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Database: UniProt
Entry: M5GCU1_DACPD
LinkDB: M5GCU1_DACPD
Original site: M5GCU1_DACPD 
ID   M5GCU1_DACPD            Unreviewed;       440 AA.
AC   M5GCU1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Putative phospholipase {ECO:0000256|PIRNR:PIRNR018169};
DE            EC=3.1.1.47 {ECO:0000256|PIRNR:PIRNR018169};
GN   ORFNames=DACRYDRAFT_19590 {ECO:0000313|EMBL:EJU06425.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU06425.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJU06425.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU06425.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; JH795855; EJU06425.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5GCU1; -.
DR   STRING; 1858805.M5GCU1; -.
DR   HOGENOM; CLU_022501_4_1_1; -.
DR   OMA; EAPCDGR; -.
DR   OrthoDB; 2787776at2759; -.
DR   Proteomes; UP000030653; 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; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR   PANTHER; PTHR10272:SF0; 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|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR018169};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR018169}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        78..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        270
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT   ACT_SITE        300
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT   ACT_SITE        365
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ   SEQUENCE   440 AA;  49950 MW;  48A9A75B96B8BE0F CRC64;
     MSLPRYKGPY DVGLTTLVLP VHPTASYGKC RVRGDEALRL EEVAFNVFYP ARPANRRKRG
     VHWLVRPFSL TVEGYSKFVG FSTWILAPLF FLLGAFAKMP VFANAPLRQE EPFEESQEKR
     LPDFTIDEKK QWPLVLFSHG LAGGRTTYST FCGRLASSGY VVLALEHRDG TGPMVYPKDK
     NGAVYAKPYS RVDEVECPDV DAKDLALHFR RTQLDFRKRE VYEAYRAFRA LVAGDSAHGG
     LQSIDGSPVD WDMFVGTVCA EEDVVLSGHS FGGATAFHIM SSPPPEGFNN IPISRSLVLD
     PWLDPLPSPG PNPRTDVPRP NLCVVLSERF TLWKAHFART SEVVSNWRNE KGTESWLMTI
     SRCRHDSFSD FPLIIPYSHP RGRLLHNVIQ RISLAFLTDR LELEFRKDER YPLHVIQPRI
     RKKRGKARLS APKGRVVWHD
//
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