ID A0A498KKT9_MALDO Unreviewed; 1096 AA.
AC A0A498KKT9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=DVH24_018427 {ECO:0000313|EMBL:RXI06385.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXI06385.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXI06385.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXI06385.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) 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|ARBA:ARBA00000798};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683}.
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:RXI06385.1}.
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DR EMBL; RDQH01000328; RXI06385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498KKT9; -.
DR STRING; 3750.A0A498KKT9; -.
DR EnsemblPlants; mRNA:MD02G0104800; mRNA:MD02G0104800; MD02G0104800.
DR Gramene; mRNA:MD02G0104800; mRNA:MD02G0104800; MD02G0104800.
DR Proteomes; UP000290289; Chromosome 2.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd04015; C2_plant_PLD; 1.
DR CDD; cd00590; RRM_SF; 1.
DR Gene3D; 3.30.70.330; -; 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; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR024632; PLipase_D_C.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF86; PHOSPHOLIPASE D DELTA; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 1..155
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 370..405
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 715..742
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 922..1000
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 843..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..909
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 124983 MW; C1081BF15BAFA962 CRC64;
MAETESEERM IYLHGDLDLT IFEARRLPNM DMFSERFRRC FTACDTINIS STPSAEDDGG
HDGGERKNHV PHRKIITSDS YVTVTVPQTT VARTRVMKNS QNPQWKEHFF VPLAHPAINL
EFHVKDDDVF GAETIGTAEI PAERIATGEL ISGWFPIYGP SGKPPKPDSA IKLELQFTPF
EKNPVYKQGI AGDPEHKGVQ NTYFPLRKGS SVRLYQDAHC PAGLLPEIQL DGGKVYKAEN
TWEDICYAIT EAHHLVYIVG WSVFHKVRLI REPSRPLPRG GDLLLGDLLK YKSEEGVRVL
LLVWDDKSSH DKFGFKTAGM MGTHDEETRK FFKHSSVNCV LSTRYASSKL SIIKQQAGFI
MTFCCFVVGT LFTHHQKCVI VDTQADGNNR KITAFLGGLD LCDGRYDTPE HRLFRNLDTV
FKGDVHQPTF PAGTKAPRQP WHDLHCRVDG PAAYDVLINF EQRWRKATRW KEFALLSKKV
SHWHDDALIK IDRISWILSP PPTVSKDGTT IPEDEPSLWV NNEKDPENWH VQIFRSIDSG
SLKGFPKAGR AAEAKHLICS KNLVIDKSIQ TAYIQAIRSA QHFIYIENQY FLGSSYAWPD
YKNAGADNLI PMELALKIVS KIKANERFTV YVVLPMWPEG DPKTLAMQEI LFWQRQTMQA
MYSTVAAALK SVQIQDSHPQ DYLSFYCLGN REILPEDTAN DDASSVSDSQ KNQRFMIYVH
AKGMVVDDEY VILGSANINQ RSMAGTKDTE IAMGAYQPHY TWAARKKHPH GQIYGYRMSL
WAEHLDMLDP CFEEPESLKC MRKVNEVAGE NWTRFTSPEF TLLQGHLMKY PIDVDVDGKV
GPLPGHENFP DVGGKADSPR KKYSRSPSPW RAQSRSRSRS WSRPRSRSRS WSRPPRQRSR
SRSRGRSRSR SPGRSAAINP GNTLYVTGLS TRVSEKDVER HFSKEGKVAS CFLVMEPRTR
ISRGFAFVTM DSVEDAERCI KHLNQSVLEG RYITVERSRR KRPRTPTPGH YLGLKNTRDY
GDRGDRVRDR ERDRGRYRGG SSRDDYGYRR SPRRSPYRGG RDYSPRGGSP YGGRSRRERS
YSPYGSPERK YARGSR
//
