ID A0A395SR46_FUSSP Unreviewed; 823 AA.
AC A0A395SR46;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=FSPOR_997 {ECO:0000313|EMBL:RGP74933.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP74933.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP74933.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP74933.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP74933.1}.
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DR EMBL; PXOF01000018; RGP74933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SR46; -.
DR STRING; 5514.A0A395SR46; -.
DR Proteomes; UP000266152; 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: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; 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; 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 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:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT DOMAIN 180..207
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 608..635
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 521..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 95444 MW; F4B1807CB2C2278E CRC64;
MGEHKRTESL MEKLKLHDAK VHLVHQKHDE EHEQRCDEKR SAICEQNRYK SYFPIRAGNR
VKWYVDGRDY FWAVSIALEN AKESIYIADW WLSPELFLRR PPYKEQEYRL DKLIKRKAEA
GVQIYVCVYK EVEQALTCNS AHTKHALRKL CPKGTPGYGN IHVARHPDHN VFENFGDMTW
YWAHHEKFIV IDYEIAFVGG LDLCFGRWDN HQHPLADIHP ADVRDEIWPG QDFNNNRVMD
FQKVDSWQDN ELSKADYGRM PWHDVAMCIQ GSAAYDVAEH FILRWNFVKR DKYKRDERFN
WLMLEGREGE DEDLVGVQRP KHPVGDYVRH PYTPLSEKKL DGIGTVNCQI VRSSADWSSG
ILTDHSIQNA YIEIISKAQH YIYIENQFFI TATGDQQAPV KNQIGRAIVD AIVRAAKEGR
KFRVIVLIPA IPGFAGDLRE EAATGTRAIM DYQYKSICRG EHSIYGQCRA EGVDPTKYIF
FFNLRSYDRL NKTPGIIKAE KETGVSYQQV QRAEAEEIMS EGIHGSYDPE DSEGDEHMRR
DKDKKELDED IKKTMEARKK FEAALPPENI HTTSSVAHHA MADTGEGLKG ESWFEEDPES
EIKNWIQEEL YIHGKLLLVD DRIAVCGSSN LNDRSQLGDH DSELSVVMED TRLIPSVMDG
QPYEAGYHAA TLRRYLWREH MGLLPPQEHD ASKDINAMPV NVNPDNDIYD RDESYKFVED
PLSDEVWDMW TSRADKNTML FRHLFHADPD DHIKTFEDYD RYLPPKGVKA GHIFDQFLPV
ADAREKLSQI KGHLVWFPLE FLSEAEMAEW GLQVNAVTES IYT
//