ID W2ZUQ5_PHYPR Unreviewed; 578 AA.
AC W2ZUQ5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=F442_04619 {ECO:0000313|EMBL:ETP49964.1}, F442_04620
GN {ECO:0000313|EMBL:ETP49961.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP49964.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP49964.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP49964.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETP49964.1}.
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DR EMBL; ANIY01001025; ETP49961.1; -; Genomic_DNA.
DR EMBL; ANIY01001024; ETP49964.1; -; Genomic_DNA.
DR AlphaFoldDB; W2ZUQ5; -.
DR EnsemblProtists; ETP49961; ETP49961; F442_04620.
DR EnsemblProtists; ETP49964; ETP49964; F442_04619.
DR Proteomes; UP000018948; 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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd09104; PLDc_vPLD1_2_like_1; 1.
DR CDD; cd09105; PLDc_vPLD1_2_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; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF60; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 1.
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:UP000018948};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..578
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009351580"
FT DOMAIN 444..471
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 38..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 64546 MW; E2A3D6BB983E8472 CRC64;
MDFTQKVLSR LTITLLCMLA LAPSSSTAWS FSSIFGGDDD SSSASGNSVV DKSDGSDVEM
QQPLLKAADW FLTEEEITAS RGGSPRSDMA TYSTGNAVKT FTVTKEFFDS VFDDLTTTEV
NDRVMLASWN TDLVPFKPDV DPTGAKSNFD VVFGGVVKRG GDVKILGWAN KFLFFQDVKV
RNKINKLPKS GTNDGNALFI FDDRLPYGMS SQHQKALVIA AGSSTGKDDH PVAYVGGIDL
SNDRWDNIYH NATAIRKESG VHFRQNGWVD SSMRIHGPAA KDVANNFLAR WNSPYLPAQG
LGDDLVDFEN PQYSYLPPLD YASSNTTSKL GNQNVQIVRT FSCKYKNWEF APNGENSLFH
ARIKAIKNAK NFIYIEDQYF ILVPELLDAL MEVLPSLQRL IVVAQPPELI TKSAGYEKYM
YQNVQALKEK FPNKFKFYSM KPKLDVYVHS KLVVVDDVYL SDGSANWNRR SMTSDPELDA
NVVDSDIVDT PDGIKVGKII RDFRVRKFQE MTGRSYKKIN AMKFLDAANL YDTAAAEASS
LIEKLEVDKE WYYNLYGDAI QKRVDPQDTC DGISYGSS
//
