ID   YL446_MIMIV             Reviewed;         332 AA.
AC   Q5UQP2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   02-DEC-2020, entry version 56.
DE   RecName: Full=Uncharacterized protein L446;
DE            EC=3.1.1.-;
GN   OrderedLocusNames=MIMI_L446;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- FUNCTION: Probable lipid hydrolase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AY653733; AAV50712.1; -; Genomic_DNA.
DR   RefSeq; YP_003986953.1; NC_014649.1.
DR   SMR; Q5UQP2; -.
DR   GeneID; 9925070; -.
DR   KEGG; vg:9925070; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..332
FT                   /note="Uncharacterized protein L446"
FT                   /id="PRO_0000247289"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          58..239
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           93..97
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           226..228
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        95
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        226
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   332 AA;  37991 MW;  C6E1247647F1F992 CRC64;
     MNNSNTDNII IINDSEPTYN LEDVINEIGD LLEDFDKIID QYKQTIDQMV KKPKYVNLVL
     SGGSIRGISH IGVIKKLIDE ELLDLSKMKA VAGVSAGAML GLLIVLGFTI GEIWDFILNL
     DTKKIVDPDF MLILEKCGVE RGRIIYDLIE DILTSKTDTK HINFKQLYEK TGIHFTVVGS
     CLTTKDVIYY DHINTPTFKV SVAVRISIGM PGFFTPIDIG GKKYIDGAVL NNYPMNLFAK
     ELDKTIGILI CNEHNTNYKY FEEYFMAIIN LFMYNYFEKT CHQYADNTIY VKKAPENVFI
     FNFDLDNNTK MKLFEYGIEA AEEFIKNKFD NK