ID A0A395GRB1_9EURO Unreviewed; 832 AA.
AC A0A395GRB1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 02-APR-2025, entry version 22.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=BO80DRAFT_447904 {ECO:0000313|EMBL:RAK97912.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK97912.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK97912.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK97912.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ824458; RAK97912.1; -; Genomic_DNA.
DR RefSeq; XP_025572240.1; XM_025721638.1.
DR AlphaFoldDB; A0A395GRB1; -.
DR STRING; 1448316.A0A395GRB1; -.
DR GeneID; 37226503; -.
DR VEuPathDB; FungiDB:BO80DRAFT_447904; -.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:TreeGrafter.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
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:000032; Phospholipase; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
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:SF128; 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; 2.
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:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT DOMAIN 196..223
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 620..647
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 832 AA; 95700 MW; ABD2D947BC4AB27A CRC64;
MDLFKSKIEN LEEHLKETRI EEKASHFKHK VGKFFNIVNP NHRHDEAHEK ATDAKRATIA
ESHRFKSFAP IREGNKVKWY VDALDYMWAV SIALEEAKET IYIADWWLSP ELFLRRPPFM
AQEWRLDQVL KRRAEAGVKI YVIVYKEVNQ ALTCNSAHTK HALRNLCPEG TPGHGNIRVL
RHPDHNIFEN AADMTLYWAH HEKFIVIDYA LAFIGGIDLC FGRWDAHQHP LADVHPSNLR
NEIFPGQEFN NNRIMDFQSV GDWQANELSK ADYGRMPWHD VAMGVMGDCV YDIAEHFVLR
WNFIKRDKYK RDKNVDWLML EGRLDEDEDL VAVQRPKFPC GEYLQHPLSP LDTKPLGQQG
FARAQIVRSS ADWSSGILTE HSIQNAYKEI ISQAQHFVYI ENQFFITATG DQQAPILNTI
GRSIVDAVVR AGKEGRKFRV IIVIPAIPGF AGDLRQNAAT GTRAIMDYQY KSILRGEHSI
FGQIAAQGVN PREHVFLFNL RAYDRINKTP ALLKLESEAD VTYNDIQRGI AESIMSDSVH
PAIGKEGDKH EVGYEDAQQE KEIRLARLRK YEEQHERFTE LEGLKGSDTV AHTTMLNGGK
MSDEPWEGRP EDELENFVQE ELYVHGKVCI VDDRVVICGS ANINDRSQVG YHDSELAIVV
EDQDFIGSTM DGKPYRAARM AATLRRQLWR EHLGLLPVQD YDASQHPNAK PPYQCMNHIL
EGPENDFVTD PMSDELWEMW TGRATVNTDI YRMLFRADPD DKIRTFEDYD NHCPRGTKQG
HLFDPYQPIE EIRAKLDKIK GHLVWMPLEF LKDANMAEPG LAVNQITESI YT
//
