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Cacao
| GO:0019062 | virion attachment to host cell | PMID:19780551 | ECO:0000247 | UniProtKB:Q9T1V4 | Biological Process | Tail spikes in Escherichia phage P2 (Bacteriophage P2) is composed of gpV. In Fig 9 B, P2 gpV gets compared to Mu gp45. The results indicate that P2 gpV has typical features of phage tail spikes, such as a protease-sensitive N-terminal domain, a host-binding C-terminal domain, and a trimeric structure. This shows that gpV is a receptor-binding protein involved in the second step of phage adsorption. | complete | |
| This annotation made on page: BPP2:SPIKE By: MAntonescu (group Death by Gene) on 2019-03-12 20:34:16 CDT. | ||||||||
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| Entry Type | Challenging User,Group | Time/Date | Challenge Reason | Points/Assessment |
|---|---|---|---|---|
| Public Assessment | Ivanerill | 2019-03-15 12:05:05 CDT | Figure 9B shows a sequence alignment between P2 phage gpV and Mu phage gp45. The authors admit that 45% sequence identity is not significant and they then speculate that this might tell them something about the function of gpV. But in no way do they state that from Figure 9b one can conclude that BPP2:SPIKE is involved in GO:0019062, which is a biological process (their speculation is mostly restricted to molecular function). | Unacceptable ✔ Protein ✔ Publication ✗ Go term ✗ Evidence ✗ Notes |
