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Database: UniProt
Entry: A0A5C3Q1B9_9AGAR
LinkDB: A0A5C3Q1B9_9AGAR
Original site: A0A5C3Q1B9_9AGAR 
ID   A0A5C3Q1B9_9AGAR        Unreviewed;       893 AA.
AC   A0A5C3Q1B9;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   18-JUN-2025, entry version 22.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=BDV98DRAFT_608823 {ECO:0000313|EMBL:TFK95611.1};
OS   Pterulicium gracile.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotineae; Pterulaceae; Pterula.
OX   NCBI_TaxID=1884261 {ECO:0000313|EMBL:TFK95611.1, ECO:0000313|Proteomes:UP000305067};
RN   [1] {ECO:0000313|EMBL:TFK95611.1, ECO:0000313|Proteomes:UP000305067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 309.79 {ECO:0000313|EMBL:TFK95611.1,
RC   ECO:0000313|Proteomes:UP000305067};
RX   PubMed=30886374; DOI=.1038/s41559-019-0834-1;
RA   Varga T., Krizsan K., Foldi C., Dima B., Sanchez-Garcia M.,
RA   Sanchez-Ramirez S., Szollosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA   Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA   Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA   Damon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA   Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA   LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA   Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA   Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA   Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA   Grigoriev I.V., Vagvolgyi C., Papp T., Martin F.M., Miettinen O.,
RA   Hibbett D.S., Nagy L.G.;
RT   "Megaphylogeny resolves global patterns of mushroom evolution.";
RL   Nat. Ecol. Evol. 3:668-678(2019).
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; ML178879; TFK95611.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C3Q1B9; -.
DR   STRING; 1884261.A0A5C3Q1B9; -.
DR   OrthoDB; 14911at2759; -.
DR   Proteomes; UP000305067; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:TreeGrafter.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR   CDD; cd00138; PLDc_SF; 1.
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:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000305067}.
FT   DOMAIN          181..208
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          678..705
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          338..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  103066 MW;  6C70AA0454769AC4 CRC64;
     MSFFKNLKNK VEQAADKLPQ GLMNARAEAI GLWNPNRRHD EPHEIENDRV REDIMQGHRF
     RSFANERNDN TVKWHIDGHD YMWAMSELLD KAKEAIFILD WWLTPELFLR RPPARHPEWR
     LDRLLKRKAE EGVKVYVIVY KEVTQTMSMS SKHTKNYLEG LHPNIVCLRH PDHVGSKDSV
     QFWSHHEKVV VVDNHYACIG GLDLCFGRWD THNHPCADCH PTDFSKTLFP GQDYNNARVM
     DFQNVFNYAS NAISVLESPR MPWHDVHMTL TGPVVLDIVQ HFVERWNEIK KRKYRDKENV
     DWLSLPHNVQ ASPNEAVARH PHRDEWQNKG RRFKQRFHFS SEEEQEEHRN SEYHGGRDRR
     DEGEDRDGDR YRDGERDGDR YRGGDRDGER RSAREGTCRV QVVRSVSDWS HGVLTECSIQ
     NAYVESIRDA RHYIYIENQF FITATKTGGQ VVNQIGKALV DRIVQAAQNR EKFKVVVVIP
     EVPGFAGDVK TESSIKYIMA AQYRSINRGG DSIYEQIRRA GYEPLDYIRF YHLRSYDRIN
     APMPTFINQM EENSGVRFHE AQVALSRLLI GTSQTDQREV TLAVPEPMMH GLVEGGTAGH
     KTGEGNTQKP NTITIPIPES EDAAREIIER FERGAEGVRG DEEVSDSVAQ HMLGDRTGLK
     DEKWLGTEEE ELKSYVSELL YIHTKLMIVD DARVIMGSAN INDRSQKGDG DSEIALVVED
     MDLIDATMGG QHVMVSRFAS SLRRKLYREH IGLIEPQNCG IANDRVTSFM RAAPHANKDE
     FDEEEDRLVA DPLADDTWRL WNETAKRNTQ IFTELFRPVP TNLVRDWGAY DNYVAKVKPG
     HVVEGISLET VKDRLSEVKG ALIECPLDFL IDQRDFVEGP EWRGFDPTLP IYI
//
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