ID A0A1V6R373_9EURO Unreviewed; 1169 AA.
AC A0A1V6R373;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=PENSOL_c018G07380 {ECO:0000313|EMBL:OQD95938.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD95938.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD95938.1}.
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DR EMBL; MDYO01000018; OQD95938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6R373; -.
DR STRING; 60172.A0A1V6R373; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000191612; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; 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; 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:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000191612}.
FT DOMAIN 296..323
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 933..960
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 130619 MW; F156BBD4954F9D83 CRC64;
MSKQDDLAYG GYYQGAERGS GDGSRGLGDT FKKLRDTYKN HGSSQGQANQ TYDPSGYQGQ
SYPTQTEPQY TQNTSGQQQN PNYHGKPQKE DKLAGLLGKL QGTVTEFGSE FAQKIGTTID
PQAYAEYGPS KPNTEHRFGS FAPPREHNDA KWYVDGCSYF WAVSRALENA RESVWILDWW
LSPELYLRRP PAKNEQYRLD RMLQAAAQRG VRVNVIVYKE VTQALTLSSS HTKHALENLH
PNIAVFRHPD HLPDRQELAA SITSTFQNMS LDSASLSKMS KDTLKGLYGM NDDVILYWAH
HEKLCLIDGR VAFMGGLDMC FGRWDTNQHE LSDLHPSDVS QTVFPGQDYN NSRVLDFQDV
VHWENNQLDR KTMSRMGWSD ISVSLHGAAV EDLRRHFVER WNFIYDLKYK VRSDSRYARL
ALHGRPASST GPSTGQQQAG SPQPNLYPSG QASPQVQAPA PSWQQKPSGV TSPTYPPPPG
QAPSPSQPQS QSQPQHQQSA EAYQPYNSAS ASNYPPPPAQ TSSNQQQYQH QNTSTSYQPG
NASTYPPPPS QSPLGSQSQS AQSPGHDTSQ YSYTGSSFPP PPPGPPPAQS TANTSYQPYQ
QAQQQEQKPY FPPPPGQEAS HSNTRGVNDY QHEGDRERGS LAPRRFREDL TQYGSTLRGQ
LAGQIHQYQD RLTTYGRPSS SQGRGNMSCQ IVRSCAKWSN GSPLEHSIAD AYCAIIRNSE
HFVYIENQFF ITATGDSQRP VKNQIGAAIV ERILRAARAG QKYKIIVVIP SVPCFAGDLR
DDETLGTRAI MEFQYNSINR GGHSIMEMIA KEGFNPMEYI RFYNLRNYDR INNGSMMAAA
EQQSGVNYED ARRQYDLNTA GPGGYAPSTT RSAFDTSAPF QKYQQAANQV QGGHASSNRW
DSVSECYMLG GEDIRKVPWD GHPDAEINAF VSEELYVHSK VMIADDRVVV CGSANLNDRS
QLGDHDSEIA VIIEDFTPVA SSMNGKPWTA SRFASSLRRQ LFRKHLGLLP PQDYQRPDAN
FEPVGVPNEF DFDCPESKVV ADPLSDTAQS LWNSRAHTNS EVFRKVFHAV PDDSVRNWAE
YKEFYEYYFH KTEKRASEGM EGSARPARFQ WGHVVSDDFA PGAEGAKQVK ELLSQVKGTL
VEMPLMFLIE EDIAKEGLTL NDLTEPLYT
//
