GenomeNet

Database: UniProt
Entry: X0B8Y4_FUSOX
LinkDB: X0B8Y4_FUSOX
Original site: X0B8Y4_FUSOX 
ID   X0B8Y4_FUSOX            Unreviewed;       580 AA.
AC   X0B8Y4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Putative phospholipase {ECO:0000256|PIRNR:PIRNR018169};
DE            EC=3.1.1.47 {ECO:0000256|PIRNR:PIRNR018169};
GN   ORFNames=FOMG_02107 {ECO:0000313|EMBL:EXK49607.1};
OS   Fusarium oxysporum f. sp. melonis 26406.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089452 {ECO:0000313|EMBL:EXK49607.1};
RN   [1] {ECO:0000313|EMBL:EXK49607.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=26406 {ECO:0000313|EMBL:EXK49607.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum melonis.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXK49607.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=26406 {ECO:0000313|EMBL:EXK49607.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of the Genome Sequence of Fusarium oxysporum f. sp. melonis
RT   26406.";
RL   Submitted (MAY-2012) 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; JH659329; EXK49607.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0B8Y4; -.
DR   VEuPathDB; FungiDB:FOMG_02107; -.
DR   HOGENOM; CLU_022501_3_0_1; -.
DR   Proteomes; UP000030703; 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|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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        117..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        397
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT   ACT_SITE        425
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT   ACT_SITE        489
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ   SEQUENCE   580 AA;  64349 MW;  C729A5FDAB5EDCBE CRC64;
     MRPDPLASSP PSSLTNKKHS THHLTTHHFP HHNLLVPILI PQEMPQSQNS IDLELNRLNS
     PFSDSSSDPD LPLTMDPPAP KPRWLDPRPS SIFTRITSSV KPFAQYLRHV LRPRLTWRYV
     ACSVIGVYVL YCFVTWQPFF SSRLPAYSGP HDVGAIDLEI PLEKPKRLSE TLLKSTKKPA
     FEVESVLFTV YYPAVKGARS KDAPHPWVPK PLSLTAEGYA RAAGVNNFII RPIFTFALWV
     LVGSIKIPAK VDVPLLGSDG EKFPVMVFSH GSVSSRTDYT HYLGELASRG HVIAALEHRD
     GSCPGSMVQI KNKKDRPVFL LKEGDLISEP PMNDTLLKKE QLAFRTEEIM QAIRVLKDVN
     DGKGKDIFTS SSRGEGSTLD GWKDRLDFKH LTINGHSYGA TGALQALKTA NTTAANPAIG
     GIALDPGKSS GQLNTNIPVP LLVVHSNSWS KTHSIFFGRP HFDTVLDLVR GVRDEVGSAW
     FLTSVGTAHP SVTDAPLLQP LLLNFATGAT ADVKKALGEY VKVTMDFLEF TKTNKENGVL
     DEAVTHEKYG EWVSKEREKS FPKEYAKYWE VHVCPLDQDK
//
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