(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 > Amphiesmenoptera: NE > Lepidoptera: NE > Glossata: NE > Neolepidoptera: NE > Heteroneura: NE > Ditrysia: NE > Obtectomera: NE > Noctuoidea: NE > Noctuidae: NE > Heliothinae: NE > Helicoverpa: NE > Helicoverpa armigera: 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 MAMISAVNDFLDDLRGGRMTDAPVVTVEQGQLQGKVVNSPTGKAYYSFQG IPYAKPPLGSLRFKAPQPPEPWDGIREATSEGSVSAQVDFLGSKQFTGDE NCLFLNISTPNLDGEFLPVMVFIHGGGFTFGSGNSDFYGADYLVEKDVVV VTINYRCGVLGFLSLNTPEVPGNAGIKDMVQAIRWIKNNIHNFGGNSGNV TIFGESAGGAAVSLLTASPLTKNLISKAIIQSGTALSNWSIQRNPLESAR NIAKILGCESTDPEEILDFLNATSTKDLVEAHQKLSPEEEFPDTINAFGY VVEKEFPGVEAVITESFLDLLTSGRVADIPIMIGSTSLEFTLERKTDDLQ VFIPDELNIERNSEESLAIADQIKTLYFKGSHTGVESLPEYFELLSDAII NIDTHRHVQYLINVSKKPIYYYKFDYVGELNISNKILNSFGLKRAMHMDE LGYLFKNDLQKGVEPTTLDVKMRERMLRLWTNFAKSGNPTPDENHYLTVT WLPVTKDNLYYLNLGQELSLATNPDKEKMEFWDELYS
Some of the resistance of Helicoverpa armigera to conventional insecticides such as organophosphates and synthetic pyrethroids appears to be due to metabolic detoxification by carboxylesterases. To investigate the H. armigera carboxyl/cholinesterases, we created a data set of 39 putative paralogous H. armigera carboxyl/cholinesterase sequences from cDNA libraries and other sources. Phylogenetic analysis revealed a close relationship between these sequences and 70 carboxyl/cholinesterases from the recently sequenced genome of the silkworm, Bombyx mori, including several conserved clades of non-catalytic proteins. A juvenile hormone esterase candidate from H. armigera was identified, and B. mori orthologues were proposed for 31% of the sequences examined, however low similarity was found between lepidopteran sequences and esterases previously associated with insecticide resistance from other insect orders. A proteomic analysis of larval esterases then enabled us to match seven of the H. armigera carboxyl/cholinesterase sequences to specific esterase isozymes. All identified sequences were predicted to encode catalytically active carboxylesterases, including six proteins with N-terminal signal peptides and N-glycans, with two also containing C-terminal signals for glycosylphosphatidylinositol anchor attachment. Five of these sequences were matched to zones of activity on native PAGE at relative mobility values previously associated with insecticide resistance in this species.
