ID   EST5B_DROMI             Reviewed;         545 AA.
AC   O16170; Q56RI7;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Esterase-5B;
DE            Short=Est-5B;
DE            EC=3.1.1.1;
DE   AltName: Full=Carboxylic-ester hydrolase 5B;
DE            Short=Carboxylesterase-5B;
DE   Flags: Precursor;
GN   Name=Est-5B; Synonyms=Est5B;
OS   Drosophila miranda (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7229;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9475741; DOI=10.1093/genetics/148.1.305;
RA   King L.M.;
RT   "The role of gene conversion in determining sequence variation and
RT   divergence in the Est-5 gene family in Drosophila pseudoobscura.";
RL   Genetics 148:305-315(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MSH22;
RX   PubMed=15545653; DOI=10.1534/genetics.104.033068;
RA   Bartolome C., Maside X., Yi S., Grant A.L., Charlesworth B.;
RT   "Patterns of selection on synonymous and nonsynonymous variants in
RT   Drosophila miranda.";
RL   Genetics 169:1495-1507(2005).
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   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P25726}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AF016109; AAB70221.1; -; Genomic_DNA.
DR   EMBL; AY754520; AAX13095.1; -; Genomic_DNA.
DR   AlphaFoldDB; O16170; -.
DR   SMR; O16170; -.
DR   ESTHER; dromi-est5b; Carb_B_Arthropoda.
DR   MEROPS; S09.947; -.
DR   FlyBase; FBgn0021337; Dmir\Est-5B.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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   Disulfide bond; Glycoprotein; Hydrolase; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..545
FT                   /note="Esterase-5B"
FT                   /id="PRO_0000008555"
FT   ACT_SITE        207
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        467
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        84..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        259..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        515..536
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   545 AA;  60810 MW;  B47AE31B95D7E657 CRC64;
     MYCEKLILLL GCFWISSSAS DPADPLLVDL PNGKLRGRDN GNYYSYESLP YAEPPVGDLR
     FEAPQPYKQQ WTDTFDATQP PVLCMQWDQF IQGDDKLAGN EDCLTVSVYR PKNSSRNSFP
     VVAQIHGVAF MFGGASQNGH ENFMREGNLI LVKISYRLGP LGFVSTGDAD LSGNFGLKDQ
     RLALLWIKQN IASFGGEPEN ILVIGHSAGG GSVHLQVLRE DFSKVAKAAI SFSGNALDPW
     VVQQGGRGRA FELGRIVGCG QASDSVTLKK CLKSKPASEI VSAVRNFLVF AYVPFTPFGP
     VVESPEAPEA FISQHPIDII KSGKFAQVPW AVTYTTEDGG YNAALLLEKQ ASSGRELIVD
     LNDRWFDWAP YLLFYRDSMT TIKDMDDYSR KLRQEYLGDR RFSVESYWDL QRLFTDVLFK
     NSTEISLDLH RKHGKSPVYA FVYDNPANTG IGQGLAKRTD INFGTVHGDD YFLIFENIVR
     EPQLRSDEEI ISRNFLKMLN DFVLSENGTL AFGTCDFQDN VGSSKLQLLS ITRNGCENLE
     LESFP