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Database: UniProt
Entry: A0A136IKP9_9PEZI
LinkDB: A0A136IKP9_9PEZI
Original site: A0A136IKP9_9PEZI 
ID   A0A136IKP9_9PEZI        Unreviewed;       861 AA.
AC   A0A136IKP9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=Micbo1qcDRAFT_48532 {ECO:0000313|EMBL:KXJ85495.1};
OS   Microdochium bolleyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX   NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ85495.1, ECO:0000313|Proteomes:UP000070501};
RN   [1] {ECO:0000313|Proteomes:UP000070501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG   DOE Joint Genome Institute;
RA   David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA   Barry K., Grigoriev I.V.;
RT   "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT   beachgrass.";
RL   Submitted (FEB-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; KQ964280; KXJ85495.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136IKP9; -.
DR   STRING; 196109.A0A136IKP9; -.
DR   InParanoid; A0A136IKP9; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000070501; 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: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; 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; 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:UP000070501}.
FT   DOMAIN          211..238
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          627..654
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          365..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   861 AA;  97602 MW;  888771CBB55A6563 CRC64;
     MSFFNKAKDR LEKGLKDGLQ QAQSALNINK DPEHSHTHDG ACDHHHDNYD SNHRYQSFAP
     QSSGDVKWYV DGASYFWAVS MAIENAKESI YILDWWLSPE LYLRRPPSHN ERYRLDKMLH
     NAAERGVDVR IIVYKEVAAA LTCDSAHTKH ALEALHQNIK VFRHPDHTPN SKEVISGFSG
     LTLKTYKPGD LAKASTNALA SIYGQFGDSV LYWAHHEKLC LVDRRVAFMG GLDMCFGRWD
     TMSHPIADAH PGNLDNIIFP GQDFNNARAF DFEGVNNWNH QNKLDRSKNG RMGWSDITIS
     MVGPIVTNLL EHFVDRWNFI QDEKYAKKDS GKYNKLSAEG GAVIEEHHIP RNLHEMHGRF
     KRFIGDDDNE EENGRQHEQQ RQGDNERHET AAIQLTRSCC EWSAGHPTEH SIANAYLDAI
     TNAKHYVYIE NQFFITATSD AQKPVTNKIG LCIVNRIVKA HEAGEDFRIV VIMPAVPAFA
     GDLKSDGALG TRAILEFQYQ SISRGGHSII ETLQQRGVQD WGRYIGFYNL RNYDRLNSST
     TMQRAEQASG VSYDQARQGY DQKQDQPGAP QQGEQADAYK RYQYVATQQE DSTWDTVSSC
     YMQGGKDIRE VPWSGSPEAE LDAFISEELY IHSKVLIADD KLVICGSANL NDRSQLGNHD
     SEIAVIIEDP TPVDSKMAGR PYTASRFAAS LRRQLYRKHL GLLPDQRWDQ PTAAWTPVDA
     NPQEYDWGSR SDQLVEDPLG GDFLRLWADT ARTNTEVFSK VFHNVPNDAV RNWAQYDDFF
     GKHFVIPGNE YKNGEDKDPN RVLYGHVVKS EFPGGVGEVK DWLSRVRGTL VDMPLDFLVE
     LGDDLAMEGF GLNFATKELY T
//
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