(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 > Eulophidae: NE > Tetrastichinae: NE > Oomyzus: NE > Oomyzus sokolowskii: 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 MEGRACLVLLLLLRPLAARPNDDLFAAHEIAYRGDDYADDPLVVETTTGL MRGLSRTILDKEVHIYYGVPFAKPPIGPLRFRKPAPLEPWKGVYNATTMP NSCIQERYEYFPGFEGEEMWNPNTNISEDCLYMNIWVPKKIRLRHKGGGD SAEKKNHHQGMPILVWIYGGGYMTGTATLDVYDADMMAARSNAIIASMQY RVGAFGFLYLKDYLEANDDAPGNMGLYDQAMALKWLKDNAKVLGGDPELI TIFGESAGGGSVSLHLMSPVTKGLARRGILQSGTLNAPWSYMSAERATEV ARVLVEDCGCNSTMLEDNPKRVMDCMRSVEARTISVQQWNSYGGILGFPS APTIDGEFLTKDPIEMLKDKKFDKTEIIIGNNENEGTYFILYDFIDYFEK DNPSSLDRSKFLQIINTIFKNMSKIEREAIAFQYTEWENTNDEYMYQRMV ADIVADYFFICPSIHFAQLFADTGMKVYYYFFTQKSSTNMWGDWMGVMHG DEIEYVFGHPLNTSLRYTERERELALRMILAYSNFALHGQPMDENEWPPY TRDNPAYYIFNAEKTAVGKGPRTTACAFWNEFMPRLKGVPDPSPESCNGA VASSVSAGAWALRSDSWLTTPWLLTSLLLLPSSFSLRSL
Reference
Title: Identification and characterization of ace2-type acetylcholinesterase in insecticide-resistant and -susceptible parasitoid wasp Oomyzus sokolowskii (Hymenoptera: Eulophidae) Zhuang HM, Li CW, Wu G Ref: Mol Biol Rep, 41:7525, 2014 : PubMed
A full-length acetylcholinesterase (AChE) cDNA sequence (Os-ace2.s) from insecticide-susceptible (S) parasitoid Oomyzus sokolowskii (Hymenoptera: Eulophidae) and a partial cDNA sequence (Os-ace2.r) from insecticide- resistant (R) O. sokolowskii were identified firstly. Both Os-ace2.s (encoding a protein of 639 amino acid residues) and Os-ace2.r (encoding a protein of 530 amino acid residues) contained the typical conserved motifs, including FGESAGdomains, catalytic triad, acyl pocket, three oxy-anino hole, choline binding site, peripheral anionic site, omega loop and conserved aromatic residues. The multiple alignment and Blast results indicated that Os-ace2.s were ace2 member of AChE gene. There were three replacements of the amino acid residues (Glu 115 Leu, Phe 394 Leu, and Lys 424 Arg) between Os-ace2.s and Os-ace2.r. The ace2 of O. sokolowskii was the AChE gene firstly isolated from hymenopteran parasitoid so far. R O. sokolowskii displayed about 15-20-folds resistance ratios to methamidophos and avermectin. The bimolecular rate constant (k i) value in S O. sokolowskii was 3.8-folds for methamidophos and 12.3 for dichlorvos, respectively higher than those in R O. sokolowskii. The results indicated that the insensitive AChE and replacements of the amino acid residues in Os-ace2 might be involved in the resistance to methamidophos in R O. sokolowskii.
