Gene_locus Report for: 9neop-ACHE1

Chilo suppressalis (striped riceborer) acetylcholinesterase 1 (Ace1) mRNA, complete cds

Comment

Asiatic rice borer moth

Relationship

Family	\|	ACHE
Block	\|	C
Position in NCBI Life Tree	\|	Chilo suppressalis

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Protostomia: N E > Ecdysozoa: N E > Panarthropoda: N E > Arthropoda: N E > Mandibulata: N E > Pancrustacea: N E > Hexapoda: N E > Insecta: N E > Dicondylia: N E > Pterygota: N E > Neoptera: N E > Holometabola: N E > Amphiesmenoptera: N E > Lepidoptera: N E > Glossata: N E > Neolepidoptera: N E > Heteroneura: N E > Ditrysia: N E > Obtectomera: N E > Pyraloidea: N E > Crambidae: N E > Crambinae: N E > Chilo: N E > Chilo suppressalis: N E

There are 34 a/b hydrolases in Chilo suppressalis view in a: Table

ACHE : 9neop-ACHE2Chilo suppressalis (striped riceborer) (Lepidoptera: Pyralidae); Papilio xuthus (frgt); Pectinophora gossypiella(frgt) acetylcholinesterase.
Carb_B_Arthropoda : 9neop-a3qr02Chilo suppressalis (striped riceborer) esterase (fragment), chisp-a0a0b4rxr9Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4rxs2Chilo suppressalis (Asiatic rice borer moth). Carboxyl/choline esterase, chisp-a0a0b4rxs5Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4rxs6Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0k0xrs9Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4rxt0Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4rxt5Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4rxu8Chilo suppressalis (Asiatic rice borer moth). Carboxylesterase, chisp-a0a0k0xrw3Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4rxv9Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4rxw5Chilo suppressalis (Asiatic rice borer moth). Carboxyl/choline esterase, chisp-a0a0k0xrv9Chilo suppressalis (Asiatic rice borer moth). Antennal carboxylesterase 5, chisp-a0a0b4rxy3Chilo suppressalis (Asiatic rice borer moth). Antennal esterase, chisp-a0a0b4rxy9Chilo suppressalis (Asiatic rice borer moth). Carboxylesterase, chisp-a0a0b4ry19Chilo suppressalis (Asiatic rice borer moth). Carboxyl/choline esterase, chisp-a0a0b4ry26Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4ry77Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4ry83Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4ryb9Chilo suppressalis (Asiatic rice borer moth). Carboxylic ester hydrolase, chisp-a0a0b4ryc8Chilo suppressalis (Asiatic rice borer moth). Carboxyl/choline esterase, chisp-a0a0k0xrl5Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein, chisp-a0a0k0xrm7Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein, chisp-a0a0k0xrn6Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein, chisp-a0a0k0xrp4Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein, chisp-a0a0k0xrp9Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein, chisp-a0a0k0xrt4Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein, chisp-a0a0k0xrt8Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein, chisp-a0a0k0xrv7Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein, chisp-a0a0k0xrw2Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein, chisp-a0a0k0xrx2Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein.
Juvenile_hormone_esterase : chisp-a0a0k0xrw8Chilo suppressalis (Asiatic rice borer moth) Uncharacterized protein

Molecular evidence		Database
5 mutations: Table (e.g. : A314S, E101D, F402V ... more) (less) A314S : Mutation in acetylcholinesterase1 associated with triazophos resistance in rice stem borer, Chilo suppressalis (Lepidoptera: Pyralidae) E101D : Amino acid substitutions of acetylcholinesterase associated with carbofuran resistance in Chilo suppressalis F402V : Amino acid substitutions of acetylcholinesterase associated with carbofuran resistance in Chilo suppressalis H668P : Mutation in acetylcholinesterase1 associated with triazophos resistance in rice stem borer, Chilo suppressalis (Lepidoptera: Pyralidae) R667Q : Amino acid substitutions of acetylcholinesterase associated with carbofuran resistance in Chilo suppressalis No structure No kinetic No Substrate No inhibitor		2 Genbank : EF453724, ABO38111 1 UniProt : A5HBN8 3 UniProt : A5HBN8, A0A0B4RY90, A0A0G3VFZ6 3 Interpro : A5HBN8, A0A0B4RY90, A0A0G3VFZ6 3 Pfam : A5HBN8, A0A0B4RY90, A0A0G3VFZ6 3 PIRSF : A5HBN8, A0A0B4RY90, A0A0G3VFZ6 3 SUPERFAM : A5HBN8, A0A0B4RY90, A0A0G3VFZ6

Sequence

Peptide

Graphical view for this peptide sequence: 9neop-ACHE1
Colored MSA for ACHE (raw)
MRVVLAALTALAARALAGPHEHRARHHAPDHPLHFPAPANPAQPYRGHGE AARYNPELDTILPRVEDHETSSKRAKLDDAETSSKRDDDRFYSNHERIDD EGFLADEPQPGPEDDDPLIVRTRKGRVRGITLTAATGKKVDAWFGIPYAQ KPIGDLRFRHPRPAESWGEEILNTTTLPHPCVQIIDTVFGDFPGAMMWNP NTDMQEDCLYINIVSPRPRPKNAAVMLWVFGGGFYSGTATLDVYDPKIMV SEEKIVYVSMQYRVASLGFLFFDTPDVPGNAGMFDQLMALQWVKDNIAYF GGNPHNVTLFGESAGAVSVSLHLLSPLSRNLFSQAIMQSGAATAPWAIIS REESILRGTRLAEAVHCPHSLKDMGPMIECLRKKSADELVNNEWGTLGIC EFPFVPIIDGSFLDEMPIRSLAHQNFKKTNILMGSNTEEGYYFILYYLTE LFPKEENVGITREQYLQAVRELNPYVSDVGRQAIVFEYTDWLNPEDPVRN RNALDKMVGDYHFTCGVNEFAHRYAETGNNVYTYYYKHRSKNNPWPSWTG VMHADEINYVFGEPLNPGKNYSPEEVEFSKRIMRYWANFARSGNPSLNPN GDMTKVHWPVHTAFGGEYLSLAVNSSAVGHGLKVKQCAFWQKYLPQLMAA TTKPEPIQNCTSNSGTRHYYGVTSLSLVTVFGFLQPTILKYIII
Legend This 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
MRVVLAALTALAARALAGPHEHRARHHAPDHPLHFPAPANPAQPYRGHGE
AARYNPELDTILPRVEDHETSSKRAKLDDAETSSKRDDDRFYSNHERIDD
EGFLADEPQPGPEDDDPLIVRTRKGRVRGITLTAATGKKVDAWFGIPYAQ
KPIGDLRFRHPRPAESWGEEILNTTTLPHPCVQIIDTVFGDFPGAMMWNP
NTDMQEDCLYINIVSPRPRPKNAAVMLWVFGGGFYSGTATLDVYDPKIMV
SEEKIVYVSMQYRVASLGFLFFDTPDVPGNAGMFDQLMALQWVKDNIAYF
GGNPHNVTLFGESAGAVSVSLHLLSPLSRNLFSQAIMQSGAATAPWAIIS
REESILRGTRLAEAVHCPHSLKDMGPMIECLRKKSADELVNNEWGTLGIC
EFPFVPIIDGSFLDEMPIRSLAHQNFKKTNILMGSNTEEGYYFILYYLTE
LFPKEENVGITREQYLQAVRELNPYVSDVGRQAIVFEYTDWLNPEDPVRN
RNALDKMVGDYHFTCGVNEFAHRYAETGNNVYTYYYKHRSKNNPWPSWTG
VMHADEINYVFGEPLNPGKNYSPEEVEFSKRIMRYWANFARSGNPSLNPN
GDMTKVHWPVHTAFGGEYLSLAVNSSAVGHGLKVKQCAFWQKYLPQLMAA
TTKPEPIQNCTSNSGTRHYYGVTSLSLVTVFGFLQPTILKYIII

Reference

Title:

Jiang X, Qu M, Denholm I, Fang J, Jiang W, Han Z

Ref:

378

PubMed

Other Papers

Send your questions or comments to :Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.

For technical information about these pages see:
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AcePerl Lincoln Stein Home Page

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