ID A0A0D1W3L7_9EURO Unreviewed; 649 AA.
AC A0A0D1W3L7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=PV11_05401 {ECO:0000313|EMBL:KIV83370.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV83370.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV83370.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV83370.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846952; KIV83370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1W3L7; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
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; 2.
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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599}.
FT DOMAIN 3..30
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 436..463
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 356..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 73953 MW; C93A6BDFAE420E62 CRC64;
MTFYWAHHEK FIVIDYHLAF IGGLDLCYGR WDVRQHLLAD VHPSGVVNEI FPGQDFNNNR
IMDFQTVQDW SHNELNKTEY GRMPWHDVAM GLVGECVLDI AEHFVLRWNF VKRDKYKRDD
NVDYLCLTTR ARADGSNPDE DLISVQRPKF PCGEYIEHPL SPLENKGLKN AGTVHAQIVR
SSDDWSSGIL NDQSIQNAYA EVIENAQHYV YIENQFFITA TGENQAPVHN TIGRAIVNAC
VRAGKEGRKF RVIILIPAIP GFAGDLRDDA AIGTRAIMDY QYKSINRGEN SIMGQIAKAG
LDPTQYIFAF NLRAYDRINR TPALIQQEKE SGVSYQELQR AEAEEIMGTG IHGYEGEKKE
KDHRGSGRGD AFSEDERHRT IDRKRQFEAS RKQIDVEDPV TSADSIAEDA LARGGKVSEE
PWEGPPEEEK ANFVQEELYI HAKLLIVDDR TVICGSSNLN DRSQLGSHDS ELSIVMTDSR
VLESTMDGKP FQAGHHAATL RRHVWREHLG LIEAQEVDGS KDPNAQPPTD CLNDEYSGEE
WEFVADPLGD EVWNLWTSQA TTNTDIYRHL FRADPDNNIK TWKDYDQFAP RDAIKQGHLH
DPHMPGDLIR KELDKIRGHL VWMPLDFLCN ENMAERGLQI NSYTESVYV
//
