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Cacao

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GO:0003796lysozyme activityPMID:21816821IDA: Inferred from Direct Assay F
This annotation made on page: BACAN:Q81YZ2
By: Otihso (group Team ZIRTS) on 2017-04-17 10:54:09 CDT.



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Entry TypeChallenging User,GroupTime/DateChallenge ReasonPoints/Assessment
Private
Assessment
Suzialeksander2017-06-26 16:01:59 CDTYou need to be an instructor to view these notes.Unacceptable
Protein
Evidence
Notes
Public
Assessment
DanielRenfro2017-05-12 20:49:17 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:0003796 lysozyme activity PMID:21816821 ISS: Inferred from Sequence Similarity F In Figure 2A, both XylA and PlyL’s structures were being compared which indicated that the two of these proteins are amidase lysins. In this particular figure(2A), their functions were being tested based on their ability to lyse B. Subtilis. They found that the catalytic domain of PlyL which was indicated in the paper by “PlyL CAT” had homologous lysing abilities to the entirety of XylA. Missing: with/from
CACAO 12646
on BACAN:Q81YZ2
Flagged
Public
Assessment
DanielRenfro2017-05-07 13:24:05 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:0003796 lysozyme activity PMID:21816821 IDA: Inferred from Direct Assay F When going through this paper, one can see that XylA is an endolysin from a prophage of the B. subtilis genome. In Figure 3B, the sequence alignment between XylA and PlyL is extremely similar. Because it is known that XylA is an endolysin and there are many similarities to that of PlyL their sequencing, PlyL is also an endolysin. The Catalytic domain of XylA has a 45% nucleotide identity with PlyL. The red boxes show XlyA contains catalytic and substrate recognition residues identical to PlyL. The asterisks indicate base pair identity between XlyA and PlyL sequences. The colons indicate base pair similarity between XylA and PlyL. The high similarity and identity within the sequence alignment and secondary structure assignments of XylA and PlyL support the lysozyme function of XylA. complete
CACAO 12646
on BACAN:Q81YZ2
Flagged
Public
Assessment
AAJohnson2017-04-19 09:24:34 CDT

You are combining sequence alignment, molecular modeling and crystallography statistics into one annotation. Let's look at those three parts. Sequence alignment: "The Catalytic domain of XylA has a 45% identity with PlyL." What kind of identity is this? What/where is the evidence? How does this support the GO Term you chose?

Molecular modeling: "There is also a very large similarity in their overall backbones." " In Figure 2B the presence of a very similar construction in both XylA CAT(blue) and PlyL CAT(green) is demonstrated." Can you put 'very large similarity' into more quantitative or scientific words? What kind of similarity is this, and how do you know? What kind of experiment was done in Figure 2B? What/where is the evidence? How does this support the GO Term you chose?

Crystallography statistics: "Table 2 displays the similarities between XylA CAT, XylA CAT+5K, And PlyBa04 CAT. Both the catalytic domain of XylA and PlyL have high lysing activity. The authors of this paper used experimental evidence found in Table 2 to illustrate the similarities in the charge as well as makeup of the catalytic domains of XylA CAT, XylA CAT+5K, And PlyBa04 CAT respectively.The net charge is directly related to the lytic activity and crystal structure found in Table 2." How do we know net charge is directly related to lytic activity (this relates to your GO Term)? How do we know the catalytic domains have high lysing activity? I'm not sure Table 2 supports your GO Term but you have some interesting statements here that sound like they have potential if you can improve your description.

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Notes