ID A0A3N4JS39_9PEZI Unreviewed; 1826 AA.
AC A0A3N4JS39;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=L873DRAFT_1791555 {ECO:0000313|EMBL:RPA96574.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA96574.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPA96574.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPA96574.1,
RC ECO:0000313|Proteomes:UP000276215};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(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 ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR EMBL; ML120413; RPA96574.1; -; Genomic_DNA.
DR STRING; 1336337.A0A3N4JS39; -.
DR Proteomes; UP000276215; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
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 CDD; cd06093; PX_domain; 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 SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000276215}.
FT DOMAIN 411..617
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 878..905
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1184..1211
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1632..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1675..1777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1826 AA; 203320 MW; 75DCBFEC81EF71F7 CRC64;
MATKPLESGD EQQQVQRQHD RPPRPLLAPI VLNTSNSSGK KRPNPIPHLE PSPMLRTRST
PVSPTQLIDM EPPPPIPAAI EEQGYRSRPS SQHSIRWKDC SDDEGVQSDG GGYKTPGRPS
SAATESTTAW ELSPGGESVA GPSNSARGRR RRGGFFNAGN HSGSSFENAY AYDGTATAAR
ANRPSGDYST GDETEIPLPA KKQGFFSRLR NFGSGNGVHG RSQSGWTIES VGDSTTPIGP
FSPVPYSPAV GGAPDEDEEL EDTDHTMGGR SVRSATPEGS RTAPGTPRAP HGPRRRATVT
NIPEEAGTQS DRGYSSRRAS FRRITQFNHR RSHDGGESLP TTPMYGSGWR ALKAGLKMMG
QRKKEESRVD REKSAELVAE LTAATPAAVI LASMFQRDEH GNKRIPILLE QLKVKIVDSN
PTSKGAGRAH TTFRIELEYG SGLTRMKWVI HREFRDFVNL HSRYRLADIS NTTFGGRDAY
KLPKFPRATI PYLRGVRGLG SEDDSESENS GAEATAAGDG AAAVQKKKRR PHIRRMSSNF
LGEHAPQGIA TGIAAGLGTL TAPIGAPGST QNPRKEGFAI RQRQQLEDYL RSLIRIMIFR
PDSNRLCKFL ELSALGVRLA AEGSYHGKEG YLIIRSSKGS DYRRAWNPSA VAKRHSPKWF
LVRHSYIVCV DSPEEMNIYD VFLVDSKFMV NAKKSLRKKP QDMAITNGNP ARPQHHSLVI
QNSERTLKLL AKHERQLGQF TESIKFMRDN TDWAKPQRFE AYAPVRTGVF AQWLVDGRDY
MWNVSRAISM AKDVIYIHDW WLSPELYLRR PAAVSQKWRL DRLLQRKAQE GVKIFVIIYR
NIGAAIPIDS TYSKYSLLDL HPNVFVQRSP NQIRQATFFW AHHEKILIVD HMVAFVGGLD
LCFGRWDTPQ HSLVDDKPTG FEEGSNRADP DSFQLWPGKD YSNPRVQDFY SLDKPYEEMY
DRSRVPRMPW HDIHMQVVGQ PARDLTRHFV QRWNYLLRQR TPSRPTPVLL PPPDFTQAEL
ESLGIDGTCE VQILRSASSW SLGTPSTTEC SIMNAYIKSI ELSEHFVYIE NQFFITSTEW
EGTKIENKIG DALVERIIRA YNNDEDWRAI ILIPLMPGFQ NTVDSQDGTS VRLIMQCQYR
SISRGEYSIF GRLRAHGIEP EEFIQFFGLR NWGKIGPEKA LVTEQLYIHA KCMIVDDRIA
IIGSANINER SMLGHRDSEV ATIVRDTDTT MSSMAGKPFR VGKFPHTLRL RLMREHLGID
VDELMACEHR VDSDMKGEEW EEQIREWSNQ GDGADEKFLS QQHRKNGSVA MVTSKLTLED
EAVLRQEELR SFNHDVDWEQ ENNPHLKTRK RGTTDNRITG NQEHRNDVKG YGPDNMHARA
RWGTPSTVNE KVSEEMRSPV SPPPVTIRSP TSETVRPSAE AKSPIEGNRQ NLSSTNLSSP
ASSYPRNSTI SSSRASSSDG PGNANLPPPP GPERVSSVEL GLPQLSQLPP LPVTSDQDIG
GPFTTRPVSV PGEGPPVPLL DTMEVPKVEP DMFMDPLNES FYQGIWNACA QNNTKIYRQV
FRCMPDNEVK TWAAYKEYAA YGERFSQSQG VDKSKMRRQQ ETPGKSGPPG ADLSGIAAAI
AVPGEKLGTL GDKVGEKVGA PVHDGNSHLP QGNVKDWAIP TVQSQDELNR VVGGDAMGEK
SEHPPIHKSS RPRSTSLASS RLNTAVTAAT TSTTAGAPNS SHSHDSSEKK LDPNLLSSGA
GSISYSSNTN LGNGGSTKRR RRGTTRSSKR DFHASEPLLE KDVAEQLLNL TQGHLVVWPH
EWLSREEEGG NWLYSIDQLA PIEIYN
//
