ID   CHLE_MIMIV              Reviewed;         579 AA.
AC   Q5UR02;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   23-FEB-2022, entry version 64.
DE   RecName: Full=Probable cholinesterase;
DE            EC=3.1.1.8;
DE   AltName: Full=Acylcholine acylhydrolase;
DE   Flags: Precursor;
GN   OrderedLocusNames=MIMI_L906;
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: May be involved in the disruption of the host membrane.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acylcholine + H2O = a carboxylate + choline + H(+);
CC         Xref=Rhea:RHEA:21964, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:35287; EC=3.1.1.8;
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY653733; AAV51163.1; -; Genomic_DNA.
DR   RefSeq; YP_003987440.1; NC_014649.1.
DR   SMR; Q5UR02; -.
DR   ESTHER; mimvi-cxes; Cholinesterase-like.
DR   GeneID; 9925575; -.
DR   KEGG; vg:9925575; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0004104; F:cholinesterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Reference proteome; Serine esterase; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..579
FT                   /note="Probable cholinesterase"
FT                   /id="PRO_0000041775"
FT   ACT_SITE        217
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        337
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        451
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   579 AA;  64868 MW;  1DD9D68940B8B9E6 CRC64;
     MTDHKIIMLL LLGIYCIQAT QFTQVNIDNG PIKGTLQYVE GRAIRVFKGI PFAEPPVNNL
     RWKAPVPYTK KWHNPLNTTE YKPKCPQYVA PGTVPEPRGI SEDCLYTNVW APVPEYHGET
     FPVMVWIHGG AFISGSPEDF GVGNFSILAV TKRIIIVAAS YRVNAFGFFS SELLGKSQLE
     ARGVYGLLDQ RLGLKWVKNN IAAFGGKSKD ITIYGQSAGG ISVCLQAVTP LNDLPGEKLF
     TRVIGSSGYC DILPMTNNSA DAGLVQKLNC TTKECLYALP WQNITNAVGP GFLSFQPTVG
     INKFLPDQPI SLLADRTNPR SKNFVPDIYM QGFTANEGTF VLYNYFPQTY DNPNTPGFPT
     QQMADALSIA SGNYSAEFYY NDLAPLYSTE YNSNVTYPGQ GFISRVDDIM ACNTRRNMIY
     WQQSKKTKAH SWYFDSAPDT HIYPSWTKVF HESDVFYVAR RCDGLWCTNL TCQQDNLGKT
     MNIYWNSAIR AASLTPKNKM DNLRDVPVWP QYGKNEVVMH FTAVGENKGP QTSVLFSSII
     SADGDYQYLQ RCKILDRVRA EYYNIPALDP ETYLNACSK