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Database: UniProt
Entry: A0A2T7EM58_9POAL
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ID   A0A2T7EM58_9POAL        Unreviewed;       838 AA.
AC   A0A2T7EM58;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, 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=GQ55_2G067500 {ECO:0000313|EMBL:PUZ68918.1};
OS   Panicum hallii var. hallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Panicum.
OX   NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ68918.1, ECO:0000313|Proteomes:UP000244336};
RN   [1] {ECO:0000313|EMBL:PUZ68918.1, ECO:0000313|Proteomes:UP000244336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA   Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA   Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA   Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA   Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT   "WGS assembly of Panicum hallii var. hallii HAL2.";
RL   Submitted (APR-2018) 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}.
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DR   EMBL; CM009750; PUZ68918.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7EM58; -.
DR   STRING; 1504633.A0A2T7EM58; -.
DR   EnsemblPlants; PUZ68918; PUZ68918; GQ55_2G067500.
DR   Gramene; PUZ68918; PUZ68918; GQ55_2G067500.
DR   Proteomes; UP000244336; Chromosome 2.
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:SF189; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12357; PLD_C; 1.
DR   Pfam; PF00614; PLDc; 1.
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:UP000244336}.
FT   DOMAIN          1..144
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          350..385
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          684..711
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          810..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  94706 MW;  051B9BFE42891393 CRC64;
     MGKHSAESGV SMLLHGDLDI QIIEAKCLPN MDLMTERMRK CFTAYGACST DCGKSDAHPD
     MRKIITSDPY VSVCLSGATV AQTRVIANSE NPKWEEHFYV QVAHSVSRVE FLVKDNDVFG
     AELIGVASIP VEQIAPGDMV TGWFPIAGQY SNPMKPSPEL HLSIQYKTID TNPLYKDGVG
     ADGSQSVGVP NAYFPLRKGG MVTLYQDAHV PDDFRPQIEI DGGRTYEQNK CWEDICHAII
     EAHHLIYIVG WSLYHPVKLV RESSKPVPNG NPLTIGEILK RKVQEGVRVI VLLWDDKTSH
     DKFLLKTDGL MHTHDEEARK FFRHSGVHCV LSPRYASNKL SIFKQQVVGT LFTHHQKCVI
     VDTQATGNNR KITAFIGGLD LCDGRYDTPE HRLFKDLDTI FKDDFHNPTF PVNKIGPRQP
     WHDLHCKIEG PAAYDILINF EQRWRKSAKW KVSVRRAVSW HHDTLVKIDR MSWIVSPSAD
     ELNAHVCEEK DPENWHVQVF RSIDSGSVKG FPKLVQEAES QNLVCAKNLQ IDKSIHNAYI
     KAIRSAQHFV YIENQYFIGS SYYWSAHRSA GAENLIPIEL AIKIARKIKA KERFAAYIVI
     PMWPEGNPTT AAMQEILYWQ GHTMSMMYKI VADALRKEGL HESHPQEYLN FYCLGKREVS
     SDVAQTNTSN ENSAIRLAQK FRRFMIYVHS KGMIVDDEYV LIGSANINQR SMDGSRDTEI
     AMGAYQPHYS WAGSGSPPRG QVYGYRMSLW AEHLGTVEEC FRQPESEECV QRVNQVADDN
     WATYVSPQME DMKGHLMRYP VKVEQDGRVG PLPGQESFPD VGGKVLGTHS SLPNALTT
//
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