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User:Khana25

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Phage Hunters Spring 2016

My Annotations

StatusPageDate/TimeGO Term (Aspect)ReferenceEvidenceNotesLinks
updatedbyinstructorBPA51:A8ASU22016-04-22 10:38:45 CDTGO:0098024 virus tail, fiber (C)PMID:24673724ECO:0000314 direct assay evidence used in manual assertion

Figure 7. Panel O, shows the gp108 tail fiber in electron microscopy, at the appropriate location for the function of a tail fiber. Specifically, the immunogold particles binding near the baseplate, which is where you would expect to see the tail fiber.

challenge
updatedbyinstructor9CAUD:S4U6W52016-04-25 10:33:56 CDTGO:0019062 virion attachment to host cell (P)GO_REF:0000100ECO:0000247 sequence alignment evidence used in manual assertion

Blastp results for transfer annotation yield an E-value of 0.0, Identity similarity of 98.1%, and a Query Coverage of 100%, as evidence for sequence similarity

challenge
updatedbyinstructor9CAUD:A0A059T8532016-04-25 10:47:19 CDTGO:0019062 virion attachment to host cell (P)GO_REF:0000100ECO:0000247 sequence alignment evidence used in manual assertion

Blastp results for transfer annotation yield an E-value of 0.0, Identity similarity of 98.1%, and a Query Coverage of 100%, as evidence for sequence similarity.

challenge
updatedbyinstructor9CAUD:A0A059T6U22016-04-27 01:54:10 CDTGO:0019062 virion attachment to host cell (P)GO_REF:0000100ECO:0000247 sequence alignment evidence used in manual assertion

Blastp results for transfer annotation yield an E-value of 0.0, Identity similarity of 97.7%, and a Query Coverage of 100%, as evidence for sequence similarity.

challenge
updatedbyinstructor9CAUD:A0A059T8Q02016-04-27 02:00:44 CDTGO:0019062 virion attachment to host cell (P)GO_REF:0000100ECO:0000247 sequence alignment evidence used in manual assertion

Blastp results for transfer annotation yield an E-value of 0.0, Identity similarity of 97.7%, and a Query Coverage of 100%, as evidence for sequence similarity.

challenge
updatedbyinstructor9CAUD:A0A060AKZ12016-04-27 02:14:14 CDTGO:0019062 virion attachment to host cell (P)GO_REF:0000100ECO:0000247 sequence alignment evidence used in manual assertion

Blastp results for transfer annotation yield an E-value of 0.0, Identity similarity of 97.0%, and a Query Coverage of 100%, as evidence for sequence similarity.

challenge
updatedbyinstructor9CAUD:A0A068CCS02016-04-27 02:29:28 CDTGO:0019062 virion attachment to host cell (P)GO_REF:0000100ECO:0000247 sequence alignment evidence used in manual assertion

Blastp results for transfer annotation yield an E-value of 0.0, Identity similarity of 97.2%, and a Query Coverage of 100%, as evidence for sequence similarity.

challenge
updatedbyinstructorBPA51:A8ASU22016-05-02 09:26:44 CDTGO:0019062 virion attachment to host cell (P)PMID:24673724ECO:0000314 direct assay evidence used in manual assertion

Figure 2 shows how the antibody of gp108 tail fiber protein inhibits adsorption of bacteriophage A511 to the WSLC 3009 host cell. The bars on the graphs above the label WSLC3009 + gp108 show a significant decrease in efficiency in plating and adorption. This indicates the antibody gp108's ability to block the binding of the A511 to the host cell.

challenge
unacceptable9CAUD:Q8LTE62016-05-16 11:56:38 CDTGO:0009253 peptidoglycan catabolic process (P)PMID:18662316ECO:0000247 sequence alignment evidence used in manual assertion

Figure 1a in the literature shows a schematic representation of PlyG and PlyL, and the umbers of amino acid residues involved in catalysis are respectively, 233 and 234, indicating a high sequence similarity and low E-value, allowing assumption of function similarity to the endolysin PlyL. In addition, figure 2a, shows a sequence alignment of PlyG and PlyL and PlyG has a high degree of sequence similarity to PlyL. There are only 10 amino acid residue differences within the N-terminal regions of PlyG and PlyL, while 30 amino acid residues are different within their C-terminal regions. Therefore, it seems likely that the N-terminal region of PlyG also has similar characteristics.

challenge
updatedbyinstructor9CAUD:Q8LTE62016-05-16 17:17:28 CDTGO:0051672 catabolism by organism of cell wall peptidoglycan in other organism (P)PMID:18662316ECO:0000315 mutant phenotype evidence used in manual assertion

Figure 2d. in the literature compares Lytic activities of wild-type PlyG and its C-terminal deletion mutant. Catalytic activity was examined by colony-forming assay, and the control, PlyGB, was set to 100%. As shown in the figure, deletion of the C-terminal region completely abolished the lytic ability of PlyG, with the colony forming units of the C-terminal deletion mutant at a very high percentage, versus the normal wild type PlyG, which yielded a very low colony forming unit percentage. This indicates that the cell-wall-binding domain of PlyG is essential for its catalytic activity, and that addition of PlyG restricts colonies of bacteria from forming, characterizing it as an endolysin with peptidoglycan catabolic process and cleavage.

challenge

acceptable:0
unacceptable:1
requires_changes:0
flagged:0

Annotations challenged by Khana25

StatusAuthor,GroupPageGO Term (Aspect)ReferenceEvidenceLinksPage history
unacceptableE63,
Team Blue A
9CAUD:A0A0K2D000GO:0004146 - dihydrofolate reductase activity (F)PMID:10731419ECO:0000250 sequence similarity evidence used in manual assertionchallengeC: 5
unacceptableMnguy1,
Team Blue B
BPT7:DPOLGO:0004527 - exonuclease activity (F)2703498:2703498ECO:0000315 mutant phenotype evidence used in manual assertionchallengeC: 5
updatedbyinstructorBarlowrm,
Team TRUMP2016
BACSU:TYSY1GO:0004799 - thymidylate synthase activity (F)PMID:9778348ECO:0000314 direct assay evidence used in manual assertionchallengeC: 4
unacceptableHeatheca,
Team ContaminatorZ
9CAUD:A0A024B0X2GO:0098020 - obsolete virus tail, minor subunit (C)PMID:22923442ECO:0000314 direct assay evidence used in manual assertionchallengeC: 5
updatedbyinstructorDalton.Fellows,
Team Tiger2
BPMD2:VG65GO:0008310 - single-stranded DNA 3'-5' DNA exonuclease activity (F)PMID:19028888ECO:0000314 direct assay evidence used in manual assertionchallengeC: 1

0 annotations fixed by Khana25

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