ID   K1Y2S0_MARBU            Unreviewed;      1029 AA.
AC   K1Y2S0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   ORFNames=MBM_02701 {ECO:0000313|EMBL:EKD19464.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19464.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD19464.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19464.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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DR   EMBL; JH921431; EKD19464.1; -; Genomic_DNA.
DR   RefSeq; XP_007290590.1; XM_007290528.1.
DR   AlphaFoldDB; K1Y2S0; -.
DR   STRING; 1072389.K1Y2S0; -.
DR   GeneID; 18758636; -.
DR   KEGG; mbe:MBM_02701; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_000690_2_2_1; -.
DR   InParanoid; K1Y2S0; -.
DR   OMA; ILYWAHH; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000006753; 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; 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; IPR007110; Ig-like_dom.
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:SF186; PHOSPHOLIPASE D; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
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:UP000006753}.
FT   DOMAIN          367..394
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          741..829
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          792..819
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          175..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1029 AA;  113508 MW;  5584917028198ABF CRC64;
     MPTLCKCSVT LIALQERLVP KPFDCALQTL FAPEALAGAS LRNPIFLPAK NLCALLEDAE
     CAASFFRRPV GISANNKAVV KKAAERVSST GKPLGLALWW EGQQLSVSAK IALPKAKALR
     ICSPLCGNSA ANPKFHLSHL VAVTTIMSFF ESAKNALETF TSDIQKKVDE ITSNTEADDA
     PGAAPLGLQN AADDGPARRG AASSPNRFGS FAPPRRGRGN DAKWFVDGCG YMWAVSVAME
     EARDSIWILD WWLSPELYLR RPPTENEDYR VDRLLIAAAE RGVKVNVIVY KEVSAILTLC
     SEHSKKALEL HPNIAVFRHP DHAPRGQDLH SEIMESFKDF SLKSLQLADV PEETFKALYG
     VSQDVVLYWA HHEKLCLVDG RIAFMGGLDL CFGRWDTNSH PLADAHPTDI SQALFPGQDF
     NNARVYDFDD VPNWENNKLD RTKNGRMGWS DISICVRGPV VEDLKAHFVQ RWNFVFEEKY
     NVRDDPRYTG LTFNPVEIPE GYYQANGKNA APMSGDQAGG DQDSSRGFDG GSMFDVEDSE
     EDRSNTGMSI QLVRSCTEWS NGVPKENSIQ NAYIEVIKNS QHFVYIENQF FITATGDEQH
     PVSNQIGAAL VERIVRAYQN GEKYKVIVCM PAVPAFAGDL HADDSLGTRA IMEYQYQSIC
     RGGHSIMEAI ERAGVPDSKQ YIRFYNLRNY DRINAGAAMS RVQDASGVDY EGARREHDDM
     VGAGYDGRGE GTGAYDGRSN PAYEQYQEAG AQVSDGSKYD SVSECYMDNG PSITDIPWAG
     TEEAEFDAFV SEELYIHSKV LIADDRIVIC GSANLNDRSQ LGDHDSEIAL VIADPTPVQS
     EMNHAPYRAS AFATSLRRQL FRKHLGLLPH QDPARPDANF LPIDQAPQNA YDWGSPADLL
     VRDVLSDEFD ELWTATAAVN TRVFNNAFHC VPSDEVRNWE DYQAYFADLF IGSGAGAGGD
     GDGGAEVPAA RYAYGHVVKE AFPGGVRELK EELARVRGSL VEMPLLFMDG VDFAKEGLSL
     NALTDEIYT
//