ID G0RFT3_HYPJQ Unreviewed; 1068 AA.
AC G0RFT3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=TRIREDRAFT_76771 {ECO:0000313|EMBL:EGR49965.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR49965.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR49965.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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}.
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DR EMBL; GL985061; EGR49965.1; -; Genomic_DNA.
DR RefSeq; XP_006964298.1; XM_006964236.1.
DR AlphaFoldDB; G0RFT3; -.
DR EnsemblFungi; EGR49965; EGR49965; TRIREDRAFT_76771.
DR GeneID; 18488665; -.
DR KEGG; tre:TRIREDRAFT_76771; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_76771; -.
DR eggNOG; KOG2088; Eukaryota.
DR HOGENOM; CLU_001871_0_0_1; -.
DR OrthoDB; 373802at2759; -.
DR Proteomes; UP000008984; 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:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G02710)-RELATED; 1.
DR Pfam; PF01764; Lipase_3; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 745..836
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT DOMAIN 863..911
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 238..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 116199 MW; D44D569FE89F2B56 CRC64;
MPTDDAVVAS KQAQQKQGPT LLPSPVAQAV SLAARSTSLA IRIGSVVSNA SLDAARLTTL
GGLGLARGLI EGVMSRAAKD TIEQSRTDLA VQDAETVLER SLESLHYAVT QAVFWTSVSF
RLTGTTISTA SAGSQLLLSS FDQLFGSTDS SRAVASIVTL IRREFENPAT GLQGERVGVI
DLTLALSTLA YLQRACRKTV EEERRRQSCE EVIWDVVVLE DGDRVDIDEK VLSEIRGGYG
PGDKDEIPSS PIGSSWTGTE DDEAVVSRLK SQIMASLTPG TTVSVSNSVS SVQTITVDVH
GPRLLSLPTP PGAEIVETKT LLASGSQLPY TSSNQRDQTS TTSYRVVYKL HRQKKETSSF
PGDEEIKDDA LEIMSDNQSC SSEETLAPGT PTITLPEYQS PPVSPNLLPS STFALHLRPS
TSTETKRRHK SHSHDFSKPT QSSSRKNNSD SAKAVASRTS TAVSKEPIYL EDLEALANQK
RQRTPVHSAK SQDKSHRQAH SGSRTEGGAS SRSSDKKTGL RHVLRGSGPS ISSIWTKESG
PMDYVTAKDK SKLHLKSSHR DSKDGRPGSP NSDLAIRSPP EHHNIYLVPP SVGHRRNRSY
ATSIYSVGTN DSQSSLMLSS YYQKSAYNTA DALRALREEG FVDGTFPEGH LLPNITRYMR
FSSACYGSNF LKLTGISNEI PKVGAWDGTH HDIQHFLHHT ESQADNILLA SFVDPNGGSD
SSGATGSGVP LVHYISLDHA AKAVVLACRG TLGFEDVLAD LTCDYDRLVW RGKGYRVHKG
IHASARRLLY GGDGRVLMTL KEALREFPDY GLVLCGHSLG AGVTSLLGIM LSEPNPLGPG
FVTSAEPYTL RPPPHEALVN VRLSDIRPPS GRRIHVYAYG PPAVMSSSLR KITRGLITTV
VHGNDLVPHL SLGLLHDFQG VALAFKQDEN NTKSEIRQQI WNALQDNVSE RWYSYRSASK
VASSGGVSDE ERWMLPALEN LRAAMKGKKL LPPGEVFTIE TQRVLRRDAF LLLDEEHIGR
PAQRIVLKYI KDVEGRFGEV RFGTSMLTDH SPAKYEDALN KLRVGVST
//
