| Challenge | AHutchison,
Team Purple A 2018 | 2018-03-20 22:29:21 CDT | I agree with the majority of your annotation. The Go number and IDA part annotation look great. However I do not think the information from table 1 is necessary to support your IDA claims. I would consider adding more to your notes, especially including parts C and D of figure 2 to help support the annotation. Finally, is the annotation considering a cellular component or is it more of a biological function? Overall, I think this annotation was pretty solid, it just needs a few minor changes.
| None, yet. |
Public
Assessment | Ivanerill | 2018-04-15 15:05:22 CDT | Your annotation is to gp16. The paper mostly talks about gp17 activity, and how gp16 modulates it. Either change the GO term to reflect that, or request to change the protein.
| Requires Changes
✗ Protein
✔ Publication
✔ Qualifier
✗ Go term
✔ Evidence
✔ With/From
✔ Notes
✔ Unique/Original
|
Public
Assessment | DanielRenfro | 2018-03-26 14:40:30 CDT | This annotation has been flagged because it has been edited since last assessment
| Qualifier |
GO ID |
GO term name |
Reference |
Evidence Code |
with/from |
Aspect |
Notes |
Status
|
|
GO:0032781 |
ATPase activity |
PMID:21127059 |
IDA: Inferred from Direct Assay |
|
F |
A packaging machine is assembled at the portal vortex of empty proheads, where a large terminase (gp17) cuts the concatemeric genome before assembly. The T4 large terminase is made of 2 domains, an N-terminal ATPase domain and C-terminal nuclease domain. gp17 exhibits weak ATPase activity, but is stimulated more than 50 fold by gp16 (small terminase). Figure 2A with lane RB49 gp17 shows similar weak ATPase activity to the T4 large terminase. The lane containing RB49 gp17+gp16 has a 56 fold increase of ATPase stimulation, similar to T4. An In vivo nuclease assay also showed strong nuclease activity in RB49 similar to T4 gp17 due to broad smears of fragmented DNA (Figure 2B). There’s specificity with large and small terminase interactions, as when T4 gp17 mixed with gp16 from different phages, showed high ATPase activity only with its own gp16. Stimulation of T4 gp17 ATPase by RB49 gp16 was only 14% of T4 gp17-gp16 interaction (Figure 3A) |
complete
CACAO 13121
| on BPR69:Q7Y4X1
| Flagged
|
Public
Assessment | DanielRenfro | 2018-03-25 19:34:58 CDT | This annotation has been flagged because it has been edited since last assessment
| Qualifier |
GO ID |
GO term name |
Reference |
Evidence Code |
with/from |
Aspect |
Notes |
Status
|
|
GO:0016887 |
ATPase activity |
PMID:21127059 |
IDA: Inferred from Direct Assay |
|
F |
A packaging machine is assembled at the portal vortex of empty proheads, where a large terminase (gp17) cuts the concatemeric genome before assembly. The T4 large terminase is made of 2 domains, an N-terminal ATPase domain and C-terminal nuclease domain. gp17 exhibits weak ATPase activity, but is stimulated more than 50 fold by gp16 (small terminase). Figure 2A with lane RB49 gp17 shows similar weak ATPase activity to the T4 large terminase. The lane containing RB49 gp17+gp16 has a 56 fold increase of ATPase stimulation, similar to T4. An In vivo nuclease assay also showed strong nuclease activity in RB49 similar to T4 gp17 due to broad smears of fragmented DNA (Figure 2B). There’s specificity with large and small terminase interactions, as when T4 gp17 mixed with gp16 from different phages, showed high ATPase activity only with its own gp16. Stimulation of T4 gp17 ATPase by RB49 gp16 was only 14% of T4 gp17-gp16 interaction (Figure 3A) |
complete
CACAO 13121
| on BPR69:Q7Y4X1
| Flagged
|
Public
Assessment | DanielRenfro | 2018-03-22 15:16:54 CDT | This annotation has been flagged because it has been edited since last assessment
| Qualifier |
GO ID |
GO term name |
Reference |
Evidence Code |
with/from |
Aspect |
Notes |
Status
|
|
GO:0016887 |
ATPase activity |
PMID:21127059 |
IDA: Inferred from Direct Assay |
|
F |
Small and large terminase sequences from coliphage RB69 were analyzed for sequence identity with T4 terminases and showed 80-100% similarity (Table 1). A packaging machine is assembled at the portal vortex of empty proheads, where a large terminase (gp17) cuts the concatemeric genome before assembly. The T4 large terminase is made of 2 domains, an N-terminal ATPase domain and C-terminal nuclease domain. gp17 exhibits weak ATPase activity, but is stimulated more than 50 fold by gp16 (small terminase). Figure 2A with lane RB49 gp17 shows similar weak ATPase activity to the T4 large terminase. The lane containing RB49 gp17+gp16 has a 56 fold increase of ATPase stimulation, similar to T4. An In vivo nuclease assay also showed strong nuclease activity in RB69 similar to T4 gp17 due to broad smears of fragmented DNA (Figure 2B). There’s specificity with large and small terminase interactions, as when T4 gp17 mixed with gp16 from different phages, showed high ATPase activity only with its own gp16. Stimulation of T4 gp17 ATPase by RB69 gp16 was only 14% of T4 gp17-gp16 interaction (Figure 3A) |
complete
CACAO 13121
| on BPR69:Q7Y4X1
| Flagged
|
Public
Assessment | DanielRenfro | 2018-03-22 15:12:16 CDT | This annotation has been flagged because it has been edited since last assessment
| Qualifier |
GO ID |
GO term name |
Reference |
Evidence Code |
with/from |
Aspect |
Notes |
Status
|
|
GO:0016887 |
viral terminase, small subunit |
PMID:21127059 |
IDA: Inferred from Direct Assay |
|
C |
Small and large terminase sequences from coliphage RB69 were analyzed for sequence identity with T4 terminases and showed 80-100% similarity (Table 1). A packaging machine is assembled at the portal vortex of empty proheads, where a large terminase (gp17) cuts the concatemeric genome before assembly. The T4 large terminase is made of 2 domains, an N-terminal ATPase domain and C-terminal nuclease domain. gp17 exhibits weak ATPase activity, but is stimulated more than 50 fold by gp16 (small terminase). Figure 2A with lane RB49 gp17 shows similar weak ATPase activity to the T4 large terminase. The lane containing RB49 gp17+gp16 has a 56 fold increase of ATPase stimulation, similar to T4. An In vivo nuclease assay also showed strong nuclease activity in RB69 similar to T4 gp17 due to broad smears of fragmented DNA (Figure 2B). There’s specificity with large and small terminase interactions, as when T4 gp17 mixed with gp16 from different phages, showed high ATPase activity only with its own gp16. Stimulation of T4 gp17 ATPase by RB69 gp16 was only 14% of T4 gp17-gp16 interaction (Figure 3A) |
complete
CACAO 13121
| on BPR69:Q7Y4X1
| Flagged
|
