(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Protostomia: NE > Ecdysozoa: NE > Panarthropoda: NE > Arthropoda: NE > Mandibulata: NE > Pancrustacea: NE > Hexapoda: NE > Insecta: NE > Dicondylia: NE > Pterygota: NE > Neoptera: NE > Holometabola: NE > Hymenoptera: NE > Apocrita: NE > Terebrantes: NE > Chaldicoidea group: NE > Chalcidoidea: NE > Pteromalidae: NE > Pteromalinae: NE > Anisopteromalus: NE > Anisopteromalus calandrae: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MERPEVKTLSGQVRGLKQISVEGIGFYAFKGIPYAKPPVGELRFKDPVPI EPWQEVREATEFGPMAAQFDVISKFSGGSDDCLYINVYTKKINSNVKQPV MFYIHGGGFIFGSGNDFFYGPDFLMRKDIVLVTFNYRLGVFGFLNLEHEV APGNQGLKDQVMALKWVRDNIANFGGDSENVTIFGESAGGASVHYLTVSP LAKGLFHKAISQSGVFMNPWASVSGEPRKKAYELCELLGKKTTDPVEIVK FLRTVDTMKLIEHQGELQIQELQKKCLSAFVPGVDDKSPNPFMPFSREVA VEQAAHVPYLIGYNDREGTLLYKIFENDDFESKNLRFEEFIHPNFAETLK RKKISLEDLKRMYFKNKKISKETTGKFIDLFSDMYFIQGIHQVARVQAER NSAPTYMYQFTYDQGPNFSKGMFSIDEPGSTHMDELIYLFSMKFQETLNM EPIDKKSPHFRVMEQMVELWTNFAKYGRPIPAPTELLPVHWLPMNDGTVL RYLNIGEELRMEKVLNIEERYDYKLICHREKV
References
Title: Differential mRNA expression levels and gene sequences of a putative carboxylesterase-like enzyme from two strains of the parasitoid Anisopteromalus calandrae (Hymenoptera: Pteromalidae) Zhu YC, Dowdy AK, Baker JE Ref: Insect Biochemistry & Molecular Biology, 29:417, 1999 : PubMed
Carboxylesterase-like enzyme cDNAs have been cloned and sequenced from malathion-resistant and susceptible strains of the parasitoid Anisopteromalus calandrae (Howard) (Hymenoptera: Pteromalidae). The cDNAs consist of 1963 nucleotides including a 35 bp untranslated 5'-end, a 1596 bp open reading frame, and a 332 bp untranslated 3'-end. The open reading frame encodes 532 amino acid residues. The predicted protein sequence from these cDNAs includes 2 potential N-glycosylation sites, a carboxylesterase type-B serine active site FGGDSENVTIFGESAG, and conserved residues Ser187, Glu317, and His432 to function as the catalytic triad. The predicted carboxylesterase-like enzyme sequence is most similar to that of the carboxylesterase from the peach-potato aphid, Myzus persicae with 45% sequence identity. Alignment of the parasitoid carboxylesterase-like enzyme cDNAs revealed that there are two nucleotide differences in the open reading frame between the parasitoid strains, including a silent mutation and a point mutation that presumably causes a gene product difference. A nucleotide thymine at position 658 in the susceptible strain cDNA is replaced by a guanine in the resistant strain cDNA. This substitution leads to an amino acid change from tryptophan (Trp220) in the susceptible strain to glycine (Gly220) in the resistant strain. This substitution is genetically linked to resistance but it is not known how or if this amino acid substitution affects detoxification of malathion. Northern blot analyses demonstrated that expression level of the carboxylesterase-like enzyme mRNA in adult A. calandrae is approximately 30-fold higher in the resistant strain relative to that in the susceptible strain. Southern analysis indicated that Pst I or Eco RI restriction sites are different in the two strains. Both a modified gene structure and an increase in expression of carboxylesterase may be responsible for the high level of resistance found in this beneficial wasp.
Title: Detection of single-base substitution in an esterase gene and its linkage to malathion resistance in the parasitoid Anisopteromalus calandrae (Hymenoptera: Pteromalidae) Zhu YC, Dowdy AK, Baker JE Ref: Pest Sci, 55:398, 1999 : PubMed
Anisopteromalus calandrae (Howard) (Hymenoptera : Pteromalidae) is an important para-sitoid of stored-grain insect pests. Partial cDNA sequences of an esterase-like enzyme have been obtained from a malathion-resistant (R) strain and a susceptible (S) strain of this wasp. A single-base substitution in the R strain has been confirmed by using PCR amplification of specific allele (PASA) to amplify genomic DNA extracted from individual resistant and susceptible parents, F1 hybrids from double reciprocal crosses, and progeny from backcrosses. The R allele appeared to be inherited in a strict Mendelian fashion in both diploid female and haploid male progeny. The esterase fragment co-segregated with resistance in these crosses and backcrosses. Female wasps in a mixed population of A calandrae that survived a malathion screen carried the R allele for the esterase-like enzyme, while those wasps that died did not have the R allele. The single base-pair mutation, guanine in the R strain and thymine in the S strain, presumably results in a tryptophan-to-glycine amino acid substitution in the encoded protein. We do not know how these amino acid substitutions may relate to functional differences in the enzyme. However, this esterase gene or another linked esterase gene may encode the resistance-associated malathion detoxifying activity in the R strain.
