ID   R7YPW1_CONA1            Unreviewed;      1039 AA.
AC   R7YPW1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=W97_03189 {ECO:0000313|EMBL:EON63960.1};
OS   Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Coniosporium.
OX   NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON63960.1, ECO:0000313|Proteomes:UP000016924};
RN   [1] {ECO:0000313|Proteomes:UP000016924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Coniosporium apollinis CBS 100218.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; JH767566; EON63960.1; -; Genomic_DNA.
DR   RefSeq; XP_007779277.1; XM_007781087.1.
DR   AlphaFoldDB; R7YPW1; -.
DR   STRING; 1168221.R7YPW1; -.
DR   GeneID; 19900500; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_000690_2_2_1; -.
DR   OMA; ILYWAHH; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000016924; 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; 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; 2.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 4.
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:UP000016924}.
FT   DOMAIN          290..317
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          810..837
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1039 AA;  117635 MW;  984C16163ABCECB5 CRC64;
     MASRYDDDLA YGDYYHGQGQ DEGGERGIVG DIYKRFRGRQ SQQQQPNVPA PYNPQSSEDP
     YQYHYQPQKP TSSGGMSFLF DKLHGAVHGV GAELKDRLAA REETHGHTHP SGQCSDGTHD
     HHAENRFHSF APQREGNEIK WYVDACGYMW AVSIALEQAR ESIWILDWWL SPELYLRRPP
     AKHEQYRVDR MLQAAARRGV KVNIIVYKEE TNPLIAPPVT VSSSHTKHAL EDLHPNIAVF
     RHPDHLPDRQ TIAADFLASF QSMNLTAANA AKMPLSALQG LYGQTEGTVL YWAHHEKLCL
     VDGKTAFMGG LDLCYGRWDT NQHAIADAHP GNLDDIVFPG QDYNNARVMD FQDVKNWQNN
     KLDRTKNSRM GWSDVSICIS GPAVQDLQNH FVQRWNFIYA EKYTVRKDAR YAPLTFPGTV
     SGYGDGAPPG AFPSYSEQSY RGVEGEEFGR ERSYGGDYES SRRGYDEEYD SRGRGYGDEY
     ESRDRGYGDP YEGGQDRNFR REAYERGERA LFHGHEGGIR DRLKDRLGEE LQGRHDHLGV
     GRRTGSRPAT AGARGPAAIQ LTRSSAKWSH GIVVEHSIAN AYMEVIRNSQ HFIYIENQFF
     ITATDDKQKP IKNKIGAAIV ERILRAARNG EKYKMIVMMP AVPAFAGDLK SDDALSTRAI
     MEFQYTSINR GNGHSIMESI AREGFDPTQY IRFYNLRSYD RINVSGAMKA AEQQSGVSYE
     EARQKHDEAY AYGAQEGYGQ PAPYEMEGGY GRGDAYQAYQ QGAAQIGNRK GLGSGRWDSV
     SECYMLGGED IRNVPWEGGN MDEIDAFVSE ELYIHSKLLI ADDRVVICGS ANLNDRSQLG
     DHDSEIAVVI EDPTPCDSLM NGRPWRASRF AASLRREIFR KHLGLVRPQN YEVPDANYEP
     VGAPNLYDWG SEEDRLVTDP LDDGFLHFWN RRAKINTDAF ARLFHPVPYD GVRNWKQYEE
     FYGRFFSPPK DEKGKEKKPS RYQWGHVVAE EFGGDVRAVK EELAKIRGTL VEMPLLFLKE
     EDIAQEGLGL NAFTEDVYT
//