GENTAUR Molecular Products.

 A0A1B7NF25_9HOMO        Unreviewed;       818 AA.
 A0A1B7NF25;
 02-NOV-2016, integrated into UniProtKB/TrEMBL.
 02-NOV-2016, sequence version 1.
 23-MAY-2018, entry version 11.
 RecName: Full=Patatin-like phospholipase domain-containing protein {ECO:0000256|RuleBase:RU362055};
          EC=3.1.1.- {ECO:0000256|RuleBase:RU362055};
 ORFNames=K503DRAFT_731419 {ECO:0000313|EMBL:OAX43465.1};
 Rhizopogon vinicolor AM-OR11-026.
 Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
 Agaricomycetes; Agaricomycetidae; Boletales; Suillineae;
 Rhizopogonaceae; Rhizopogon.
 NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX43465.1, ECO:0000313|Proteomes:UP000092154};
 [1] {ECO:0000313|EMBL:OAX43465.1, ECO:0000313|Proteomes:UP000092154}
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX43465.1,
 ECO:0000313|Proteomes:UP000092154};
 DOE Joint Genome Institute;
 Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J.,
 Sharma A., Barry K., Grigoriev I.V., Spatafora J.W.;
 "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
 vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales)
 reveals a divergence of the mating type B locus.";
 Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
 -!- FUNCTION: Lipid hydrolase. {ECO:0000256|RuleBase:RU362055}.
 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362055};
     Single-pass membrane protein {ECO:0000256|RuleBase:RU362055}.
 -!- SIMILARITY: Belongs to the PLPL family.
     {ECO:0000256|RuleBase:RU362055}.
 -!- CAUTION: Lacks conserved residue(s) required for the propagation
     of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01161}.
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 EMBL; KV448137; OAX43465.1; -; Genomic_DNA.
 EnsemblFungi; OAX43465; OAX43465; K503DRAFT_731419.
 Proteomes; UP000092154; Unassembled WGS sequence.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
 GO; GO:0004806; F:triglyceride lipase activity; IEA:EnsemblFungi.
 GO; GO:1990748; P:cellular detoxification; IEA:EnsemblFungi.
 GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
 GO; GO:0006642; P:triglyceride mobilization; IEA:EnsemblFungi.
 InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
 InterPro; IPR002641; PNPLA_dom.
 InterPro; IPR021771; Triacylglycerol_lipase.
 Pfam; PF11815; DUF3336; 1.
 Pfam; PF01734; Patatin; 1.
 SUPFAM; SSF52151; SSF52151; 1.
 PROSITE; PS51635; PNPLA; 1.
 3: Inferred from homology;
 Complete proteome {ECO:0000313|Proteomes:UP000092154};
 Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01161,
 ECO:0000256|RuleBase:RU362055};
 Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU01161,
 ECO:0000256|RuleBase:RU362055};
 Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU01161,
 ECO:0000256|RuleBase:RU362055};
 Membrane {ECO:0000256|RuleBase:RU362055};
 Reference proteome {ECO:0000313|Proteomes:UP000092154};
 Transmembrane {ECO:0000256|RuleBase:RU362055};
 Transmembrane helix {ECO:0000256|RuleBase:RU362055}.
 TRANSMEM     85    112       Helical. {ECO:0000256|RuleBase:RU362055}.
 DOMAIN      267    459       PNPLA. {ECO:0000259|PROSITE:PS51635}.
 MOTIF       298    302       GXSXG. {ECO:0000256|PROSITE-
                              ProRule:PRU01161}.
 ACT_SITE    300    300       Nucleophile. {ECO:0000256|PROSITE-
                              ProRule:PRU01161}.
 ACT_SITE    446    446       Proton acceptor. {ECO:0000256|PROSITE-
                              ProRule:PRU01161}.
 SEQUENCE   818 AA;  91606 MW;  78E5FE3BF4B274E5 CRC64;
 MKAPAGVFDV DYVDESHINA FVNAIKSDNL DGLSEVSPNT APSSPAIPQS PRVRKVSALS
 DFAPINLKVK RKRKGDKATN RRQEWLFLLL RWPLLFLIFA IIAAQFSLYI VIRQLVNTKE
 WLVAWRGRKG LLRKRLRGAN TYQEWKEAAT TLDEYLGFDD WKKIDEDAFY DWKLVRKVNR
 SLKTLREKKD VRGVLGILEM CIRTNFVGVE SSRLYSESFL GTKDLIESYH NELESALQFI
 RESSELTIEE KKRFFKNANT NLGTSALCLS GGASFGYYHF GVVKAFLDAG LLPRVIAGTS
 AGGLIAAMVC THTDVELKAL LVPELARKLT ACEDQFPTWI KRFWTTGARF DSVAWARKCV
 FFTKGSTTFR EAYMQTGRIL NISVVPSDRH APTMLLNYMT APDTIIWSAL LASTAVPGIL
 NPVVLMQKLS DGRVVPWNWG ISKFKDGSLR VDIPLQALKL DFNVTHPVVS QVNPHVHLFF
 FAPRGSAGKP VAHRKGKGWR GNFLLSAAEQ WLKLELVKNF KVIRDLELLP QLLGQDWSSV
 FVQRFDGAVT IWPRTRILDW FHILSDPDPA ELERMMKVGQ IVTWPKLHMI ENRFRIEKQI
 LLGRQAARTT VERARSRANP GNTRNIVIDD QVVPEPVTGT QHPTTVRFES PIPMDSDTER
 AFEGNVAARY FRRIRSTAST PRESGVNTPY ENGYNDTTDP LRSPVLRRKW ASDLLDAVGG
 SSSASPRPTT PEASVDEQRS PPSSTFSTRV GPGSLATLSI PSSGSRRTSR SNGKGVSVGA
 SEMVWSSESS SEDDSDHLDP NTDFNQEVIS DADGVVSD

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