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Database: UniProt
Entry: A0A1X2GQK2_9FUNG
LinkDB: A0A1X2GQK2_9FUNG
Original site: A0A1X2GQK2_9FUNG 
ID   A0A1X2GQK2_9FUNG        Unreviewed;       906 AA.
AC   A0A1X2GQK2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE            EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN   ORFNames=DM01DRAFT_1211570 {ECO:0000313|EMBL:ORX59026.1};
OS   Hesseltinella vesiculosa.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Hesseltinella.
OX   NCBI_TaxID=101127 {ECO:0000313|EMBL:ORX59026.1, ECO:0000313|Proteomes:UP000242146};
RN   [1] {ECO:0000313|EMBL:ORX59026.1, ECO:0000313|Proteomes:UP000242146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3301 {ECO:0000313|EMBL:ORX59026.1,
RC   ECO:0000313|Proteomes:UP000242146};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORX59026.1}.
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DR   EMBL; MCGT01000006; ORX59026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2GQK2; -.
DR   OrthoDB; 1341793at2759; -.
DR   Proteomes; UP000242146; 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:UP000242146};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          581..722
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
FT   REGION          177..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..286
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   906 AA;  101799 MW;  44359DB29A906D89 CRC64;
     MRVRLGSQQY YSSRSHDPHG NWNEGFLFTI SYHNQLFDTI ELDLYDRKKG WRSKTKHIGK
     AKLKIAKLKH HEDVFLTFVP MYEYHTKRYL PAHIQLPHNF LKANMPNFPS LPHPMSKKNG
     TANPVQEHYL HYEQHPSHRK HSMTPFIGSI QIRIRYQYQH PDDSLDHSTK PVYLPYNASK
     EVDPSSPSRP VSLHPHSSQA TSLSSHTMLT MATTQATDDD DLSSSDNDSM LDNASVCCSL
     YSTASALDSQ PPRSTPPTKQ VQADEPPTPV PDVVVSPTSP THPPDLEPEV KPSKPDRAWP
     FSNTRLRFAA AQSLSASSSA STHRIINRAS STSMSSRTSS VRSRASDCSS HSAMSPSAGF
     GFSRCDDDRR HALLSRHGLG NNHHDGASLF SDRDSAISDS ASIRSNNFGD KNFAFRWINE
     NFEEVALSHP SLDRMIGMVV SPQTRILVRA VVKMMNAFGQ GFKITSVQLF SSLSMLQKFY
     NEIPRSPPPA SKVTDLRFLD EAHYFLGHAI IAYGWRGISY LGDYAKYLKD VMKTRSNKLA
     IVRFLKMPPE DLLGYEYGLR KGAVFQPSYF VSVDRGHEAI VLGIRGTWSL YDVITDLVCD
     YKPWKGGLVH SGMLASAQWF FTRIVPQIFH YIHQQCKQDK PPHIKSFIIT GHSLGAGTAA
     ILTMMIADHM DELLQISGNP NFRLHCYSYA PVASVSLDIS EKYKDYVDSF VCHDDLVARL
     SYGTASCTKE LVMDALIAAD GLGGITKVNH DQETRRQCFD IISTRRQEIF QANEPRYPLL
     YVPGRVFQFR RRPIPARPPP QRRASVHEPA HPLSSHGQAH RKPSDASVDF TLHESSALLS
     EEMLITKTCL EDHMLVTYLK AFQTARENCM RDSHLEKSSA PSSSPTPDQP PPSILLHDPD
     GQLSSI
//
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