ID G2Y7A4_BOTF4 Unreviewed; 863 AA.
AC G2Y7A4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=BofuT4_P108900.1 {ECO:0000313|EMBL:CCD48506.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD48506.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
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DR EMBL; FQ790293; CCD48506.1; -; Genomic_DNA.
DR AlphaFoldDB; G2Y7A4; -.
DR STRING; 999810.G2Y7A4; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_2_1; -.
DR InParanoid; G2Y7A4; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
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; 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; IPR016555; PLipase_D_euk.
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 PIRSF; PIRSF009376; Phospholipase_D_euk; 3.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
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:UP000008177}.
FT DOMAIN 213..240
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 631..658
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 863 AA; 97918 MW; 8E373F19066AA237 CRC64;
MSHFFHDAKA AIGDFVHEVE AEVSKVAGIS DGEKHSHTHL GEACHTLHIN GNENRFGSFA
PQRTGHDIKW HIDGCAYMWA VSVALEEAQE SIWILDWWLT PELYLRRPPS ANEEYRIDRM
LLAAAERGVK VNIIIYKEVT KVLTLCSEHT KKALEVHPNI SVFRHPDHVP SGIHVESELI
TDLKNFSLKD FDLAQLPKEG IEALYGARND VILYWAHHEK LCLVDSKVAF MGGLDLCFGR
WDVNQHPIAD AHPSNLDNIV FPGQDFNNAR VYDFENVTDW QENKLDRTKY SRMGWSDLSM
SLTGPVVEDL RAHFVQRWNF IFREKYDTQD TRYTALSLIP NDIPDGYYNE DGTNVGSSTE
GTISDTFRRA GTFFGRSGGN SGYGDDQNGV SIQLVRSCTE WSNGVATEHS IANAYIEVIR
RSQHFVYIEN QFFITACSDE QHPVENKIGA AIAERIIRAY QNGEQYKVIV CMPSVPAFAG
DLHGDDALGT RAIMEYQYSS ICRGGNSIME TVAKAGVPDP KDYIRFYNLR NYDRLNDNGT
MAQTEQESGV SYENARKEHD DIVGAGYGGY GEETGARRGQ ENYEYDQYQR AAPRSQEHDT
VAACYMEDGP SITSIPWNGT PEAELDAFVS EELYIHTKLL IADDRVVICG SANLNDRSQL
GTHDSEIAIV IEDTETVDSY MNGREFRAAK YATSLRRQLF RKHLGMVAPQ DWTRPDANYM
PINKDPNDYD WGSDYDIAVQ DVFSPEFTDL WNGRARTNTE VYSKVFHAIP ADNVRNWDDY
HEFYEQYFVS PSDKDTKEED KEPAKYLYGH VVKEEFPGGV EEVKEELSRV RGMLVEMPLL
FMDGVDFAKE GLSFNALTAT IYT
//
