ID A0A0D2A1S9_9PEZI Unreviewed; 538 AA.
AC A0A0D2A1S9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 28-JUN-2023, entry version 32.
DE RecName: Full=Putative phospholipase {ECO:0000256|PIRNR:PIRNR018169};
DE EC=3.1.1.47 {ECO:0000256|PIRNR:PIRNR018169};
GN ORFNames=PV09_08165 {ECO:0000313|EMBL:KIW00275.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW00275.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW00275.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW00275.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC Evidence={ECO:0000256|PIRNR:PIRNR018169};
CC -!- SIMILARITY: Belongs to the serine esterase family.
CC {ECO:0000256|PIRNR:PIRNR018169}.
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DR EMBL; KN847565; KIW00275.1; -; Genomic_DNA.
DR RefSeq; XP_016210144.1; XM_016362024.1.
DR AlphaFoldDB; A0A0D2A1S9; -.
DR STRING; 253628.A0A0D2A1S9; -.
DR GeneID; 27316138; -.
DR VEuPathDB; FungiDB:PV09_08165; -.
DR HOGENOM; CLU_022501_3_0_1; -.
DR InParanoid; A0A0D2A1S9; -.
DR OrthoDB; 2787776at2759; -.
DR Proteomes; UP000053259; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016715; PAF_acetylhydro_eukaryote.
DR PANTHER; PTHR10272:SF11; PHOSPHOLIPASE-RELATED; 1.
DR PANTHER; PTHR10272; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR Pfam; PF03403; PAF-AH_p_II; 1.
DR PIRSF; PIRSF018169; PAF_acetylhydrolase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR018169};
KW Lipid degradation {ECO:0000256|PIRNR:PIRNR018169};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR018169};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053259};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 71..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 352
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 379
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 443
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ SEQUENCE 538 AA; 60356 MW; 3F8EAAC12F640D60 CRC64;
MAPNDAHYSD DVELADFDED DPIAEHDSPL PRRPGMDSPW KQPRWLTQQT KHWRIPDSFV
RLIQPRLTWR YALFILLLLY VLYCLVRGSP LLASNLPKYT GPHEVGVMDL EVPLEKPVMI
SQTVYKETGQ RAFELETVLF KLFYPAAKGS RSSKPSHYWV PKPVSLTARG YAKFASIDNF
IMRPIMTAAL WAIAGGITIP AKVDVPLAEP VDEVAFPIMV FSHGMASSRT DYTHYAGELA
SRGHVVAMIE HRDGSCPGSV LVRADGTTKH ILHFKESELL PAPETEMDTP RMKREQLNFR
QAEITETISV LRRINSGRGE QTRHANTRGE GTHLADWEGR LDFNHLVIAG HSYGATGALQ
ALKHANSSSN PAVGGIILDP GKSSGPMNHD IDVPILVIHS NSWSSKHSIF EGRPHFDYVK
DLVVEVRDRV GASWFLTSLG TTHPSVTDAP LIEPLLLSWT TGATIDVRQG VQEYVKTSVE
LYAWLKDGKR QGLLAEAVTH DAYEHWVNEE RKNEFPAKYR KYWEVHVTPD PVLNSKAL
//