ID A0A0E0C138_9ORYZ Unreviewed; 1038 AA.
AC A0A0E0C138;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 18-JUN-2025, entry version 40.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI01G12060.4};
RN [1] {ECO:0000313|EnsemblPlants:OMERI01G12060.4}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [2] {ECO:0000313|EnsemblPlants:OMERI01G12060.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. OR44 {ECO:0000313|EnsemblPlants:OMERI01G12060.4};
RA Zhang J., Kudrna D., Lee S., Talag J., Welchert J., Wing R.A.;
RT "OmerRS3 (Oryza meridionalis Reference Sequence Version 3).";
RL Submitted (MAY-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 ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
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DR AlphaFoldDB; A0A0E0C138; -.
DR EnsemblPlants; OMERI01G12060.4; OMERI01G12060.4; OMERI01G12060.
DR Gramene; OMERI01G12060.4; OMERI01G12060.4; OMERI01G12060.
DR Proteomes; UP000008021; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR FunFam; 3.30.870.10:FF:000011; Phospholipase; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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:SF76; 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; 3.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
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:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 398..425
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 834..861
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..21
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..588
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 117368 MW; B70845539FE5F0E3 CRC64;
MSGGRSAARE GEEEEEAEVE EYGPRYVRMP QEPEGEAAAA GAGSFLRLPE SAGAFDELPR
ARIVGVSRPD AGDITPMLLS YTVEVQYKQV KEWLQNLGIG EHMPVVHDDD EADDVHVPSQ
HDEHSVKNRN VPSSAVLPVI RPALGRQQSV SDRAKVAMQE YLNHFLGNME IVNSREVWAV
LKPGFLALLQ DPFDPKLLDI VIFDVSPHMD RNGEGQSALA REIKEHNPLH FSFEVSSGGR
TIKLRTRSSA KVKDWVSAIN TARRPPEGWS HPHRFGSFAP PRGLTEDGSV VQWFLDGQAA
FNAISSSILE AKSEIFITDW WLCPELYLRR PFHHHESSRL DILLESRAKQ GVQIYILLYK
EVSLALKINS MYSKQRLLNI HENVKVLRYP DHFSTGIYLW SHHEKIVIVD NQVCYIGGLD
LCFGRYDTPE HKVVDVPPSI WPGKDYYNPR ESEPNSWEDT MKDELDRTKY PRMPWHDVQC
ALYGPACRDI ARHFVQRWNY AKRNKAPNEQ AIPLLMPQHH MVIPHYMGKI KESNEEVSKQ
THVEDIKGQK LSSLKAPASC QDIPLLLPHE PDHQASNNGE LGLNGLDNNH GHSDHPNKTY
WKQPIPNRKA KQDTSLQDLQ MKGFVDNLGT PDVSSVIGHY DTSKQNVHHM DNEWWEETQE
RGDQVGSVLD IGEVGPRATC CCQVVRSVGP WSAGTTQIEG SIHNAYFSLI EKAEHFVYIE
NQFFISGLSG DDTIKNRVLE ALYRRILRAE KEKRCFRVII VIPLLPGFQG GIDDGGAASV
RAIMHWQYRT ICRGPNSILK NLYDVVGSKA HDYISFYGLR AHGRLGDGGP LVTNQIYVHS
KLLIIDDRMT LIGSANINDR SLLGSRDSEI GMIIEDKEVV SSIMDGRHWE AGKFSLSLRL
SLWAEHLGLH PGEVSQIMDP VDDLTYNNIW MGTAKANTKI YQNVFSCVPN DHIHSRSQFR
QGFAHRKEKI GHTTIDLGVA VEITETHKDG DLAGTDPMEK LQAVRGHLVS FPLEFMCQED
LRPFFGESEY YTSPQVFH
//
