ID A0A319DPA8_9EURO Unreviewed; 1199 AA.
AC A0A319DPA8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 02-APR-2025, entry version 23.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=BO71DRAFT_371184 {ECO:0000313|EMBL:PYH98474.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH98474.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH98474.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH98474.1,
RC ECO:0000313|Proteomes:UP000247810};
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; KZ825811; PYH98474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319DPA8; -.
DR STRING; 1448320.A0A319DPA8; -.
DR VEuPathDB; FungiDB:BO71DRAFT_371184; -.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000247810; 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: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 FunFam; 3.30.870.10:FF:000034; 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; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF186; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 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:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000247810}.
FT DOMAIN 298..325
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 965..992
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..62
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..93
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..454
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..505
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..584
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..603
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..634
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 133068 MW; 212C9A9649A40584 CRC64;
MTRQEEGLAY GQYNQDSARG SSSDTARGFV GDTFSKLKQT YKSQQTQQGT SQQQSQSAGY
GAENQTYQSQ GSSQPHAAQG SPQASQGQKP QKPQKQDKFS GLFGKLEELG NEVAQKLGTA
LDPQAYAQYG AVKPHSENRF GSFAAPRQGN DVKWHVDGCA YFYAVSKALE SAKDYIWILD
WWLSPELYLR RPPAKNEQYR LDRMLQAAAQ RGVRVNIIVY KEVTQALTLS SHHTKHYLED
LHPNIAVFRH PDHLPDRQEL EASIAQSVQN LSLDAGNLVK MSEDTIKGLY GMREDVILYW
AHHEKLCIID GRVSFMGGLD MCFGRWDTNQ HALADVHGQD LNEIVFPGQD YNNARVSDFH
DVAHWEQNQL NRTKTSRMGW SDISVSLHGQ VVEDLRQHFV QRWNFIYDSK YQSRENSRYS
RLPLYGRPTS SNAQQQQAPQ QGGQAQQPAI APQPGANPGP PTPSWQQHAA SPQTSGSTTN
TQSSTGPTPS WQQQSAGSQS GGYSSNTQPP NTASPATPTW QQHAAPAQPS YNTQSPQATS
PSWQQHAASP QQHSAQPPQG SQEAPSYQQQ SSNPPASSSQ GSAQNYTYTG NSFPPPPSGP
PPSQGSGQGQ QYQTQGQTQT GQGQYQALGQ TQTGHSQAPY YPPPTQETQH VQQHSQTRGV
QDSHHGGYAD SDRGFGRLRE NFTGYSNSLR GELAGQIHHY QDRFSGQGSR PGVHPRGNMT
CQIVRSCSKW SNGTETEHSI QDAYVAVIRN SQHFIYIENQ FFITATSDAQ KPVENKIGAA
IVERILRAAR AGEKYKIMVV IPSVPCFAGD LEDDSTLGTR AIMEFQYNCI NRGGNSIMEL
IAKEGFNPMD YIRFYNLRNY DRINVSNPLA AAEQRSGVNY EDARKQHDVT TGGPGGYGPG
APRAAFDTTA PYQQYQQAAQ QVSGGKSAPG KWDSVSSCYM LNGEDIRNVP WEGSPEAEID
AFVTEELYVH SKVMVADDRV AICGSANLND RSQLGTHDSE IAIVIEDYTP VQSRMNGKPW
TASRFASSLR RQLFRKHLGL LSPQDPQQPD ANYEPVGVPN VLDFESPESQ IVADPLADTL
QSMWNTRANT NTGVFRKVFH SVPDDTVRDW ATYKEFYGYY FHNSDKQAYG EDDSKPSRYE
YGHVVRDDFP QGPEGVRQVK ELLSQVKGTL VEMPLMFLIN EDVAKEGLTL NELTEPIYT
//
