ID S8C395_DACHA Unreviewed; 889 AA.
AC S8C395;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=PNPLA domain-containing protein {ECO:0000259|PROSITE:PS51635};
GN ORFNames=H072_3978 {ECO:0000313|EMBL:EPS42157.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS42157.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS42157.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS42157.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable lipid hydrolase. {ECO:0000256|ARBA:ARBA00002682}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPS42157.1}.
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DR EMBL; AQGS01000129; EPS42157.1; -; Genomic_DNA.
DR RefSeq; XP_011109938.1; XM_011111636.1.
DR AlphaFoldDB; S8C395; -.
DR STRING; 1284197.S8C395; -.
DR eggNOG; KOG2214; Eukaryota.
DR HOGENOM; CLU_324653_0_0_1; -.
DR OMA; NCCAIEL; -.
DR OrthoDB; 154387at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:UniProt.
DR CDD; cd07230; Pat_TGL4-5_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000015100}.
FT DOMAIN 215..412
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 586..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 889 AA; 97014 MW; 7154E7C0D5840497 CRC64;
MSFLREQPLI HLPGAGACGT TQKHQLYAAG KGPSPASSTS PPKSVFNPLL NFVKHPGDAI
RNFAIDEAGK QRLVLQARLK NAKTHAEWIE AATLLDELDG NNRWKSEPLS SEYDANQVKA
RLDQLEEARI SGDIGRILFL IRTTLTRHLG GMGTVELYRH SYTGTKYLIE SYIETALATL
DALIKPPPSA DPQLSPKKIL ESLVATRQSF GRTALLLSGG ATFGMTHIGV LKALWEADLL
PRIISGASAG AIVASVLCVR TDNEIPNTLE HFPYGELDVF EHAAEPEGVM ARVGRMLKMG
AWMDIANLTR VMRNMLGDIT FQEAYNRTRR ILNICVSPAS VYELPQLLNY LTAPNVLIWS
AVAASCSLPL LFTPASLLAK NPKTGLAEPW NASPQKWIDG SVDNDLPMTR LAEMFNVNHF
IVSQVNPHVV PFLEKEPIQP LQHEGSSESQ SSYEAWKSTF VSLAMGEALH RINVLTEMGI
FTTSLTKAKS ILSQKYAGDI TIFPEVPLAD LQKLIKNPTP EFMIEASLRG EKATWPRLSR
IRNCCAIELA LDRCIHQLRT QVVFSGSQVD LRLNTLDSTK VNEKGEAYVS QSRASNISRK
RPVTGDPNEL SMFVPPPGAP LAPLYDPYPQ NRLSYPPSTT RNRSHSTGPP QLPQFSPAIT
RTLTAGKGYF DNGAAKAPGS PNSSRSSYSM NSTKQVAIRS PKQSSTTSGS NRNSSHIGSP
SATKIAGEET IGVSLKRVGS RYRLVRQTPS SELDPADAED ESAAIAGSSE DEDPFQLPES
LDDHSGDDGP VIIPDQAPSS GSSSFTFNSF KDEISNGDQP LSLQRRPFTS RSVTALPLYS
TYLPNDEAYA TRINSNNTSL PASSVTSPIA TTQRSFSRKS EDQIQDEES
//
