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
//