ID S3CD71_OPHP1 Unreviewed; 889 AA.
AC S3CD71;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=F503_05972 {ECO:0000313|EMBL:EPE10877.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE10877.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE10877.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE10877.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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; KE148146; EPE10877.1; -; Genomic_DNA.
DR AlphaFoldDB; S3CD71; -.
DR STRING; 1262450.S3CD71; -.
DR VEuPathDB; FungiDB:F503_05972; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_2_1; -.
DR OMA; EWRLDQI; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000016923; Unassembled WGS sequence.
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; 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 PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
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:UP000016923}.
FT DOMAIN 215..242
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 674..701
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 563..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 889 AA; 101583 MW; DA6DA7FB3818ADAD CRC64;
MAGDGKDKSS LSDKFKNPFR DMKEALEDKL ENSTPLRDAK IHLSHKKHQI GKLGNLFNSQ
HRHDEEHEKL CDEKRTKACE SHRYESYFPE RDGNLTKWYV DGRDYFWAVS ESLNNAKETI
YIADWWLSPE LFMRRPPYYN QEWRLDQILK RRAEAGVKIY LIVYREVEAA LACNSAHTKH
ALQALCPEGT PGYGNIRIMR HPDHNFLENA ADMTFYWAHH EKFIVIDYNI AYFGGLDMCF
GRWDDHTHAL ADVHPEGVIN ETWPGQDFNN NRVMDFQNVK DWKENELSKA VNGRMPWHDV
SMGIIGPCVY DIAEHFVLRW NFIKRDKYKR DDRFDWMQLR GREGEDEDLV GVQRPSHPVG
DYILHPLKPL EEIPELQPNQ GTVHAQVVRS ACDWSNGTLT EHSIQNAYSD IIRKAEHYVY
IENQFFITAT GDQQSPVHNT IGAAIVDAVV SNSERGKKNF KVIILIPAVP GFAGDLRGDA
AMGTRAIMDY QYKSICRGPE SIYEKIRARG VDPTKHIFFF NLRSYDRLAK TPAIKKMEAE
SGVSYKELAR AEAEEIMGEG IYGTVDTEGG RDKHMGHASQ QKNAEEESDF KRDSAKPDYL
EHATDVKRRF EASRNNSSIT QRTGADGEPG AGAVDADNKV KPVVAGHAMA GQGSLADEYW
EGEPNDEVQN WIQEELYIHA KLLIADDKYV VCGSSNLNDR SQLGTHDSEL SLVMQDTRIL
KSTMDGEPFE AGHHAATLRR YLWREHLGLL PPQTVDAAGD PNAQPPSPDS PNDVWDKDES
WNIVEDPLSE ELWTQWTEQA STNTEIFRHL FHADPDDHVK TFADYDRFMP SKGIAPGHIF
DQFMPAEDVR AKLDKVRGHL VWMPLDFLKD SPMAETGLQV NQFTESVYA
//
