ID A0A0N0RSD9_9BASI Unreviewed; 944 AA.
AC A0A0N0RSD9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=Malapachy_0806 {ECO:0000313|EMBL:KOS14872.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS14872.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS14872.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS14872.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-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 -!- 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 -!- 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:KOS14872.1}.
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DR EMBL; LGAV01000003; KOS14872.1; -; Genomic_DNA.
DR RefSeq; XP_017992504.1; XM_018135319.1.
DR AlphaFoldDB; A0A0N0RSD9; -.
DR STRING; 77020.A0A0N0RSD9; -.
DR GeneID; 28727194; -.
DR VEuPathDB; FungiDB:Malapachy_0806; -.
DR OrthoDB; 1424726at2759; -.
DR Proteomes; UP000037751; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:SF8; DIACYLGLYCEROL LIPASE-ALPHA; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 571..740
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 107320 MW; 89443F48EB3FFF07 CRC64;
MNSPSLSQSD ELPETPVMMP GGYFHDPNQF PMLPPPLIDD EGSDPRSFEG LLGVRRMREQ
QQRRQQYEAL VKRNRPAHRV DAFTAFINFV RSAKATQVRH KAYRIPRRRF TASRDPNTQV
WTWGKSREKP SGTPAKQEQA PSYELPKQPA QDDMDSAVES SPLGYVSDSE VPSSRVQSYN
VPSSPMEELD LAMSVPNLEL PRPSSAQAFA AGDSQPLLHR RITPQEILSR STSAHTSPDK
PPSSSAVSPA SNLSSNEATL SYVWVGVSVV FACVTFLPDF CVFLMAHLLD LVMDTFEVLS
YTVWFLLWIW QNITGQTILG QIVYEAYHLV QKEWEHVIRE DHEEASEHMV RFLGIPLFRQ
PRGLSTWQVL RGLIEIICIQ TVTREQYQKE GAGLVRLQNW RRHETSTSSQ KEEGQSESKD
PKAGVASESY GSNEEESDDD DDDDLVVTDQ TVDVLELSRN TKPQTEEQVP SKPHRNYPYE
MWHETNGAMV RNIKWASQLS MSAYGLRVLI VDLPPIFTPS GQELPKQTFA HLTRLQADDV
LHADIQNLDM EATYLPTFYI VRDMRRKVVC VAVRGTQSFA DIVVDLDMKT EDVTSSLAEW
RDTEVDEKTE RFAYHAGIWR AAKTLVEPGS VLFKKVCDAL NENEDFGLVF VGHSLGAAIA
SAAVIQLSEY HIEDTGPNAD PRKGVWRTSG QTGYPAGRLI RAITFAHPST LSHTLSKRVS
YGRVPLVINV TYATDLIPRF GHGQVREIRR VLGALTRVRR RRKMVSTTIS SHPTYANEDD
EIRLHVIRRF WDWWSIQRNK SPDQVMLARK KLLEKQFWRL RLEVESDLYT NARRRFEEAA
AEKMHETQTP MSPWVPEDHY KAMPLHTMSG RRQRLDYATV QSESRQGGVL VPGGRSLWLN
DGEFYDITNP LAFFSLPDLH FAMFTDHFPA AYEEAVLALD STST
//
