ID   S3DN17_GLAL2            Unreviewed;       876 AA.
AC   S3DN17;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=GLAREA_06504 {ECO:0000313|EMBL:EPE33491.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE33491.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE33491.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
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; KE145358; EPE33491.1; -; Genomic_DNA.
DR   RefSeq; XP_008080108.1; XM_008081917.1.
DR   AlphaFoldDB; S3DN17; -.
DR   STRING; 1116229.S3DN17; -.
DR   GeneID; 19465557; -.
DR   KEGG; glz:GLAREA_06504; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_000690_2_2_1; -.
DR   OMA; ILYWAHH; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000016922; 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:UP000016922}.
FT   DOMAIN          208..235
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          648..675
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          18..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   876 AA;  98903 MW;  D362208397136187 CRC64;
     MSFFDNLTSK IQDGIQEAFG DNNENDNRPQ EHSDQQQSYD ANSYTAPANR FHSFAPTRTG
     NDAKWYVDGC GYMWAVSIAL EEARESIWIL DWWLSPELYL RRPPSENENY RLDRMLIAAA
     ERGVKVNVIV YKEVSQILTL ASVHTKHALE VHPNIRVFRH PDHIPKGQEL HEDLIEGLKN
     LSFSPFHLAQ LPGKQIESIY GASEDIVLYW AHHEKLCLVD SEIAFMGGLD LCFGRWDTNS
     HPIADVHPTD LNKALFPGQD FNNARVFDFA DVEHWDQNKL DRTKNSRMGW SDISLCLRGP
     VVDDLKAHFV QRWNFIYKEK YNIPGKGYEP LTLETSKIQG GYYNFDGFNT TPMKEQPKGG
     EFDAPPDGYQ QEGAPRRRHH FSAFREQMGL ISHDDDPQGP SANGVSVQLL RSCTKWSAGV
     PLEHSIANAY INVIKNSEHF VYIENQFFIT ATGEHQSPVK NQIGAALVER VVRAYESGQR
     YKVIVLMPSV PAFAGDLHAD DSLGTRAIME YQYQSICRGG HSIIEEIQKA GVPDAGQYIR
     FYNLRNYDRL NTGSSMSRVE DASGVDYEDA RREHDDLVGA GYDGRGEETG AQYGQPNRQY
     DQYQQAASGE DTSQFDSVSA CYMDGGPSIT EIPWSGSPDA EMNAFVSEEL YIHSKVLIAD
     DRIVICGSAN LNDRSQLGNH DSEIAVLIDD PTPVSSLMNG QEYTASAYAS SLRRQLFRKH
     LGLLPHQICD QPNENFEPVN RYPNIYDWDS PGDLLVRDVL SDEFDLLWNE TAAVNTAVFS
     KAFHCVPADN VTTWEEYEEF FGALFVPKGE GEDVTPSRYE YGHVVTEEFP GGVGELKEEL
     NRVRGTLVEM PLRFMQGVDF AVEGLSFNSL TNEVYT
//