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Database: UniProt
Entry: A0A022RHK5_ERYGU
LinkDB: A0A022RHK5_ERYGU
Original site: A0A022RHK5_ERYGU 
ID   A0A022RHK5_ERYGU        Unreviewed;       527 AA.
AC   A0A022RHK5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE   Flags: Fragment;
GN   ORFNames=MIMGU_mgv1a0212841mg {ECO:0000313|EMBL:EYU38375.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU38375.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU38375.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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};
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DR   EMBL; KI630481; EYU38375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022RHK5; -.
DR   STRING; 4155.A0A022RHK5; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF60; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT   DOMAIN          121..156
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          470..497
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EYU38375.1"
FT   NON_TER         527
FT                   /evidence="ECO:0000313|EMBL:EYU38375.1"
SQ   SEQUENCE   527 AA;  61180 MW;  64F7B0BE90615672 CRC64;
     LPDIRLDDGR NFEHQKCWED ICRAILEAQN LVYIAGWSIY HKVMLVRESS EQLPNGGDLS
     LGELLKYKSQ QGVRVVLLLW DDKTSQNKCF FKSGGLMQTH DKETRKFFKH SYVTCVLVCR
     IFSSQHQKCV ITDTKGHENN RKITVFLGGL DLCDGRYDTP DHRLYNDLDT VFKDDYHNPT
     FSVRQKGPRQ PWHDLHCKIE GPAAYDMLKN FEQRWKKATE CSDLTRFCKK ILGQHDYNLV
     NIEHISQIAS PSGTIPNDHQ SLWVSKEGDP ENWHIQIFRS VDLESVDGFP KNVLAAKEQN
     LVLVNKWAID RSIQMAYIQA IRSAQRFIFI ENQYFIGHLS LGHLIIKQPN IFRLINNFWS
     SFYCPNNLIP MELALKIASK IRANERFVVY VIIPMWPEGE PSSPTVQGIL YWQSQTMQMM
     YKIIAHELKS VNLKNAHPTD YLNFYCLGNR EENHKEESSS DSASEAFRRF MIYVHSKGMI
     VDDEYVIIGS ANINQRSMAG YRDTEIAMGA YQPHYTWAKK KEHPLGQ
//
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