PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12369927-2	2001	Similar to other nucleotide binding proteins, dUTPase also consists of a sequence motif rich in glycine residues known as P-loop motif.	Glycine	96-103	Deoxyuridine triphosphatase	Drosophila melanogaster	46-53	
30902068-8	2019	The resulting Dr-dUTPase had the leading peptide Gly-Ser-His- originating from the vector at the amino terminus, and a mutation, Arg66Lys, to remove the internal thrombin site.	Glycine	49-52	Deoxyuridine triphosphatase	Drosophila melanogaster	17-24	
12369927-5	2001	One of the main reasons for this limited information is the lack of the three-dimensional structure of a dUTPase enzyme with an ordered Gly-rich P-loop motif with a bound substrate and Mg(2+) ion.	Glycine	136-139	Deoxyuridine triphosphatase	Drosophila melanogaster	105-112	
12369927-6	2001	This review presents an insight into the role of Gly-rich P-loop motif in the function of dUTPase as revealed from the crystal structure.	Glycine	49-52	Deoxyuridine triphosphatase	Drosophila melanogaster	90-97	
12369927-7	2001	The analysis reveals the Gly-rich P-loop motif of dUTPase to be the longest in terms of its amino-acid composition as compared to other nucleotide binding proteins and exhibit a high-degree of sequence conservation among spectrum of species.	Glycine	25-28	Deoxyuridine triphosphatase	Drosophila melanogaster	50-57	
7950368-4	1994	The purified dUTPase has two additional vector-encoded residues at the amino terminus (gly-ser), but they have no apparent effect on the activity of the enzyme since the recombinant dUTPase has catalytic properties similar to those reported for dUTPase purified from human cells (32.3 U/mg, kcat = 25 s-1, Km = 2.6 microM).	Glycine	87-90	Deoxyuridine triphosphatase	Drosophila melanogaster	13-20	
9261872-9	1997	I conclude that the glycine-rich motif is functionally relevant for E. coli dUTPase.	Glycine	20-27	Deoxyuridine triphosphatase	Drosophila melanogaster	76-83