ID W6Q0J5_PENRF Unreviewed; 583 AA.
AC W6Q0J5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acyl transferase/acyl hydrolase/lysophospholipase {ECO:0000313|EMBL:CDM30063.1};
GN ORFNames=PROQFM164_S02g000212 {ECO:0000313|EMBL:CDM30063.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM30063.1};
RN [1] {ECO:0000313|EMBL:CDM30063.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM30063.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- FUNCTION: Probable lipid hydrolase. {ECO:0000256|ARBA:ARBA00002682}.
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DR EMBL; HG792016; CDM30063.1; -; Genomic_DNA.
DR AlphaFoldDB; W6Q0J5; -.
DR STRING; 1365484.W6Q0J5; -.
DR OMA; SIVPWPH; -.
DR OrthoDB; 154387at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; 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 CDD; cd07229; Pat_TGL3_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:SF44; TRIACYLGLYCEROL LIPASE 3; 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, ECO:0000313|EMBL:CDM30063.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Transferase {ECO:0000313|EMBL:CDM30063.1}.
FT DOMAIN 185..379
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 555..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 65565 MW; 3CD9817822BDB702 CRC64;
MGSWWLGLWN IVGAVWNMLL DVAQFWRYKL SSWWHSKSPR DRLFYTLANA KSYEDWEEAA
FELDELQSKD LWRQNPVSRH YDYRLILGRL EALMSARESE DILTLVNLLR SGLVRNLGNI
TSTKLFTHAY AGTKLLIDDY ITQVALSIQY VTSVPGAPMH PSGFSSQAKL ELLHDTRQAF
GRTTLLLQGG SAFGLCHLGV VKALHLQGLL PRIITGTASG AMIAALVGIH SEDELLPLLD
GEGIDLSAFD TRKMINGGVE ESSDSGWVGT FYRRLRRLMK KGYLFDVGVL EECVRANVGD
LTFEEAYARS KRILNITVVT TGKNGTPNLL NYLTAPNVLI WSAAVASNAS SSSGLYSPVT
IYCKDETGTI VPWPHTQDAV FRPWRHVHYN EGESPLSRIS ELFNVNHFVV SQARPYLVPF
LRSELNLLDR RQTGWSNLSR STMRLIMVEL RHRLRQLDYL GVLPAPVSRI LIDETIPGPN
LTLVPDLSFW DLRKLFQSPT KAGIADWALK GERGVWPAIS ALKVREAIEI ELDRGYQLVR
RRRPSDPSVS VAIPKQVNAM NEGVPRRRRG GSENDEGILA DRE
//
