ID   A0A1B8GBH0_9PEZI        Unreviewed;       858 AA.
AC   A0A1B8GBH0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=VE01_09244 {ECO:0000313|EMBL:OBT93127.1};
OS   Pseudogymnoascus verrucosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT93127.1, ECO:0000313|Proteomes:UP000091956};
RN   [1] {ECO:0000313|EMBL:OBT93127.1, ECO:0000313|Proteomes:UP000091956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT93127.1,
RC   ECO:0000313|Proteomes:UP000091956};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000091956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX   PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT   white-nose syndrome of bats.";
RL   Nat. Commun. 9:35-35(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; KV460257; OBT93127.1; -; Genomic_DNA.
DR   RefSeq; XP_018126860.1; XM_018278659.1.
DR   AlphaFoldDB; A0A1B8GBH0; -.
DR   STRING; 342668.A0A1B8GBH0; -.
DR   GeneID; 28842630; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000091956; 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; 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   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:UP000091956}.
FT   DOMAIN          214..241
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          646..673
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          585..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..605
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  97926 MW;  479B2930F2C7F524 CRC64;
     MSATTTAHCA SHPVGLKSNF KHPFKFLHEK LQPKINNVKV AFSHKRHELG KLGNTFNPNH
     RHDEKHEKIT DDKRTRISSG HPFQSFAPER PGNDVKWYVD GRDYYWAVSI ALERAKETIY
     IEDWWLSPEL FMRRPPCFNQ EWRLDQILKR RAEAGVKIYV IVYREVEAAL TCNSKHTKQV
     LQGICPVGSK GYGNIVVMRH PDHNRFENAA DRTLYWAHHE KFVVIDYHTA FIGGLDLCFG
     RWDTHQHPLV DVHLGGIFNE IWPGQDFNNN RVMDFQNVEE WKSNALSKAE YGRMPWHDVA
     MGVLGPCVVD IAEHFVLRWN LIKRDKYKRD GRYNWLIMEG RDGRDEDLIG VQRPNFPVGE
     YVSHPLSPLS SKALGNRGTV HAQVVRSSSD WSSGILTEHS IQNAYSEVIR NAQHYIYIEN
     QFFITATGDK QAPIKNTIGK AIVEAVVRAG REGRKFRVIA VIPAIPGFTG DLRHGVAVGT
     RRGPEVGTRA IMNYQYQSIC RGEQSIFEQI RAQGVDPAQH IFFFNLRSYD RLRATTALEP
     HGGKHGVKNR EVQMAEAQQT TDSGIHSAGD QGGDLGRHIP NYGDYDEEKR TNAKRRHETA
     EEPVGSNRAT ERTQSVAKNA MYQMPKLEDE LQGCNTIGEV DSWVQEELYI HAKLLIADDR
     TVICGSSNLN DRSQLGSRDS ELSIVMTDTE PLESKMNGQE FVAGRHAATL RRYLWREHLG
     LLPPQDLDAR REANAQPPGI PNDPHQGDTY EFVGDPLGNE VWHMWTSRAT QNTNVFSELF
     HADPDNSVKT FKDYDKYLPA KGTKAGHVYD RTLPRKDILR KLDLVKGHLV WMPLEFLKDT
     PMSEPGIQFN SLTDYVYT
//