ID   EST1_SCHGA              Reviewed;         198 AA.
AC   P81429;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Esterase SG1;
DE            EC=3.1.1.1;
DE   AltName: Full=Carboxylic-ester hydrolase;
DE   Flags: Precursor; Fragment;
GN   Name=SG1;
OS   Schizaphis graminum (Green bug aphid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC   Aphidoidea; Aphididae; Aphidini; Schizaphis.
OX   NCBI_TaxID=13262;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-41.
RX   PubMed=10612041; DOI=10.1016/s0965-1748(99)00082-x;
RA   Ono M., Swanson J.J., Field L.M., Devonshire A.L., Siegfried B.D.;
RT   "Amplification and methylation of an esterase gene associated with
RT   insecticide-resistance in greenbugs, Schizaphis graminum.";
RL   Insect Biochem. Mol. Biol. 29:1065-1073(1999).
CC   -!- FUNCTION: Overproduction of nonspecific esterases is a common mechanism
CC       of resistance to organophosphate insecticides.
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10039};
CC   -!- MISCELLANEOUS: This esterase confers organophosphate insecticide
CC       resistance.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; Y17580; CAA76792.1; -; mRNA.
DR   AlphaFoldDB; P81429; -.
DR   SMR; P81429; -.
DR   MEROPS; S09.962; -.
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   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Serine esterase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:10612041"
FT   CHAIN           22..>198
FT                   /note="Esterase SG1"
FT                   /id="PRO_0000008568"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        87..104
FT                   /evidence="ECO:0000250"
FT   CONFLICT        24
FT                   /note="A -> T (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28
FT                   /note="R -> N (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         198
SQ   SEQUENCE   198 AA;  21897 MW;  EFEF43EA6A5D5987 CRC64;
     MSNTCRIVLF YLITCIFTCS ASDAPKVRVN SGDIAGGYEY TYSGRKIYSF LGIPYASPPV
     QNYRFKEPQP VKPWLGTWNA TIPGSSCMGP DYESNFKLVG QEDCLYLNVY TPKLPRENTP
     DDLMDVVVHI HGGAFMSGEG ISLGPQYLLD INNFVYVTIN YRVGVLGFAT TGDNILPANN
     GMKDQVAALK WIQQNIVA