ID A0A0E0C139_9ORYZ Unreviewed; 999 AA.
AC A0A0E0C139;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 18-JUN-2025, entry version 39.
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:OMERI01G12060.5};
RN [1] {ECO:0000313|EnsemblPlants:OMERI01G12060.5}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [2] {ECO:0000313|EnsemblPlants:OMERI01G12060.5}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. OR44 {ECO:0000313|EnsemblPlants:OMERI01G12060.5};
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; A0A0E0C139; -.
DR EnsemblPlants; OMERI01G12060.5; OMERI01G12060.5; OMERI01G12060.
DR Gramene; OMERI01G12060.5; OMERI01G12060.5; OMERI01G12060.
DR HOGENOM; CLU_000690_2_0_1; -.
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; 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 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; 5.
DR SMART; SM00155; PLDc; 2.
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 359..386
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 795..822
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 533..564
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 538..549
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 999 AA; 113439 MW; 5E007FE7D618A6C6 CRC64;
MSGGRSAARE GEEEEEAEVE EYGPRYVRMP QEPEGEAAAA GAGSFLRLPE SAGAFDELPR
ARIVGVSRPD AGDITPMLLS YTVEVQYKQV KEWLQNLGIG EHMPVVHDDD EADDVHVPSQ
HDEHSVKNRN VPSSAVLPVI RPALGRQQSV SDRAKVAMQE YLNHFLGNME IVNSREVWAV
LKPGFLALLQ DPFDPKLLDI VIFDVSPHMD RNGEGQSALA REIKEHNPLH FSFEIFITDW
WLCPELYLRR PFHHHESSRL DILLESRAKQ GVQYLFVCNR FGSIKCLTGS CLHEMIIDKC
MKFNFADIGC MHFKIYILLY KEVSLALKIN SMYSKQRLLN IHENVKVLRY PDHFSTGIYL
WSHHEKIVIV DNQVCYIGGL DLCFGRYDTP EHKVVDVPPS IWPGKDYYNP RESEPNSWED
TMKDELDRTK YPRMPWHDVQ CALYGPACRD IARHFVQRWN YAKRNKAPNE QAIPLLMPQH
HMVIPHYMGK IKESNEEVSK QTHVEDIKGQ KLSSLKAPAS CQDIPLLLPH EPDHQASNNG
ELGLNGLDNN HGHSDHPNKT YWKQPIPNRK AKQDTSLQDL QMKGFVDNLG TPDVSSVIGH
YDTSKQNVHH MDNEWWEETQ ERGDQVGSVL DIGEVGPRAT CCCQVVRSVG PWSAGTTQIE
GSIHNAYFSL IEKAEHFVYI ENQFFISGLS GDDTIKNRVL EALYRRILRA EKEKRCFRVI
IVIPLLPGFQ GGIDDGGAAS VRAIMHWQYR TICRGPNSIL KNLYDVVGSK AHDYISFYGL
RAHGRLGDGG PLVTNQIYVH SKLLIIDDRM TLIGSANIND RSLLGSRDSE IGMIIEDKEV
VSSIMDGRHW EAGKFSLSLR LSLWAEHLGL HPGEVSQIMD PVDDLTYNNI WMGTAKANTK
IYQNVFSCVP NDHIHSRSQF RQGFAHRKEK IGHTTIDLGV AVEITETHKD GDLAGTDPME
KLQAVRGHLV SFPLEFMCQE DLRPFFGESE YYTSPQVFH
//
