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Database: UniProt
Entry: Q8FQ79_COREF
LinkDB: Q8FQ79_COREF
Original site: Q8FQ79_COREF 
ID   Q8FQ79_COREF            Unreviewed;       326 AA.
AC   Q8FQ79;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=PNPLA domain-containing protein {ECO:0000259|PROSITE:PS51635};
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18064.1, ECO:0000313|Proteomes:UP000001409};
RN   [1] {ECO:0000313|EMBL:BAC18064.1, ECO:0000313|Proteomes:UP000001409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395
RC   {ECO:0000313|Proteomes:UP000001409};
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01161}.
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DR   EMBL; BA000035; BAC18064.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8FQ79; -.
DR   STRING; 196164.gene:10741662; -.
DR   KEGG; cef:CE1254; -.
DR   eggNOG; COG4667; Bacteria.
DR   HOGENOM; CLU_048271_1_1_11; -.
DR   OMA; VACEPYV; -.
DR   Proteomes; UP000001409; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07208; Pat_hypo_Ecoli_yjju_like; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR045943; DUF6363.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR037483; YjjU-like.
DR   Pfam; PF19890; DUF6363; 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|PROSITE-ProRule:PRU01161};
KW   Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU01161};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW   ProRule:PRU01161}; Reference proteome {ECO:0000313|Proteomes:UP000001409}.
FT   DOMAIN          44..220
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   MOTIF           75..79
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           202..204
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        77
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        202
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   326 AA;  36211 MW;  410BECF7020E2CD2 CRC64;
     MFLWSTAQFS ACRLSFGCPV GGGGARRLIL MSLSSPQYFP EVALIIEGGG TRNAYTAAVV
     DQLIAHDIHV GWVGGVSAGS SHTVNYLSGD RFRTKASFVD FAADRRHSGI RPFLRGKGYF
     HAEHMYEIAP GADQQHPYDF ETFTNNPTPF QISAVRADTG ETVYWGRESA TELSQLMKRV
     RASSTMPGFM PIPVIDGTPY VDGAIGETGG LMLQPALDAG FERFLVLSSR PRDYWRSEFT
     RPGLLTAVLR RYPAVAQATL SRPARYNETK QRILDLEKAG QAYVFFSEDM AIQNTEINLG
     KLRATFDAGM RQTRRDWPAI MEFLRG
//
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