中文摘要：

本文从生物信息学角度对克隆获得的金纹细蛾几丁质酶进行分析，通过课题组提交到GenBank的数据，采用在线分析及相应软件分析预测金纹细蛾几丁质酶（LrCHI）基因核苷酸和氨基酸序列的组成、理化性质、信号肽、糖基化位点、磷酸化位点、疏水性、二级结构和三级结构等，并构建系统发育树。结果表明：LrCHI开放阅读框由1737bp组成，推导578个氨基酸；此序列所编码的蛋白属于几丁质酶18家族，其N端含有信号肽和几丁质酶18家族活性位点，C端为几丁质结合区，无跨膜结构域区域；预测LrCHI为亲水性蛋白；金纹细蛾与鳞翅目的棉铃虫、甜菜夜蛾进化关系最近。分析结果可为LrCHI的科学研究提供有价值的信息，为进一步研究其高级结构与功能的关系提供理论依据。

英文摘要：

In this paper we analyzed Lithocolletis ringoniella chitinase from the perspective of bioinformatics. Based on the data that had been submitted to GenBank by our group, Nucleotide sequence and deduced amino acid sequence ofLithocolletis ringoniella chitinase were analyzed and predicted by the tools ofbioinformatics which are available online or corresponding software in the following aspects： the composition, physical and chemical properties, signalpeptide, O-glycosylation site, phosphorylation site, hydrophobic character, secondary structure, tertiary structure, etc. We also built phylogenetic trees. The results showed that the open reading frame （OR10 of LrCHI consists of 1 737 bp which deduces 578 amino acid sequences. The protein encoded by this sequence belongs to chitinase family 18. There are a signal peptide and a chitinase family 18 active site in the N-terminal region of the polypeptide chain. There is a chitin-binding site in the C-terminal region. No possible transmembrane domain region. LrCHI might be a hydrophilic protein. Lithocolletis ringoniella, phylogenetic relationship is the nearest to Helicoverpa armigera and Spodoptera exigua than other insects. The result of this study may provided very valuable information for experimental research and application development and theoretical basis for further study of the relationships between high-level structure and function.