GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
Cacao
| GO:2000966 | regulation of cell wall polysaccharide catabolic process | PMID:16618494 | ISS: Inferred from Sequence Similarity UniProtKB:A0A023Z1P7 | P | ||||
| This annotation made on page: NEIME:A0A0G4BQJ3 By: Jheins2 (group Team Green B) on 2016-04-11 04:42:05 CDT. | ||||||||
You must be logged in to challenge this annotation.
| Entry Type | Challenging User,Group | Time/Date | Challenge Reason | Points/Assessment | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Challenge | Nguye3jq, Team ContaminatorZ | 2016-04-04 15:45:03 CDT | Prior annotations have been made on this gene in Quick GO. If the annotation is a transfer annotation, then must be noted. If not then not necessary annotation. | None, yet. | ||||||||||||||||||
| Challenge | Jheins2, Team Green B | 2016-04-04 09:53:51 CDT | You're right as usual, I didn't pick the right GO term. The proper go term should be GO:2000966 and that's regulation of cell wall polysaccharide catabolic process. This protein degrades the cell wall, for what I would presume entering bacteria | None, yet. | ||||||||||||||||||
| Challenge | Amariam1, Team You can't B. cereus | 2016-03-29 12:48:41 CDT | The article has no reference to peptidoglycan turnover (refers to murein turnover once but the two are radically different), as your GO term suggests. In addition, the article compares crystal structures. From the abstract "crystal structures of MltA from Neisseria gonorrhoeae and Escherichia coli (NgMltA and EcMltA), which have only 21.5% sequence identity. Both proteins have two main domains separated by a deep groove. Domain 1 shows structural similarity with the so-called double-psi barrel family of proteins. Comparison of the two structures reveals substantial differences in the relative positions of domains 1 and 2 such that the active site groove in NgMltA is much wider and appears more able to accommodate peptidoglycan substrate than EcMltA, suggesting that domain closure occurs after substrate binding." Furthermore, the Aspect is listed as biological process as per GO term. I think you need to either change your GO term to one that codes for a Cellular component or change your article to support your biological process. | None, yet. | ||||||||||||||||||
| Private Assessment | Suzialeksander | 2016-06-17 13:10:26 CDT | You need to be an instructor to view these notes. | Unacceptable | ||||||||||||||||||
| Public Assessment | JimHu | 2016-05-02 12:27:40 CDT | This paper does not show the activity or biological role of the protein, but discusses the structure in terms of previously inferred activity. Look to the papers referenced in this one. | Requires Changes ✔ Protein ✗ Publication ✗ Go term | ||||||||||||||||||
| Public Assessment | DanielRenfro | 2016-04-11 16:42:05 CDT | This annotation has been flagged because it has been edited since last assessment
| Flagged | ||||||||||||||||||
| Public Assessment | DanielRenfro | 2016-04-11 09:13:43 CDT | This annotation has been flagged because it has been edited since last assessment
| Flagged | ||||||||||||||||||
| Public Assessment | DanielRenfro | 2016-04-11 09:13:23 CDT | This annotation has been flagged because it has been edited since last assessment
| Flagged | ||||||||||||||||||
| Public Assessment | DanielRenfro | 2016-04-11 09:10:23 CDT | This annotation has been flagged because it has been edited since last assessment
| Flagged |
