User:Jheins2

My Annotations

Status	Page	Date/Time	GO Term (Aspect)	Reference	Evidence	Notes	Links
unacceptable	9CAUD:A0A0K2D0F3	2016-03-28 11:17:09 CDT	GO:0004799 thymidylate synthase activity (F)	PMID:16615077	ECO:0000250 sequence similarity evidence used in manual assertion	"The R166Q mutant was crystallized in the presence of dUMP and a structure determined to 2.9 A resolution, but neither the ligand nor the sulfate from the crystallization buffer was found in the active site." meaning that this protein has a TS sight and if this site was mutated from a R to a Q at the 166 peptide, the site was inactive. This has a similar sequence from the TS in E.coli.	challenge
unacceptable	9CAUD:A0A0K2CZX2	2016-04-11 04:44:14 CDT	GO:2000966 peptidoglycan turnover (P)	PMID:16618494	ECO:0000250 sequence similarity evidence used in manual assertion	MltA is a lytic transglycosylase of Gram-negative bacteria that cleaves the beta-1,4 glycosidic linkages between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan. Since these sites have determined the crystal structures of MltA from Neisseria gonorrhoeae and Escherichia coli (NgMltA and EcMltA), which have only 21.5% sequence identity but have 2 main domains separated by a deep grove pointing that they are both MltA proteins, we can conclude that this protein in Bacillus phage TsarBomba is also a MltA protein with the same protein function.	challenge
unacceptable	ECOLX:A0A023Z1P7	2016-04-11 04:40:26 CDT	GO:2000966 regulation of cell wall polysaccharide catabolic process (P)	PMID:16615077	ECO:0000250 sequence similarity evidence used in manual assertion	MltA is a lytic transglycosylase of Gram-negative bacteria that cleaves the beta-1,4 glycosidic linkages between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan. We have determined the crystal structures of MltA from Neisseria gonorrhoeae and Escherichia coli (NgMltA and EcMltA), which have only 21.5% sequence identity but have 2 main domains separated by a deep grove pointing that they are both MltA proteins.	challenge
unacceptable	NEIME:A0A0G4BQJ3	2016-04-11 04:42:05 CDT	GO:2000966 regulation of cell wall polysaccharide catabolic process (MltA is a lytic transglycosylase of Gram-negative bacteria that cleaves the beta-1,4 glycosidic linkages between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan. We have determined the crystal structures of MltA from Neisseria gonorrhoeae and Escherichia coli (NgMltA and EcMltA), which have only 21.5% sequence identity but have 2 main domains separated by a deep grove pointing that they are both MltA proteins.)	PMID:16618494	ISS: Inferred from Sequence Similarity UniProtKB:A0A023Z1P7		challenge
unacceptable	ECODH:AAEA	2016-04-11 05:42:09 CDT	GO:0004514 NAD biosynthetic process (P)	PMID:8561507	ECO:0000314 direct assay evidence used in manual assertion	The nadC gene from Escherichia coli was isolated and sequenced. The gene was then cloned into an expression vector and, following transformation, the resulting bacteria were able to produce quinolinate phosphoribosyl transferase as about 2% of the soluble protein. The enzyme was purified in five steps leading to a homogeneous preparation. The enzyme reaction shows an ordered binding mechanism where the magnesium ion complex of 5-phosphoribosyl-1-pyrophosphate binds first followed by quinolinic acid. The products are pyrophosphate, CO2, and nicotinate mononucleotide.	challenge
unacceptable	9CAUD:A0A024B3P4	2016-04-11 05:43:39 CDT	GO:0004514 nicotinate-nucleotide diphosphorylase (carboxylating) activity (F)	PMID:8561507	ECO:0000250 sequence similarity evidence used in manual assertion	Sequence similarity with protein typically expressed in E. coli that is known to have this activity. "The enzyme reaction shows an ordered binding mechanism where the magnesium ion complex of 5-phosphoribosyl-1-pyrophosphate binds first followed by quinolinic acid. The products are pyrophosphate, CO2, and nicotinate mononucleotide."	challenge

acceptable:0
unacceptable:6
requires_changes:0
flagged:0

Annotations challenged by Jheins2

Status	Author,Group	Page	GO Term (Aspect)	Reference	Evidence	Links	Page history
unacceptable	Amariam1, Team You can't B. cereus	9CAUD:A0A0K2D089	GO:0046798 - viral portal complex (C)	PMID:18567664	ECO:0000250 sequence similarity evidence used in manual assertion	challenge	C: 3
unacceptable	Mnguy1, Team Blue B	9CAUD:A0A0K2D089	GO:0046798 - viral portal complex (C)	PMID:26616586	ECO:0000315 mutant phenotype evidence used in manual assertion	challenge	C: 3
unacceptable	Mnguy1, Team Blue B	9CAUD:A0A0K2D020	GO:0004527 - exonuclease activity (F)	PMID:2703498	ECO:0000315 mutant phenotype evidence used in manual assertion	challenge	C: 5
unacceptable	Mnguy1, Team Blue B	9CAUD:A0A0K2D0H8	GO:0006508 - proteolysis (P)	PMID:23688818	ECO:0000315 mutant phenotype evidence used in manual assertion	challenge	C: 4
unacceptable	Di46616, Team Red A	9CAUD:A0A0K2CZS7	GO:0016987 - sigma factor activity (F)	PMID:11274153	ECO:0000315 mutant phenotype evidence used in manual assertion	challenge	C: 2
unacceptable	Shireen2, Team Red A	9CAUD:A0A0K2D0I8	GO:0004309 - exopolyphosphatase activity (F)	PMID:24275100	ECO:0000315 mutant phenotype evidence used in manual assertion	challenge	C: 3
unacceptable	Jheins2, Team Green B	NEIME:A0A0G4BQJ3	GO:2000966 - regulation of cell wall polysaccharide catabolic process (MltA is a lytic transglycosylase of Gram-negative bacteria that cleaves the beta-1,4 glycosidic linkages between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan. We have determined the crystal structures of MltA from Neisseria gonorrhoeae and Escherichia coli (NgMltA and EcMltA), which have only 21.5% sequence identity but have 2 main domains separated by a deep grove pointing that they are both MltA proteins.)	PMID:16618494	ISS: Inferred from Sequence Similarity UniProtKB:A0A023Z1P7	challenge	C: 3

0 annotations fixed by Jheins2

What do the icons mean in the status column?