ID   EST2_CAEEL              Reviewed;         554 AA.
AC   Q07085; O16351;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 3.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Esterase CM06B1;
DE            EC=3.1.1.1;
GN   ORFNames=F13H6.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8219278; DOI=10.3109/10425179309020836;
RA   Fedon Y., Cousin X., Toutant J.-P., Thierry-Mieg D., Arpagaus M.;
RT   "cDNA sequence, gene structure, and cholinesterase-like domains of an
RT   esterase from Caenorhabditis elegans mapped to chromosome V.";
RL   DNA Seq. 3:347-356(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Lipid-anchor;
CC       Cytoplasmic side.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; X66104; CAA46899.1; -; Genomic_DNA.
DR   EMBL; FO081144; CCD69466.1; -; Genomic_DNA.
DR   PIR; A56690; A56690.
DR   PIR; T31783; T31783.
DR   RefSeq; NP_504621.1; NM_072220.4.
DR   AlphaFoldDB; Q07085; -.
DR   SMR; Q07085; -.
DR   BioGRID; 44066; 16.
DR   DIP; DIP-25312N; -.
DR   IntAct; Q07085; 2.
DR   STRING; 6239.F13H6.3; -.
DR   ESTHER; caeel-ester; Carb_B_Nematoda.
DR   MEROPS; S09.986; -.
DR   EPD; Q07085; -.
DR   PaxDb; Q07085; -.
DR   PeptideAtlas; Q07085; -.
DR   EnsemblMetazoa; F13H6.3.1; F13H6.3.1; WBGene00017431.
DR   GeneID; 179020; -.
DR   KEGG; cel:CELE_F13H6.3; -.
DR   UCSC; F13H6.3; c. elegans.
DR   CTD; 179020; -.
DR   WormBase; F13H6.3; CE09375; WBGene00017431; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   HOGENOM; CLU_006586_13_3_1; -.
DR   InParanoid; Q07085; -.
DR   OMA; SSDFCAY; -.
DR   OrthoDB; 754103at2759; -.
DR   PhylomeDB; Q07085; -.
DR   PRO; PR:Q07085; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00017431; Expressed in larva and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; 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; IPR043187; CM06B1-like.
DR   PANTHER; PTHR45029; PTHR45029; 1.
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   Cell membrane; Cytoplasm; Disulfide bond; Hydrolase; Lipoprotein; Membrane;
KW   Myristate; Reference proteome; Serine esterase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..554
FT                   /note="Esterase CM06B1"
FT                   /id="PRO_0000070272"
FT   ACT_SITE        208
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        331
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        446
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..98
FT                   /evidence="ECO:0000250"
FT   CONFLICT        543..554
FT                   /note="ELVYGKKKSAKI -> NWSMERRSRQRFNFF (in Ref. 1;
FT                   CAA46899)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   554 AA;  61825 MW;  909F8845E864305F CRC64;
     MGGFLSHLTP EQNVEALKAS CGPVRGNIYK HDDVIVDGYL GIPYAKPPVG ELRFKKPVTV
     DVWTEIKDCY KYGPACVQTG GFEQIAGPRT PTPEEAGCLT LNVFTPRNAS SEFKNGRPVM
     VYIHGGGYEL CASSDFCAYS LSGTLPLKDV VVVSINYRLG VFGFLTTGDN VCPGNFGLWD
     QTLALKWVQK HISSFGGDPN CVTVFGQSAG GASTDLLSLS PHSRDLFQRF IPISGTAHCD
     FAIRASENQA KIFREFAEFH GFSGRDSSAL FKWYQEQSPE TLSNVKGYKK SISGFLTFIP
     NLDGDFFPKP LDELRKEAPK KQMMTGVTEY EGLMLASMNP AFSPADVGLT LMPQGIYGKD
     VVSNPDEIQK IFYEKYVEGV DKSDELAMRK KLCEALGDEF FNVGVIQAAK NAAKHGNEVY
     FYTFEYVNPD SFGMWDGMMP FKAAVHCTEL RYLLGEGVYS KFEPTEEDRK VMETTTTLFS
     NFAKYGNPNG KGATAEIWEK YSLNRPERHY RISYPKCEMR DVYHEGRIQF LEKIDGDSDK
     YQELVYGKKK SAKI