ID   A0A1X7RKT0_ZYMTR        Unreviewed;       887 AA.
AC   A0A1X7RKT0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=ZT3D7_G3157 {ECO:0000313|EMBL:SMQ48008.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ48008.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ48008.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; LT853693; SMQ48008.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7RKT0; -.
DR   STRING; 1276538.A0A1X7RKT0; -.
DR   Proteomes; UP000215127; Chromosome 2.
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; PF13091; PLDc_2; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 3.
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:UP000215127}.
FT   DOMAIN          209..236
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          653..680
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   887 AA;  100804 MW;  D8F9DE7B7F89E717 CRC64;
     MSFFMNKLKE SVNDVQLKVK AAKTGKPIHS HTNAEGECSD GDSHHLHRFQ SFAPQREGNE
     VKWYVDGCSY MYAVSMALEH AQQEIYILDW WLSPELYLRR PPAKNEQYRL DRLLFAAARR
     GVKIHIIVYK EVTQALTLSS HHTKHWLEDN DKTGNIKVFR HPDHLPDKQT MASQFVERIK
     QTGMNASKLA QLPGDALKGI YGMNDGTVLY WAHHEKLCLV DGHVAFMGGL DLCYGRWDTN
     QHSIADAHPG DLNRIVFPGQ DYNNARVMDF DDVSHWENNK LDRKVNSRMG WSDVSICAKG
     PVVEDLRAHF TQRWNFIYYE KYDVRQEARF HPLVYHPVRA GIIGHPYTQI EGEEVEGEGQ
     YHGFRERIKF QYESSKDRME SQLRERVMGG AQPEYPTGPL GGVHCQIVRS CAKWSHGTPV
     EHSIADAYIQ LIRNSQHFVY IENQFFITGT CEAQKPITNL IGAAIVERAL RAARNNEDWH
     MIINIPSVPA FAGDLKADSS LGTRAIMEFQ YNSINRGGHS ILETIAREGV DPMKYVRFYN
     LRSYDRINTN AAMAKVEQKA GVSYDYARKG YDQQYGQGNE NQQPGYAGEV QGTADAFNQY
     QQAAQEVRAE TGGDAASGRW DSVAECYMLN GPDIRTVPWD GDAQSEIDAF VSEELYIHSK
     LMIVDDRTVL CGSANLNDRS QLGYHDSEIA MIIEDNQEVD TYLAGRPWKA TLYATTLRRQ
     IFRKHLGLLP PQDYQSPDAN FTPVGQPNAY DWNSPGDHAV ADPLSPAFDA LWKNTASTNT
     AAFAKIFHPV PDDSVRNWKQ YDEYYSRFFK TEDAKKQGKD TEKPSTYKWG HVVAESFSPG
     EQGLREVKDL LSTIKGNLVE MPLLFLKEED IAKEGLGLNS FTETVYT
//