PLPL_CHAGB
ID PLPL_CHAGB Reviewed; 854 AA.
AC Q2HA54;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Patatin-like phospholipase domain-containing protein CHGG_02900;
DE EC=3.1.1.-;
GN ORFNames=CHGG_02900;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- FUNCTION: Probable lipid hydrolase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PLPL family. {ECO:0000305}.
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DR EMBL; CH408030; EAQ90965.1; -; Genomic_DNA.
DR RefSeq; XP_001229416.1; XM_001229415.1.
DR AlphaFoldDB; Q2HA54; -.
DR STRING; 38033.XP_001229416.1; -.
DR EnsemblFungi; EAQ90965; EAQ90965; CHGG_02900.
DR GeneID; 4389131; -.
DR eggNOG; KOG2214; Eukaryota.
DR HOGENOM; CLU_009031_2_0_1; -.
DR InParanoid; Q2HA54; -.
DR OMA; DMNKWLR; -.
DR OrthoDB; 425613at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:UniProt.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR021771; Triacylglycerol_lipase_N.
DR Pfam; PF11815; DUF3336; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..854
FT /note="Patatin-like phospholipase domain-containing protein
FT CHGG_02900"
FT /id="PRO_0000295555"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 387..578
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 418..422
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 70..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 420
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 565
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 854 AA; 94412 MW; 76D312484F5C204A CRC64;
MAGPGYDRVD SKDDEPPNIQ IPSRTYGFPP EAFDWSRLPD FDTNFLPPEH VEAFIQALSA
PDPIPPTPDG GATGSSSYRL NSPAWHRGST TSFDLDLARR PESSGVGFHD EDRTARDSPA
GAATAAAAGV ATPGPPLSRR ASSNSLFISA RNDWAPISQR RVARAKTAPQ SSSRNDKKKK
RARSKDETRE GYLYPLLKWP LLGVVTCWLV GLSVVHVLAR LYITVYERYW AWRGERGRLR
RAMRATARYS DWVAAARRMD DFLGNDSWKV DDAFAYYDNK TVRRVLAEMR RSRRRAEEAG
GRDTEQGREA IEDLKVLIEA CVKNNFAGIE NPRLYSQTYY GTKNLVQNFI DEVERSLKFL
VETERLSKEE KRVMFKGICA NYGRTALCLS GGATFAYYHF GVVKALLEED YLPDIITGTS
GGALVAALVA TRTNEELKEL LIPALACRIT ACREPISVWF RRWWATGARF DSVDWARQCA
WWTRGSLTFR EAYERTGRIL NVSCVPADQH SPTILCNYLT SPDCVIWSAV LASAAVPGIL
NPVVLLMKTR SGQLLPYSFG HKWKDGSLRT DIPIKALNLQ FNVNFTIVSQ VNPHINLFFF
SSRGSVGQPV THRRGRGWRG GYLGTVLVQF TKLDLTKWLR VLRSLELLPR PLGQDWSLLW
LQDFGGTVTV WPRCLLSDFA RILSDPDPAR LARMIHEGQQ SAFPKLRFVA NRLRVERLVE
RGRRENRRGG GLGDGGVGSS GGAGGGAGGG QAEAVAGQAA GPGTGQRRPS FESILSEDDL
RSLLKKRRVE RGGIGSGETE SEDETSDLDA DFYEGITYDG GDDDAGLEFG AAGMRQPGVA
TPAGLGGVER GDLS