ID   YR571_MIMIV             Reviewed;         297 AA.
AC   Q5UR46;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   07-OCT-2020, entry version 56.
DE   RecName: Full=Uncharacterized protein R571;
DE            EC=3.1.1.-;
GN   OrderedLocusNames=MIMI_R571;
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}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AY653733; AAV50834.1; -; Genomic_DNA.
DR   RefSeq; YP_003987086.1; NC_014649.1.
DR   SMR; Q5UR46; -.
DR   GeneID; 9925207; -.
DR   KEGG; vg:9925207; -.
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..297
FT                   /note="Uncharacterized protein R571"
FT                   /id="PRO_0000253923"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          17..196
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           21..26
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           51..55
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           183..185
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        53
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   297 AA;  33945 MW;  47D70C76850BE9BA CRC64;
     MENSTPKKIS ESQIKNLALS GGGFYGFAVV GALKEIFDNY IDPNNIKTIS GVSVGSIIAT
     MLAIGYSIDE ITKIMFEIDM DTLIKDSYFS YYTLWEKFGM YNADKLEQEI ERIIRDKTHI
     KNCTFSQIEK NLIIVTTNLN YQRTRIFSKL ETPTMIISKA VRMSISYPFI MVPVLFEGDL
     YGDGGETLNY PITLFDDDLD KTIGITFANH NENDDGTLKT RLPINNFYDY IVSLGLTMNR
     SSYISQISSK YLDRSIVIKI NEDISSMQFN LDLKQKEYLF ECGIKSVKQQ IIKLINH