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作 者:钱立富 项笑鹃 石安琪 董现云 孙章琦 李晓明[1] QIAN Lifu;XIANG Xiaojuan;SHI Anqi;DONG Xianyun;SUN Zhangqi;LI Xiaoming(School of Life Science,Huaibei Normal University,235000,Huaibei,Anhui,China;Experimental High School Attached to Huaibei Normal University,Huaibei Normal University,235000,Huaibei,Anhui,China)
机构地区:[1]淮北师范大学生命科学学院,安徽淮北235000 [2]淮北师范大学附属实验中学,安徽淮北235000
出 处:《淮北师范大学学报(自然科学版)》2024年第4期35-41,共7页Journal of Huaibei Normal University:Natural Sciences
基 金:安徽省高校自然科学研究重点项目(2022AH050395);淮北师范大学博士科研启动资助项目(03106094)。
摘 要:基于NCBI数据库,对大别山原矛头蝮(Protobothrops dabieshanensis)Cytb基因进行生物信息学分析,研究其结构和功能。结果表明,大别山原矛头蝮Cytb长度为1 113 bp,共编码371个氨基酸,具有较强密码子偏好性,编码蛋白为稳定、疏水性蛋白质;具有3个N-糖基化和33个磷酸化修饰位点,存在10个跨膜结构域,二级、三级结构以α螺旋和无规卷曲为主,与多个线粒体呼吸链蛋白相互作用;大别山原矛头蝮与乡城原矛头蝮(Protobothrops xiangchengensis)、菜花原矛头蝮(Protobothrops jerdonii)可能由共同祖先演化而来。研究结果为进一步开展大别山原矛头蝮能量代谢及生物学进化研究提供参考。The Cytb gene of Protobothrops dabieshanensi was analyzed by bioinformatics methods based on the NCBI database.The results showed that the sequence of Cytb gene in P.dabieshanensi was 1113 bp,with strong codon preference,which encoded 371 amino acids.Cytb protein in P.dabieshanensi was a stable and hydrophobic protein with 10 transmembrane helical domains.Cytb protein had 3 potential N-glycosylation modification sites,33 phosphorylation sites,and its secondary and tertiary structures were dominated byαhelix and random coil.Cytb protein may interact with multiple mitochondrial respiratory chain proteins.P.dabieshanensi,Protobothrops xiangchengensis and Protobothrops jerdonii may have evolved from the same ancestor.The results of this study will provide references for further research on energy metabolism and functional genes of P.dabieshanensi.
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