ID A0A397UZG7_9GLOM Unreviewed; 746 AA.
AC A0A397UZG7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=C2G38_2191948 {ECO:0000313|EMBL:RIB15620.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB15620.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB15620.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB15620.1,
RC ECO:0000313|Proteomes:UP000266673};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) 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:RIB15620.1}.
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DR EMBL; QKWP01000731; RIB15620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397UZG7; -.
DR Proteomes; UP000266673; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000266673};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 479..610
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 26..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 85188 MW; A18052865C4105CF CRC64;
MPKFVIDTMV PLREENSQQF DYITPTVKSS PESQSSNIPT QSYNDKKEDL LSINHANLGP
FSPRTQSMIN ELEKHVDELA NPDNQIFILD SPRETKSGVT LDSKSILHIQ KDSEDDIQQD
FGQMDQNSLV NNTGKFQSYN NKLYYNKDEE SNNKSSKKIS LSLDKISINL KNAMLDQEIG
AQVEDDQVPN SDSPLSSAIL PDNIYVHIKL VNFDLDSKIK RSIRLMIGLI TYHTKSSTSL
EEQLKKSFLF PFNYHSLIFD TMKLVIYEHG SFLNKKRKCG RVIVPLSALK QAIIDQKEFE
GIFPIEANGS LHEIGAVQIN IKFKFSNGSP ITSPIQSTLI NISREYIQCD NIETHPDAIS
LGILDTVLNQ ETRDAIKEIT ALYHTPNSPI TGNLCCDVDV MKKALRYIQF SMASYGSFLF
HWFGYGPINA FGITSDKKIV RKFFNLDKSD IICWEYGHNA VSVPSYMVIR DPETNSIIIS
IRGTMSITDL ITDALAHYES WNDGFVHRGA LRSAQYLINH SLKEIRDAVI KYNVNSIKVM
GHSLGASISS LTTLLLREHC KDMLDRGINI HAWNFATFPC CSLDIASKAD TMNCINNFVN
ENDVIPRLSY GNLMDFKELV KFAASELKND EYKELRSKHK LSKIFSSIDE YRKTLKLNSS
SQKLYIPGKI YYIYKRLGHS HVETSYFPSY TKEVVCEESR PDLFTDICLR KNWLFHHFPD
RYDKRLKGAI KFLKKESGER TPESVW
//