ID   A0A423WD08_9PEZI        Unreviewed;       394 AA.
AC   A0A423WD08;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Fungal lipase-like domain-containing protein {ECO:0000259|Pfam:PF01764};
GN   ORFNames=VMCG_05971 {ECO:0000313|EMBL:ROW01286.1};
OS   Valsa malicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW01286.1, ECO:0000313|Proteomes:UP000283895};
RN   [1] {ECO:0000313|EMBL:ROW01286.1, ECO:0000313|Proteomes:UP000283895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-1 {ECO:0000313|EMBL:ROW01286.1,
RC   ECO:0000313|Proteomes:UP000283895};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:ROW01286.1}.
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DR   EMBL; LKEA01000019; ROW01286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423WD08; -.
DR   STRING; 356882.A0A423WD08; -.
DR   Proteomes; UP000283895; 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:UP000283895};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..394
FT                   /note="Fungal lipase-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019465660"
FT   DOMAIN          110..273
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
SQ   SEQUENCE   394 AA;  43879 MW;  9851844717EA6D5A CRC64;
     MRTPNLLTVL GIGIFGRLLV ADSLVGDELS IGERVDGDVT QDQVKLFTFY AQYAGASYCP
     IGDVGSHVYC KHDICPSDAK GNATIYNRYY GDNTGVAAFT AIDHDAEVIV VSVRGSVLTI
     DLKNWITNFR FEWAICEFGD NCKAHGGFLD AYQELRDRNV YKDVLLAKTL YPNYNIIVTG
     HSLGGAVASL LGAYLRDSKQ SPCSIVTYSG KCRLQTWTQW LTSDAVVFLK LDIYTFGSPR
     IGNAALVKYI YNQTGKTNRI THYNDVVPRV PPMFWPFCYR HTAPEYWLGA GPETRTSYTA
     DQIQICQGSA DDHCSAGLST PAVDSHLFYF VAISHCGESE SRLRLPNGTD EGEDPLDVKE
     ENRLTWFAKL DMQYVEDLRN DSGPAEKVGW WPTC
//