ID A0A0G2HGJ0_9EURO Unreviewed; 836 AA.
AC A0A0G2HGJ0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=UCRPC4_g01022 {ECO:0000313|EMBL:KKY27580.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY27580.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY27580.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY27580.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY27580.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY27580.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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:KKY27580.1}.
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DR EMBL; LCWF01000023; KKY27580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2HGJ0; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000053317; 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; 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:SF128; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; 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:UP000053317}.
FT DOMAIN 198..225
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 623..650
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 538..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 96245 MW; 073368706CF59FEE CRC64;
MPFGKLKEKF EEALEDSPLH DARAKASHLK HKFGKFHNII NPNHRHDEEH EKATDQKRSN
IAEGHRFQSF APERDNNLVK WYVDGRDYFW AVSEALENAK ETIYIEDWWL SPELFLRRPP
YFNQEWRLDQ VLKRRAEAGV KIYVIVYKEV SQALTCNSAH TKLALNSLCP KGSPGYGNIH
VLRHPDHNIF ENAGDMTFYW AHHEKFIVID YALAFIGGLD LCYGRWDARQ HLLADVHPSG
VQNEVFPGQD FNNNRIMDFQ SVQDWQNNEL SKTDYGRMPW HDVAMGVIGD CVYDIAEHFI
LRWNFVKRDK YKRDKRADWL LLEGRTGQDE DLIGVQRPKF PVGEYIQHPI SPLSTKPHGD
QGTVRAQIVR SSDDWSSGIL TEHSIQNAYC EVIRNAEHYV YIENQFFITA TGEHQKPIHN
TIGRAIVDAC VRAGKEGRKF RVIIMIPAIP GFAGDLRQDA AIGTRAIMDY QYKSINRGEH
SIMGQIAKAG VDPTNHIFVF NLRMYDRINK TPKLVEQEKK SGVKYQELQR AQAEEIMGSG
IHGSTSAESK DKEAQTHGIS EDQRHEIIDR KRRFEEARQE VHSDDPIHSA DSIAEDAMTG
GGKVSEEPWE GNAEEEQQNF VQEELYIHAK LLIVDDKTVI CGSSNINDRS QIGSHDSELS
IVMQDTKTIE ITMDGKPYQA AQLANTLRRH LWREHLGLIS AQELDASKDP NARPPNVCGN
DYDEGEHWDF VADPLSDKVW DLWTQQADKN TEIYRQLFRA DPDNNIKTFK EYNNFAPREH
IKQGHIHDEH IPASEVRAKL DQIRGHLVWM PLDFLKDENM AEKGLQVNAY TESIYT
//
