(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 > Paraneoptera: NE > Hemiptera: NE > Sternorrhyncha: NE > Aphidomorpha: NE > Aphidoidea: NE > Aphididae: NE > Aphidinae: NE > Macrosiphini: NE > Myzus: NE > Myzus persicae: 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 MDQWLLWFSYLVASTYGLSLRHARHQSVGTPTAEEILEPQILIEDTDHVF RQRASDMFAQEPEYTEKRNLNHRRRSEFSGNQDNDFESSGETYSAYKSDD PLVIHTNKGKIRGITQAASTGKLVDAWLGIPYAKKPIGDLRFRHPRPIDR WDNTNPETILNCTTPPNTCVQIFDTLFGDFPGATMWNPNSPVSEDCLYIN VVVPKPRPQNAAVMVWIFGGGFYSGSATLDIYDPKVLVSEENVILVSMQY RVASLGFLYFDTEDVPGNAGLFDQLMALQWVHENIKLFGGNPNNVTLFGE SAGAVSVSLHLLSPLSRNLFNQAIMESGSSTAPWAILSREESYSRGLRLA RAMGCPDDRNEIHKTVECLRKANSSTMVEKEWDHVAICFFPFVPVVDGAF LDDYPQKSLSTNNFKKTNILMGSNSEEGYYSIFYYLTELFKKEENVVVSR ENFVKAIGQLNPNADAAVKSAIEFEYTDWFSPNDPEKNRNALDKMVGDYQ FTCNVNEFAHKYALTGNNVYMYYFKHRSLNNPWPKWTGVMHGDEISYVFG DPLNPNKRYEIEEIELSKKMMRYWTNFAKTGNPSKTFEGSWVTPKWPVHT AYGKEFLTLDTNNTSIGVGPRLEQCAFWKNYVPDLMAISKSMKSDKNCTT ISGGTKTYMIELSLWTIVMTTAVLML
Reference
Title: An amino acid substitution on the second acetylcholinesterase in the pirimicarb-resistant strains of the peach potato aphid, Myzus persicae Nabeshima T, Kozaki T, Tomita T, Kono Y Ref: Biochemical & Biophysical Research Communications, 307:15, 2003 : PubMed
cDNAs encoding two acetylcholinesterases (AChEs) were isolated from the peach potato aphid, Myzus persicae. MpAChE1 was orthologous and MpAChE2 was paralogous with the ace of Drosophila melanogaster. The deduced amino acid sequence of MpAChE1 cDNA was identical between the pirimicarb susceptible and resistant strains. However, a single amino acid substitution of Ser431Phe on MpAchE2 was found in the pirimicarb resistant strains. This substitution was located in the acyl pocket of the enzyme and was thought to alter the ligand specificity.
