Mutation detail:
Mutation site | N214A |
Virus | SARS-CoV |
Mutation level ![]() |
Amino acid level |
Gene/protein/region type | ORF1ab(3C-like protease) |
Gene ID | 1489680 |
Country | - |
Mutation type ![]() |
nonsynonymous mutation |
Genotype/subtype/clade | - |
Sample ![]() |
cell line |
Variants | - |
Viral reference sequence | AAP41036.1 |
Drug/antibody/vaccine | - |
Transmissibility ![]() |
- |
Transmission mechanism | - |
Pathogenicity ![]() |
- |
Pathogenicity mechanism | - |
Immune escape mutation | - |
Immune escape mechanism | - |
RT-PCR primers probes | - |
Protein detail:
Protein name | ORF1ab polyprotein |
Uniprot protein ID | P0C6X7 |
Protein length | 7073 amino acids |
Protein description | The Orf1ab polyprotein contains the Orf1a polyprotein and 16 non-structural proteins. The Orf1ab polyprotein and its cleavage products carry out a wide range of activities associated with the viral replication, including ATP binding and breaking down of ADP and phosphate, cysteine-directed endopeptidase, leading to the formation of nonstructural proteins, such as exonuclease that produces ribose- 5-phosphate, methyltransferase for the synthesis of new nucleotides, RNA polymerase for the viral replication, RNA helicase for the removal of super twisting, as well as the regulation of the transcription through binding of zinc. However, the functions of the Orf1ab are the collective functions of the non-structural proteins encoded by the gene of Orf1ab |
Literature information:
Pubmed ID | 21390281 |
Clinical information | No |
Disease | - |
Published year | 2011 |
Journal | PLoS Computational Biology |
Title | Dynamically-Driven Inactivation of the Catalytic Machinery of the SARS 3C-Like Protease by the N214A Mutation on the Extra Domain |
Author | Jiahai Shi, Nanyu Han, Liangzhong Lim, Shixiong Lua, J. Sivaraman |
Evidence | Therefore, the N214A mutation appears to trigger the dramatic change of the enzyme dynamics in the context of the dimeric form which ultimately inactivates the catalytic machinery. |