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Database: UniProt
Entry: A0A395SHC4_FUSSP
LinkDB: A0A395SHC4_FUSSP
Original site: A0A395SHC4_FUSSP 
ID   A0A395SHC4_FUSSP        Unreviewed;       308 AA.
AC   A0A395SHC4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Putative secretory lipase family 3 {ECO:0000313|EMBL:RGP71796.1};
GN   ORFNames=FSPOR_3162 {ECO:0000313|EMBL:RGP71796.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP71796.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP71796.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP71796.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol +
CC         H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868;
CC         Evidence={ECO:0000256|ARBA:ARBA00043665};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+);
CC         Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868;
CC         Evidence={ECO:0000256|ARBA:ARBA00043831};
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       Class 3 subfamily. {ECO:0000256|ARBA:ARBA00043996}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RGP71796.1}.
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DR   EMBL; PXOF01000039; RGP71796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395SHC4; -.
DR   STRING; 5514.A0A395SHC4; -.
DR   Proteomes; UP000266152; Unassembled WGS sequence.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00519; Lipase_3; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002921; Fungal_lipase-like.
DR   PANTHER; PTHR45856; ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR45856:SF11; LIPASE_3 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..308
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017471455"
FT   DOMAIN          94..233
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
SQ   SEQUENCE   308 AA;  33251 MW;  5DCF42FC86E20EE8 CRC64;
     MTLLRVFTVA LAALTNIANA VPTDTSKRQS GDLPFPLAHF TNTVASVQNT YCGSSANTPG
     VKFGDQTLLH ALGNGDTVQR TNIYHSESLG IIVAVQGTNL SSLVSISQDI QALPILPDPR
     LGLPLGSLVF AGWQTAWFNG WVAVSKALAE TIKQFPNDQV IVTGHSQGAA IALLTALSIQ
     KEFSNVTTIR EIIAYGIPRV GNPKFADAFD AIFPGRYTGV VNGEDWVPSF PTQPIYQHPS
     GMVWINPANT TSWKYYEGQE NPKGPHSRVG KIFYPNTLQF YWGDHQGIYM HSSMGTTLGP
     CPAQVGGF
//
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