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Patatin-like phospholipase domain-containing protein (EC 3.1.1.-)

 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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