Mutation detail:
| Mutation site | L2430F |
| Virus | SARS-CoV |
Mutation level  |
Amino acid level |
| Gene/protein/region type | ORF1ab(NSP3) |
| Gene ID | 1489680 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | AY291315.1 |
| 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 | 18362400 |
| Clinical information | No |
| Disease | - |
| Published year | 2008 |
| Journal | Japanese Journal Of Infectious Diseases |
| Title | Reduced incorporation of SARS-CoV spike protein into viral particles due to amino acid substitutions within the receptor binding domain |
| Author | Shu-Ming Li, Gui-Mei Li, Shota Nakamura, Kazuyoshi Ikuta, Takaaki Nakaya |
| Evidence | Table1 |