ID A0A316V1B3_9BASI Unreviewed; 1032 AA.
AC A0A316V1B3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE Flags: Fragment;
GN ORFNames=FA14DRAFT_140075 {ECO:0000313|EMBL:PWN31347.1};
OS Meira miltonrushii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN31347.1, ECO:0000313|Proteomes:UP000245771};
RN [1] {ECO:0000313|EMBL:PWN31347.1, ECO:0000313|Proteomes:UP000245771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN31347.1,
RC ECO:0000313|Proteomes:UP000245771};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
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DR EMBL; KZ819611; PWN31347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316V1B3; -.
DR STRING; 1280837.A0A316V1B3; -.
DR InParanoid; A0A316V1B3; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000245771; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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; cd01254; PH_PLD; 1.
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; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
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 InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896:SF76; 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; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
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:UP000245771}.
FT DOMAIN 582..609
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 905..932
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PWN31347.1"
FT NON_TER 1032
FT /evidence="ECO:0000313|EMBL:PWN31347.1"
SQ SEQUENCE 1032 AA; 117613 MW; 27B4C8D290D3D235 CRC64;
MRGGNNTNGN GSGNDKNVQD DVQHDNSNLL NSDTTDGQDG SNTIKGIDGL HGASSATPQS
SARWNALRQR LRENAAKKGK GTINRKARVV GQMSVVTEMQ TGILPVFMIK MSMERDEQGH
RRIPVLLNHL HLRISDSVNP LHTSSAVFRI ELEYGDGLIR WVCYRSLRDF INLHTHYRAA
AIKGYLGRPV GSTEGDVGVP SFPKTSLPYF TQLQRQGWGK GAGDNGKARF AQAQRSALED
YLIEIIKRTM FRPEANRLCK FFELSTLSIT LASRGGYQGK QGYLRILSRS SRKDAQGSLL
TPVTWIKAHE PKWCIVRESY IAIVDQPDST QVFDVFLLDN QFEIERPKRL YRQTLHLAQD
FGHGNSNETS KSQQKEIPSH SAALDGKDET AILTEGHFRD PGDDEYSGSH RSKADAKVSS
HTFHIKNAER KLKLVANNER QMNQFIASME RVARRNIFGR KNRFDSFAPI RLNCNARWIV
DGRDYYWQVS RALSRAKDCV YIHDWWLSPE LYLRRPGSPK YRLDNVLKRK AEEGVKVFVI
VYNEVSNNFT PTDSNYTKQR LIGLHPNIFV QRSPSHFQTG TFYWAHHEKL CVIDETIAFM
GGLDLCFGRW DTSSHVLTDN HLMENEDAKG SSPQPVGSMA HSANLMGPGA EGREFYVWPG
QDFANERVVE WHDLTKPEVD LFDREHFPRM PWHDIGLQLI GQPARDLCRH FTQRWNLLLR
IKNHKRLMPF LIPPSDFSPS DLKKFDLTGT CEAQICRSAG PWSMGTANTV EHSIQNAYLK
SIQMSDHFVY IENQFFVTST EARGTVIENM IGEALVSRII RAEREKTSWK AIIVIPLIPG
FPMPIDHPDA SSVRLIVDLQ YRSISRGEDS IFSKLRRRGI DPEQYISFFS LRQWGKLPSG
RLTTEQVYIH AKAMIVDDRL AIIGSANINE RSQRGDRDSE LACVVRDTDM IDSTMAGKSY
KVGRFAHTLR VRLMREHLGY DVDADEVQSD SGEKDDDNRQ LFIDPLDSKF FKDLWVSSAT
HNTQIFRKVF RS
//
