ID A0A0L0V2Y1_9BASI Unreviewed; 861 AA.
AC A0A0L0V2Y1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=PSTG_13286 {ECO:0000313|EMBL:KNE93344.1};
OS Puccinia striiformis f. sp. tritici PST-78.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNE93344.1, ECO:0000313|Proteomes:UP000054564};
RN [1] {ECO:0000313|Proteomes:UP000054564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL Submitted (MAR-2014) 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}.
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:KNE93344.1}.
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DR EMBL; AJIL01000139; KNE93344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0V2Y1; -.
DR STRING; 1165861.A0A0L0V2Y1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000054564; 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; 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:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000054564}.
FT DOMAIN 177..204
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 643..670
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 861 AA; 98400 MW; 0D0BB716829EBAAC CRC64;
MDKFLDHFQS HTPVADKLER LGEGIKKLFH PNSRHDDPAE KLHDERLEEI RARHRFQSFA
KEREGNQVKW YVDAHDYFYA ASELLESAKS CIFIQDWWLS PELYLRRPAG QNELWRLDRI
LKRKAEAGVK IFVIVYKEVS VSGTMNSEHT KHALEALHPN IACMRHPDHF DGEETVLFWS
HHQKVIVVDN NIACIGGLDL CFGRWDTSSH SLADCHISDL TQTVWPGQDY NNARVQDFQD
VEAWASNQQS RLEVPRMPWH DVHMMIQGPT VFDICQHFVE RWNFIYKLKY VKKPGTNGRY
ELLAFPHIPG EGIPEDPSHP DHEPVTQHPH YEQWCQSGRK FFGMEETTRA PTDLPSHDLG
PKGNMKVQVV RSCGDWSNGT TTEHSIQNAY IQLIEQAQRF IYIENQFFIT TCSTDKDRRI
HNQIGLALAN RIVQADRAEQ PFKVVVAIPC IPGFSGNLDN PEVSGGTMAI MDWTYKSICR
GPDSIFSHVQ KHGVDPRKYF SFYNLRSFDR IDYEPGTLKA IEEAAGISYY EAEAALARVY
LGESASSQEL EKNKEVTFKL AQKGESMEAG SRDMVARDGE TVKVDLPQSV EEARQRLKIW
SEAASRYDRG IPASIATQNH SNGLEDLPWL GDEQSEREAF VTEELYIHTK CMIVDDQKVI
MGSANINDRS MMGDRDSEIA LVVEDQDMID STMAGENWKA GRFAATLRRR LYKEHLGLLA
PQSNSLQSNE PTRFMLPVNV PQEDEMGSDE DRIVTDPMGR ELEDMWRGRA SVNTQSFNKV
FRCVPAAGIL NWKDYEEYVP SGSNAPKVCH VAPGAGDLHE VKHALSRIKG HLVEMPLDFL
EQDKMYREGK AVNLVTMDIY T
//
