIFGQI RKEGIDPEKH VFVFNLRSYD
     RLNKTPAMKK MEEESGVTYQ EVQRAQAEEI MSSGVHGGAE SSSSDEGESE DDEKEHYKDR
     KRKFEARRAA AGLNKDEVIS ADSVAKSAML GEKKVSEEPW DENAAEQEKE NWVQEELYVH
     GKTCIVDDRI AICGSSNIND RSQLGYHDSE LTIIMEDTNA LPSMMDGHEY QAGHHAATLR
     RMLWREHLGL LPAQPLDASE DPNAQPPDVC PNHWYEGDEW DKLVTDPLCD EVWNMWTERA
     TVNTEVFRHL FHADPDDNIR TFEDYQNFLP RGDMKQGHLY NKYQPEADVK SNLDKIKGHL
     VWMPLHFLEN AEMAEKGLAV NYYTESIYT
//