Mutation detail:
| Mutation site | T153I |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | ORF1ab(helicase) |
| Gene ID | 43740578 |
| Country | Indonesia |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | NC_045512.2 |
| 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 | P0DTC1 |
| Protein length | 7096 amino acids |
| Protein description | ORF1ab, the largest gene, contains overlapping open reading frames that encode polyproteins PP1ab and PP1a. The polyproteins are cleaved to yield 16 nonstructural proteins, NSP1-16. Production of the longer (PP1ab) or shorter protein (PP1a) depends on a -1 ribosomal frameshifting event. The proteins, based on similarity to other coronaviruses, include the papain-like proteinase protein (NSP3), 3C-like proteinase (NSP5), RNA-dependent RNA polymerase (NSP12, RdRp), helicase (NSP13, HEL), endoRNAse (NSP15), 2'-O-Ribose-Methyltransferase (NSP16) and other nonstructural proteins. SARS-CoV-2 nonstructural proteins are responsible for viral transcription, replication, proteolytic processing, suppression of host immune responses and suppression of host gene expression. The RNA-dependent RNA polymerase is a target of antiviral therapies. |
Literature information:
| Pubmed ID | 34074255 |
| Clinical information | Yes |
| Disease | - |
| Published year | 2021 |
| Journal | BMC Medical Genomics |
| Title | Molecular epidemiology of SARS-CoV-2 isolated from COVID-19 family clusters |
| Author | Gunadi,Hendra Wibawa,Mohamad Saifudin Hakim,Marcellus,Ika Trisnawati |
| Evidence | Ninety-four SNPs were detected throughout the ORP of the SARS-CoV-2 virus samples with 60% (54/94) of the nucleic acid changes resulting in amino acid substitutions (missense mutations) (Table1,1, detailed in Additional file 1: Table S1). |