ID W9SAS8_9ROSA Unreviewed; 1125 AA.
AC W9SAS8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=L484_005239 {ECO:0000313|EMBL:EXC23290.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC23290.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE345992; EXC23290.1; -; Genomic_DNA.
DR RefSeq; XP_010109581.1; XM_010111279.1.
DR AlphaFoldDB; W9SAS8; -.
DR STRING; 981085.W9SAS8; -.
DR eggNOG; KOG1329; Eukaryota.
DR Proteomes; UP000030645; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 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; 1.
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; PS50003; PH_DOMAIN; 1.
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:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000030645}.
FT DOMAIN 273..364
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 499..526
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 921..948
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 149..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 127677 MW; 76A113BACDFEAFF2 CRC64;
MESEQLIRTG SGSRYFQMQS EHPNSFSFSL RPEPTRIFDQ LPKATIVQVS RPDAGDISPM
LLSYTIEFQY KQARSPSQFL RFVVFVVSFG LRLKSAFKWR LLKKAAHVFY LHFALKKRAF
IEEMLEKQEQ VKEWLQNLGI GDHTAVVQDD DADDDADDEA VPLHHDGSAK NRNVPSSAAL
PIIRPALGRQ ESIADRAKIA MQGYLNHFLG NMDIVNSREV CRFLEVSKLS FSPEYGPKLK
EDYVMVKHLP KIQKDEDSRK CCPCQWLNCC NDNWQKVWAV LKPGFLALLA DPFDTQPLDI
IVFDVLPASD GNGEGRVSLA KEVKERNPLR HAFKVTCGSR SIRLRAKSSA KVKDWVASIN
DAGLRPPEGW CHPHRFGSFA PPRGLSEDGS WAQWFVDGQA AFEAIASAIE DAKSEIFICG
WWLCPELYLR RPFSAHASSR LDALLEAKAK QGVQIYILLY KEVALALKIN SVYSKKRLLS
IHENVRVLRY PDHFASGVYL WSHHEKIVIV DYQICFIGGL DLCFGRYDTA EHKVGDCPPL
VWPGKDYYNP RESEPNSWED TMKDELDREK YPRMPWHDVH CALEGPPCRD IARHFVQRWN
YAKRNKALYE QTIPLLMPQH HMVIPHYMGR SEEIEIENIN VNNHKGIKRQ DSFSSRSSYQ
DIPLLLPQES DGAGAANGDP KSNGLSPSPN GLPFPFRKSR TGVVGPELPL TDFVDDFDMV
HRGKLTSDGV KQPGMKYPDP EWWETQERGN QGGFTDESGQ VGPRTSCRCQ VIRSVSQWSS
GTSQVEESIH NAYCSLIEKA EHFIYIENQF FISGLSGDEI IRNRVLEALF RRIMRAYNDK
KCFRVIIIIP LLPGFQGGLD DAGAASVRAI LHWQYRTICR GNNSILYNLY DLLGPKTHDY
ISFYGLRAYG KLFDGGPVAS SQVYVHSKIM IIDDCTTLIG SANINDRSLL GSRDSEIGVL
IEDKEMVNSY MGGKPWKAGK FSSSLRLSLW SEHLGLRPGE IRQIIDPVAD STYKDIWMAT
AKTNTAIYED VFSCIPNDFI HSRAAFRQSM ASWKEKIGHT TIDLGIAPEK LDSYHNGDVT
KADPMERLES VRGHLVSFSL DFMCQEDLRP VFNESEYYAS AQVFH
//
