ID A0A2H3BV18_9AGAR Unreviewed; 1581 AA.
AC A0A2H3BV18;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=ARMSODRAFT_970779 {ECO:0000313|EMBL:PBK74731.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK74731.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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|PIRNR:PIRNR009376}.
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DR EMBL; KZ293418; PBK74731.1; -; Genomic_DNA.
DR STRING; 1076256.A0A2H3BV18; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000218334; 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; 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 InterPro; IPR001849; PH_domain.
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; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 2.
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:UP000218334}.
FT DOMAIN 785..812
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1078..1105
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1431..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1472..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1581 AA; 178527 MW; BF17857E9A7EA1CD CRC64;
MSRIAEIVGQ TIENDRRHRV SSGEEEHPRS ALSSPSHATP RASGQEQRVA HFRTPPSTPS
MRTGPPRSLS YSYSTPNSPA TSRNNSRHEN SDLKPDSDLE QQGDFPFVSP STDFRDALEV
RNAAADKKGK KRESKLLDES WNPLKWFHES PKEEKSGFDF DGVSVEGHPR EPVTDGEESS
KLPPSGLRRT SSGPPAPPER KTGPKWGRLR SLIPNVVNQS SHSPITPGPS AVTSNAVNIT
DELITGGLST LMLRLWFERD ENDLRRVPVL FHRLRIRVSD SLHPLHGHKS VFRIECEYAN
GAARWVVYRQ LRDFISLHYH YSLSNALQRN VEKLPEFPKT SALMFRLFSN PDTNLQTGLP
YFKFLQKEGR EKGNQVGHAD FARLQREALE NYLIDLIRAV MFHPAANRLA SFLEISALSM
YLSQSGGAQY KAGYMRIEAA EGEFGRKGSS WRAKRESRWC AVRESYLVAL VEPGELTVWD
AFLLDSDFKI ERPKRYYRQG LSLLHSDTHN EDDSHLKRKE RKSEASAETE HMSLMGSIKG
RFSRAFHLNH SAHFHPGHGE EEVQDGTSSS SSSVASHAPT PMLDPSTNTN PLSGGVDHQD
MVDGEPWQAE KKKKKKTQTD VSKHTFYISN SQMRLRLYAR NERQMLQWIT AFERVAAASH
YTGTNRFDSF APIRLNVAAQ WLVDGRDYFW NLSRAILLAR ESIYIHDWWL SPELQLRRPN
KERYRLDRLL ERKAKEGVKI CIIVYKEVSS RTTPTDSNYT KQRLASLHPN IMVQRSPSHF
QTGTFYWAHH EKLCVIDQAI AFMGGLDACF GRWDTPQHAV TDDIEDESSQ VWPGKDYSNA
RISDFHTLNK PQEDMYDRTK IPRMPWHDVG MQVVGQPARD LARHFVQRWN YLLRIKNHSR
AMPFLLPPPE FRPGELTQMG LTGTCEMQIC RSAGPWSLGT ASRIEHSIQN AYLKAIQMSE
HFVYIENQFF ITSTTVNDVR IENKIGDALV HRIIKAHRDG TRWKCCVVIP LLPGFAFALD
HSDGSAIRII LECQNRTISR GPNSIFGRLR KEGIDPDDYI TVFSLRNWGK LKDVLTTEQV
YIHGKVCIVD DRLAIIGSAN INERSQRGDR DSEIAAVIRD TDMIDCTMAG KPYKVGRFAH
TLRVRLMREH IGVDVDALYE EDLMASDPVK SEQEPVPSNS SGEQLHRQEN GVAESSVAGD
SHTTSDNDRR ALNGSSEATV HTTTQGSAET DDDLDTAFPK NTRTGKNVPS TTLEEKVVQD
HLNGNKPRAN GHASNDRVQD IKRRSEDKPS PNGAPHQALT SNGNLHGTPA DASRSPEIDD
QSPHLRTGMD SGDDEERTVP RARSTLRKNL GSKLGQNNKW TVPTPRPHVD ANGFEDPVSD
AFWKDVWVAC AVHNTEIYRK VFHAVPDDLV TTWKQYKEFV LHHERLNKPA ADSTTLEPVG
RVPSETGDDT IPSNDVPAPA EHVAEHSDGH VHINEEPDLN SSAGVADKEP ARARSRSTRS
TEPFMKAERD EMEKLLGELC GHLVIYPNRF LEGEDVANNF LFNADREGLH MTKKAITALN
DLERFAHPVA VAICFFAHPR I
//
