UniProt: A0A061G8A3

Database: UniProt
Entry: A0A061G8A3_THECC

LinkDB:  A0A061G8A3_THECC 
Original site:  A0A061G8A3_THECC

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (6)   
   Pfam (3)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   A0A061G8A3_THECC        Unreviewed;       809 AA.
AC   A0A061G8A3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=TCM_027158 {ECO:0000313|EMBL:EOY25796.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY25796.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY25796.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
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; CM001884; EOY25796.1; -; Genomic_DNA.
DR   EMBL; CM001884; EOY25797.1; -; Genomic_DNA.
DR   RefSeq; XP_017978949.1; XM_018123460.1.
DR   RefSeq; XP_017978950.1; XM_018123461.1.
DR   AlphaFoldDB; A0A061G8A3; -.
DR   SMR; A0A061G8A3; -.
DR   STRING; 3641.A0A061G8A3; -.
DR   EnsemblPlants; EOY25796; EOY25796; TCM_027158.
DR   EnsemblPlants; EOY25797; EOY25797; TCM_027158.
DR   EnsemblPlants; Tc06v2_t001860.1; Tc06v2_p001860.1; Tc06v2_g001860.
DR   EnsemblPlants; Tc06v2_t001860.2; Tc06v2_p001860.2; Tc06v2_g001860.
DR   GeneID; 18595246; -.
DR   Gramene; EOY25796; EOY25796; TCM_027158.
DR   Gramene; EOY25797; EOY25797; TCM_027158.
DR   Gramene; Tc06v2_t001860.1; Tc06v2_p001860.1; Tc06v2_g001860.
DR   Gramene; Tc06v2_t001860.2; Tc06v2_p001860.2; Tc06v2_g001860.
DR   KEGG; tcc:18595246; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_004684_0_0_1; -.
DR   InParanoid; A0A061G8A3; -.
DR   OMA; PNWGRGI; -.
DR   OrthoDB; 3014064at2759; -.
DR   Proteomes; UP000026915; Chromosome 6.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR   CDD; cd04015; C2_plant_PLD; 1.
DR   CDD; cd09197; PLDc_pPLDalpha_1; 1.
DR   CDD; cd09199; PLDc_pPLDalpha_2; 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:SF115; PHOSPHOLIPASE D ALPHA 2; 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:UP000026915}.
FT   DOMAIN          1..126
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          327..365
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          655..682
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   809 AA;  91711 MW;  6771BB726ADA4DCA CRC64;
     MEDILLHGTL HVTIYEADKL HSGGGGGHFF RKLMANVEET IGIGKGIPKI YATIDLERAR
     VGRTRIIEKE ISNPRWYESF HIYCAHRASN VVFTVKDDNP IGATLIGRAY VSVDELLSGE
     EVDRWVEILD EDKNPIESGG KIHVKLQYFD VTRDRNWNRG IISRKFPGVP FTFYSQRQGC
     KVSLYQDAHI PDGFVPKIPL AGGKYFEPHR CWEDVFDAIT NAKHLICITG WSVYTEITLV
     RDSRRPKPGG DITLGDLLKK KASEGVRVNM LVWDDRTSVG LLKKDGLMAT HDEETENFFK
     DTDVNCVLCP RNPDDGGSFV QDLQISTMFT HHQKIVVVDA AMPNGDTETR RIVSFVGGID
     LCDGRYDTPF HSLFRTLDTA HHDDFHQPNF TGAAITKGGP REPWHDIHSR LEGPIAWDVL
     FNFEQRWKKQ GGKDVLVKLR ELEGIIIPPS PVTFLDDHET WNVQLFRSID GGAAFGFPET
     PEDAARAGLV SGKDNIIDRS IQDAYINAIR RAKNYIYIEN QYFLGSSFGW SADGIKPEDI
     NALHLIPKEL SLKIVSKIQA GERFTVYVVV PMWPEGIPES ASVQAILDWQ KRTMDMMYSD
     IINALRDKGS EEDPRNYLTF FCLGNREVKN GGEYEPSEKP EPDTDYARAQ EARRFMIYVH
     AKMMIVDDEY IIIGSANINQ RSMDGARDSE IAMGAYQPYH LSVRQPARGQ VHGFRMALWY
     EHLGMLDDTF LFPESEECVR KVNQIADKYW DLYSSESLER DLPGHLLRYP IGISSEGTVT
     ELPGFEFFPD TKARVLGAKS DYLPPILTT
//

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