ID A0A317XWQ5_9BASI Unreviewed; 1790 AA.
AC A0A317XWQ5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=triacylglycerol lipase {ECO:0000256|ARBA:ARBA00013279};
DE EC=3.1.1.3 {ECO:0000256|ARBA:ARBA00013279};
DE AltName: Full=Autophagy-related protein 15 {ECO:0000256|ARBA:ARBA00029828};
GN ORFNames=BCV70DRAFT_229187 {ECO:0000313|EMBL:PWZ02746.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWZ02746.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWZ02746.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWZ02746.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001024};
CC -!- SUBUNIT: Binds to both phosphatidylinositol (PI) and
CC phosphatidylinositol 3,5-bisphosphate (PIP2).
CC {ECO:0000256|ARBA:ARBA00011137}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000256|ARBA:ARBA00004343}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004343}. Prevacuolar compartment membrane
CC {ECO:0000256|ARBA:ARBA00004270}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004270}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701}.
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DR EMBL; KZ819188; PWZ02746.1; -; Genomic_DNA.
DR STRING; 1882483.A0A317XWQ5; -.
DR InParanoid; A0A317XWQ5; -.
DR Proteomes; UP000246740; Unassembled WGS sequence.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:UniProt.
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 InterPro; IPR009348; NPR2-like.
DR PANTHER; PTHR47175; LIPASE ATG15-RELATED; 1.
DR PANTHER; PTHR47175:SF2; LIPASE ATG15-RELATED; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR Pfam; PF06218; NPR2; 4.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
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:UP000246740};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1559..1588
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 38..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1705..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1790 AA; 191218 MW; B5458C3A367C8600 CRC64;
MSMPTLDEQF LPRLVSIFYA VFHPTEGPKV IYQVPEGSIT EEEKDKPRKH DSKTSAPDYS
TANATQYGGM LGGEPLFDFS ALSEYLIPKA PLCGRLVTSI ARGSVKTHTR KSRDERAATP
SAAMARSRSA RSGGRSAGSS RTSSVRPRAE EDTPAQDGKD TQAVLKTYKI LGFPTMIEDA
ARYRRNNFIF NLCFVFDGQA DVRAYEPVVR KCGRVLRGLE ETQSFLSSPR SLPRMYAIIE
QLFEDLNSYC ESFVALPEAP HTSYLKSSSK PNSPEHRSTT SPLIGPDDFV SLGASFASLR
DEHHKKLIND HLRLMQAQAQ HAGPRHLPSS TSSRNQHHHH NSSGGSGDSN SKIAVGGSGN
RSRATSETGH GETSLGIGAR PSLSPLSTAT SKPGSGNEPS MTRSNSATGT SGPAADSPHS
PRQDNGPFSP DARRPSLGRS TTVAALTETA PLGASPSAES RDLAMGILSS RKQSELTREL
SAAESLGNVL SNRDSGSFDG INTPAGTRRS SRGSGASGHG VGNETSASAL EQLTESIVSL
RTIDAALSNS VNALRSETID STHRAALAEK REPPHGLGRT VRDAINLKLF PVYPNPPPVN
DWDVPVALLD LSSRVDGNWD LTMRRILPFI DGVSHVKRIA QLADADLGLT RACLEHLIYY
GCIIMVDTFQ YLNMYTVRPA IAKMADDEAM GRECAAYVTR PGFAMPSYPE LLRLYSLLRA
GKTLHDWIED NDVDAKGIDV RRFVSFGVIQ GFLRRVHRYP VYLGGPASED LESSRFDASA
NTTVRNSPVS KSNEPYSQMV GSAANRREQS GSREPRDRRP RELSGMSGAY SAFQRIGRDG
SVDNPGVGNR TPSRRAASEA GRPMGSVGGH GTPGTGVGGT GSQMTDSTHL GGGGSGAGGS
AFGTSPTKRG NRHRPRATYR LPTATAMDVA SVAFEVSASD SRWSSGHQQA PTPGFGIARS
PRKRSSMAGL SGVAGATGSG FLSTASGPGA AGASGISQRS NPVVVPPGLI DMLDGTHHDD
ELCVMFSVSW SELEKMLIQI GTAKDGLGMR LIGAGADSEE ETSTAQHRSA DWRRWHSSVQ
AGQSQGGGAA GASSGWNKGR MSGFSGVGAS AGVGQGGGTI GRSGLSGVAS SSNRTGGTQT
DSGILLNNPG ASGFGIGYGW GVDPDESGVA GWSSFSGLDR QAIESGDLGR VRILLQSALA
RYSSSAERVH HTSLSPGGRA TSAMKLIVGS DPALRRGALS MEPALSTKLL ATSYLLLIAL
LATSVHGSVI PQPPIDPWSQ VAFEQPLGLS SYLQTWFSHL LRPLMGHSDS SASDPPQITT
DSASTLAFVG YKAFGLREAY HQGMGDKSHV RAKATYDYRI SADDVRASSS DPNYIPRIRT
VRQRVTRARN PQKYLEVRGT SYESAMCAAS TELDWDDVDV EAPDVTDRTT VLAFAKMASS
AYQNDTSDWD GIGGFNPTNS FGWEGDGIRG HIFTTHDNDT IVVALKGTSN AFLPGGGETA
RRDKTNDNLL FSCCCARVSW SWSTVCDCYQ GHGDSCGQTC LERALVEKSL YYPALTNLFN
NISYTYPDSQ IWITGHSLGG ALSSLLGMTF GIPTVTFQAP GERLAALRLH LPLPPAKHPD
ESPISALPIV HVYNNADPIA TGQCNGAGSF CSNFGYAMES RCHAGKSIVY DTVGKLGWGQ
TVNAHRINSL IDDVLSEDWS DKVRKKKAKS KAVDGTSASD RIGTRGWRWP WNRGNGSDAD
DDSDQDTDED DKLPVPRLRS EDKCRDCTDW HFSDDDGDGG DKDLLKFQGK
//
