ID   A0A135L8D2_PENPA        Unreviewed;      1129 AA.
AC   A0A135L8D2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Acyl transferase/acyl hydrolase/lysophospholipase {ECO:0000313|EMBL:KXG45220.1};
GN   ORFNames=PGRI_041330 {ECO:0000313|EMBL:KXG45220.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG45220.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG45220.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG45220.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
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:KXG45220.1}.
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DR   EMBL; LHQR01000072; KXG45220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135L8D2; -.
DR   STRING; 5078.A0A135L8D2; -.
DR   OMA; MAYQANG; -.
DR   OrthoDB; 1079044at2759; -.
DR   Proteomes; UP000070168; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07216; Pat17_PNPLA8_PNPLA9_like3; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002182; NB-ARC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR24185; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR   PANTHER; PTHR24185:SF1; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   Pfam; PF13374; TPR_10; 1.
DR   Pfam; PF13424; TPR_12; 3.
DR   SMART; SM00028; TPR; 8.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48452; TPR-like; 3.
DR   PROSITE; PS51635; PNPLA; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KXG45220.1};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW   Transferase {ECO:0000313|EMBL:KXG45220.1}.
FT   DOMAIN          17..233
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
SQ   SEQUENCE   1129 AA;  125110 MW;  A313EEE96340C7E9 CRC64;
     MDPATASADS CQPLRILSLD GGGIRGISSL LILERIMERI CDAEDLDHVP RPCDQFDLIG
     GTSTGGIIAI MLGKLGMTVD ECIRAYRQVA EQAFTPKRTS ILPASPTGAF SAKALENAMK
     QIVREYCTNV ECVTRRRQGH ATVTTCPHSN MVFRDDTCTK TVVLAITKDN VDAPPTLFKT
     YDRSAAFESS TLWQVARATS AATTFFKSIK VGRDEIEFID AGFGYNNPCN ILIQEAQREF
     PDRGKMRILS IGTGLGDVVT IQNKRLSIIT ALKRMASSSK KVAADVDHRY GGNGEYYRFN
     VDQGLQDITL SDWEKASKIS AHTRNYLAEN ERVIKQLIGE ITCHSQVSGK PFFFVPLRQN
     GNFVGRGKEL DELKQKVLAQ KDNGRLAVFG LGGIGKTQIA LQVSYWARQA MPAHSIFWIP
     ALSKASFEQA CTQIVAKLGI SKISDNEDAM ESVQRHLSLQ STGPWLLIVD NADDMDLLFG
     SSDSPGGMSQ YFPESEMGVT LLTTRSREIA VSFAGNQVIT IQNMNLQETT GLLENSLIKR
     DTRQDRGETV QLLEELNYLP LAITQAAAYM NTADISISKY LSLLRGKKSD AVRLLGRQFQ
     DSTRYRGSQN AVATTWLVSF QQIHRTDEAA ANILSFISCI EPKAIPLSLL PDVGSDEELV
     HAIGTLCGYA FLAERDDASY DMHSLVHLAT QVWVREQGFA KQTIEEAVHH LVGTFPSHDY
     INRRLWQSFL PHSLRTLQES EGRDTKERSE LYIRVGRCLE ADGRIREAVN CYEEKFRWDK
     SQYSEEHPDR LASQYELAIV YQADGQVSEA VKLLEHVVAV QERTLAEEHL SRLVSQNGLA
     RAYRADGQIS EAVKLLEYVV TVLEITLAKE NPYRLASQHE LAIVYQADGQ VGKAVKLLEH
     VVAHGLAIAY QANGQVSEAV KLLEYVVAVR EKTLAEEHPS RLASQHGLAS AYQADGQVGK
     AVKLLKHVVA VQDTALAEEH PNQLASQHGL AIAYQADGQV SEAVKLLEHV VALREKTLAE
     EHPSRLASQH GLAIAYQADG QVSEAVKLLE HVVAVREKTL AEKHPDRLES QYGLAIAYQA
     DGQVSEAVKL LEHVVAVREK TLAKKHPDRL ASQHALAMVK HEYENERRH
//