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
//