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
//