ID   ESTE_SFAVA              Reviewed;         592 AA.
AC   Q0E588;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   23-FEB-2022, entry version 50.
DE   RecName: Full=Putative esterase;
DE            EC=3.1.1.1;
GN   ORFNames=ORF13;
OS   Spodoptera frugiperda ascovirus 1a (SfAV-1a).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Ascoviridae; Ascovirus.
OX   NCBI_TaxID=113370;
OH   NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16987980; DOI=10.1128/jvi.01639-06;
RA   Bideshi D.K., Demattei M.V., Rouleux-Bonnin F., Stasiak K., Tan Y.,
RA   Bigot S., Bigot Y., Federici B.A.;
RT   "Genomic sequence of Spodoptera frugiperda Ascovirus 1a, an enveloped,
RT   double-stranded DNA insect virus that manipulates apoptosis for viral
RT   reproduction.";
RL   J. Virol. 80:11791-11805(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AM398843; CAL44613.1; -; Genomic_DNA.
DR   RefSeq; YP_762368.1; NC_008361.1.
DR   SMR; Q0E588; -.
DR   GeneID; 4306180; -.
DR   KEGG; vg:4306180; -.
DR   Proteomes; UP000008030; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..592
FT                   /note="Putative esterase"
FT                   /id="PRO_0000330603"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        513
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   592 AA;  67272 MW;  38CF21FCEA311A7A CRC64;
     MCVNRVRSIV SLTLIAYLSV LMGVSVYFYV LIESVYQQFS DMSENYVQLV KDTSSTPIVV
     ATHGHSTNRS HQSVLFTARA DVNISMETIL HVEFNYTTAL GTMDDTFNII NFYGLKYRHV
     DLIDPFGNSL PVVNSKSSFG FTDCSSDERV RCPSTRRPFT GTLDCLTLDM HMQSWNRDRS
     TDHFKRPIII WLGEIMGSLW RLIGNGVIVI RVNYRRGVYG FVCHRDERLP YYNQGVNDVM
     HAIEWVTENA ERFAGDTKRI TLAGHGDDGK VVEYVRMYHS HHLPLDKYIV MSAAETGSRD
     LTCSSNSNIL VTAARILGMP SVPVHDTTAG ERGVYDAVRY LSFIEPKRLM ERLYDLKEIF
     QPCPGEIRST ASDVNGLGKA FEGVDSDDCK FINTDTPVLY MNTLNEYANK VKLDDSFMHA
     RAHTLRRVIE HVLARRFKPH RVTRYCNVTI SEPAEIGSER YEPCDGEVIN VESLGRVLTD
     FEYIAPTSRI CEAAVGCGAS FYHYVYDFKN ASHGDDLRLL MSEHDQRNLT KFERQLADGI
     GMMISRFVRR GYPVVKRDNW CSSTSLVAQI MEINTTPNVI TTQTQVRGTV ER