ID A0A2P5CSL1_TREOI Unreviewed; 851 AA.
AC A0A2P5CSL1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
GN ORFNames=TorRG33x02_274000 {ECO:0000313|EMBL:PON64049.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON64049.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. {ECO:0000256|PIRNR:PIRNR036470}.
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|ARBA:ARBA00000798,
CC ECO:0000256|PIRNR:PIRNR036470};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|PIRNR:PIRNR036470};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683, ECO:0000256|PIRNR:PIRNR036470}.
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:PON64049.1}.
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DR EMBL; JXTC01000331; PON64049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5CSL1; -.
DR STRING; 63057.A0A2P5CSL1; -.
DR InParanoid; A0A2P5CSL1; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000237000; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR CDD; cd04015; C2_plant_PLD; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR024632; PLipase_D_C.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR011402; PLipase_D_pln.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF130; PHOSPHOLIPASE D GAMMA 1-RELATED; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 2.
DR PIRSF; PIRSF036470; PLD_plant; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRNR:PIRNR036470};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036470};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000237000}.
FT DOMAIN 20..163
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 364..399
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 697..724
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 851 AA; 95644 MW; CDFEC49FEDCA6C29 CRC64;
MAHSMFAGSL SFGGSQHGQA QQELPFKTSK ESLKVLLLHG NLDIWIMEAK NLPNMDMFHK
TLGDMFGRFG KLSTKMEGHM SNKITSDPYV TVSVSGAVVG RTFVIENSEN PVWKQHFNIP
VAHKAAEVHF VVKDNDVVGS QLIGAVGIPV EQLSSGVRIE GTFPILSASG KPCKPGAVLS
LSIQYTPMEK VTLYQLGLGS SPESLGVPGT YFPLRKGGKV TLYQDAHEHD CGLPSLPLGN
GIQYKHSNCW RDIFDAISQA RRLIYIVGWS VVHKVRLIRE NGNVAESMLG DLLKRKSQEG
VRVLLLVWDD PTSRTILGYK KEGVMGTHDE DTRRFFKHSS VQVLLCPRSA AKGHSWVKKQ
EVGTIYTHHQ KTVIVDADAG DYRRKIIAFV GGLDLCTGRY DTPNHHLFRT LQTVHADDFH
NPTFPEPSAG CPREPWHDLH CQIDGPAAYD ILTNFEERWL RASKQSGLQR LKSSYDDQLL
RIERIPEFIS IAEVAGKGEN NPETWNVQVF RSIDSSSVKG FPSDPKDATN KNLVCGKNLL
IDMSIHTAYV KAIRSAQHFI YIENQYFLGS SYNWGSNKDL GANNLIPMEI ALKIVNKIRS
NERFSAYIVI PMWPEGVPTS IPVQRILFWQ RKTMEMMYEM IYEALKEVGL DSTYEPQDYL
NFFCLGNREA PDGTTPSTGT SNAEKTPQAL SRKNRRFMIY VHSKGMIVDD EYVILGSANI
NQRSLEGTRD TEIAMGAYQP HHTWSRKRSN PRGQVYGYRM SLWAEHIGGL EERFKSPESL
ECVRRVRYLS EQNWRQFTAD EATEMKGHLL KYPVEVDKTG KVKALPGCES FPDVGGNILG
TFIAIQENLT I
//
