ID Q6FTH9_CANGA Unreviewed; 883 AA.
AC Q6FTH9;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Candida glabrata strain CBS138 chromosome G complete sequence {ECO:0000313|EMBL:CAG59392.1};
GN OrderedLocusNames=CAGL0G02365g {ECO:0000313|CGD:CAL0130763,
GN ECO:0000313|EMBL:CAG59392.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG59392.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG59392.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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DR EMBL; CR380953; CAG59392.1; -; Genomic_DNA.
DR RefSeq; XP_446465.1; XM_446465.1.
DR AlphaFoldDB; Q6FTH9; -.
DR STRING; 284593.Q6FTH9; -.
DR EnsemblFungi; CAGL0G02365g-T; CAGL0G02365g-T-p1; CAGL0G02365g.
DR GeneID; 2888267; -.
DR KEGG; cgr:CAGL0G02365g; -.
DR CGD; CAL0130763; CAGL0G02365g.
DR VEuPathDB; FungiDB:CAGL0G02365g; -.
DR eggNOG; KOG2214; Eukaryota.
DR HOGENOM; CLU_009031_4_0_1; -.
DR InParanoid; Q6FTH9; -.
DR Proteomes; UP000002428; Chromosome G.
DR GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:EnsemblFungi.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0004771; F:sterol esterase activity; IEA:EnsemblFungi.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:EnsemblFungi.
DR GO; GO:0007114; P:cell budding; IEA:EnsemblFungi.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:EnsemblFungi.
DR GO; GO:0019433; P:triglyceride catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006642; P:triglyceride mobilization; IEA:EnsemblFungi.
DR CDD; cd07230; Pat_TGL4-5_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR021771; Triacylglycerol_lipase_N.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF10; TRIACYLGLYCEROL LIPASE 4-RELATED; 1.
DR Pfam; PF11815; DUF3336; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT DOMAIN 314..515
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 93..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 100222 MW; 7AA86607254EDCCE CRC64;
MAVPVKTLKR YISERQSSFD DLARLIEEDH EFDQIDGGVQ QAITQPLIER YYQYLLGRNS
QTEANTTAEE EPSEPLEPIL DYAFDRATKE KLKTTSAESL VSEDTPTDPL KSENIPQLYR
DDDEEPEELH ENSVSESNPS NEQSEISYLE SLKQYYDSTK RTLYNTFIGN YDKNVLIDRY
LRKKKLAQSY EEWKYACLKL DSLTNTNEWK EEQESTLYDY TLIKTVTNKM RELRLQNDYL
GLLYVIRTNW VRNLGNMGNV NLYRHSHVGT KLLIDHYITE SKLCLEALLQ SDLDDNYLLG
ILQQTRRNIG RTALVLSGGG SFGLFHIGVL ATLFELDLLP RVISGSSAGA IVASILCVRH
KEEIPELLQK VASKDFNIFN DDKQKTESEN LLIKISRFFK NGTWFDNKQL ANTVIEFLGD
MTFREAYNRT GKILNITVSP ATMFEQPRLL NNLTAPNVLI WSAVCASCSL PGIFPSSPLY
EKDPITSEVR EWSGSASVRF VDGSVDNDLP ISRLSEMFNI DHIIACQVNI HVFPFLKLSL
SCVGGEIEDE FSARLKQNLS HIYKFVSNEM IHLFELGSEL GIAKNLLLKL RSVLSQQYSG
DITILPDMMT LYRINELLCN PTKEFILREI TNGAQATWPK ISIIQNHCGQ EFALDKAISF
IKGRMIVSSS TKSPLQFFDA PIGLIQNNIQ KETNGYSHVL DDNLLESESA KSLSLLSEKN
TTHQLHSTEN LSLYSTPMSA RHRRRTSDVS IRAIAKNKSK SFSVTSPSSM ILKGNRNYSN
NSQINRVDLA EKESNECHRS GDYKFSRNKN VGFQINVNKV VETPRSTQTS SQSTSVGGSP
RMERQEYFRK SGRRILNSNR PAKILRSRSS SASFGESSVS LSR
//
