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Database: UniProt
Entry: A0A0G2EK83_9EURO
LinkDB: A0A0G2EK83_9EURO
Original site: A0A0G2EK83_9EURO 
ID   A0A0G2EK83_9EURO        Unreviewed;      1112 AA.
AC   A0A0G2EK83;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE            EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN   ORFNames=UCRPC4_g03291 {ECO:0000313|EMBL:KKY22596.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY22596.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY22596.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY22596.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY22596.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY22596.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty
CC         acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:28868; EC=3.1.1.116;
CC         Evidence={ECO:0000256|ARBA:ARBA00024531};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33276;
CC         Evidence={ECO:0000256|ARBA:ARBA00024531};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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:KKY22596.1}.
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DR   EMBL; LCWF01000076; KKY22596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2EK83; -.
DR   OrthoDB; 373802at2759; -.
DR   Proteomes; UP000053317; 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; PTHR45792; DIACYLGLYCEROL LIPASE HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR45792:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G02710)-RELATED; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          785..951
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1112 AA;  120350 MW;  8C491227A1817E20 CRC64;
     MPPAPDEEKA LQKYDDETKQ GPRPPPSRPL LPGFIAASIT TFTGATSLGL RVGTKIGGWA
     LGGAREATLG SLELSRAFAE AILFQAGRDV AGRRNGELGH AEAENILERS VSALHRAIST
     LSFTASAGFY MATVSMNAAS DWSQHSLATL NAILGSTESS RAVAAILTLM RDEFRKPEPD
     EKGESAGYLD LFAGTVAFVL LQRWGRRKTD RLFIEAGGEE IIWDAVIDDK GFRADVVGTQ
     LRRTEYFDGE HTDAQSRISR SVSFVSPGGD RPFEAVPREN GLATPTPRTL PLSLSAQAQS
     QLTDEEIRGH IMSQLPEGVH ANVTSETISA KTIRVDIYDA EMTDIAAPPG TVLIAERFHH
     GAEGAEGNSG NLPHQTVVFQ TSIKRTSSSE LHPLDKLRLT ASKEDAPESA VQDDAVSPTM
     SSPSDESAGE ELFMSDASEV PSTVPTAEPN APQKSSSRGP FTAPQPFGTV ANQKRQRKPP
     VKEPIHSPIA SSSRVLPKPK RIKPKSSASE PKIGNTLHKA FRKLSPTQST TNVREEVAKG
     LKPSQKQTEV HQRSINRPVP TSGLPRLSSD MQRLSSPFDK SLPKLPHQQK NTTPKRGIGL
     GKTRSDKDIW SSTEPSGSPQ SSKHHQRSRS FVPSLYSVAT RDSDGGSLII APKSMPRKSV
     FEDQENVVSL MRDGKVPGIF PDNHLIKNVR RFVRFSSASY GKSFLRIMGL TDPVANLSSS
     AELKNGDIHH EHESFSQYTG LPTDTILLSS FVDPHGVVTP LMKSADAALP LVHFISIDHE
     SRAVVLTCRG TLGFEDVLTD MMCDYDDLYW RGAPYKVHKG IHASARRLLA GTGSRVMLTL
     KAALEEYPDF GLVLCGHSLG GAVASLLAIL ISEPRTNEST SSLFATVSLQ KLLSHPHSTD
     KSAAPVDLPA GRSIHVYAYG PPATMSSSLR IATRGLITTI VNGADIVPSL SLGLLYDFRS
     IAINLKTDTT DALSAIKVRV MDRIRHSISS HFHADQAPPP DTTAGDGVGE DAWAWAALKT
     LRAGMGGEKL LPPGEVFVVE TTRVFDRSNS DGSGDYYPSL GRAATRVTLR YVRDVETRFG
     ELRFGSRMFS DHSPARYEAS LSALNRGILE DE
//
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