The conserved domains of our query protein, which can be directly linked from our original BLAST result page, are P-loop containing Nucleoside Triphosphate Hydrolases (P-loop NTPases) superfamily and Type 1 glutamine amidotransferase (GATase1)-like superfamily domains.

Structure of P-loop NTPase

P-loop NTPase is a superfamily conserved domain consisting of a nucleotide phosphate-binding motif, also known as Walker A motif, and Walker B motif.  Walker A motif typically bind to ATP or GTP while Walker B typically bind to Mg2+ cation. P-loop NTPase can be classified into 2 classes: kinase-GTPase class and additional strand catalytic E (ASCE) class. Kinase-GTPase function is to hydrolyse GTP and in turn regulate cellular processes. ASCE, like its name suggest, is in charge of binding specific residues or substrates.

Structure of GATase-1-like superfamily domain.

GATase-1-like is a superfamily conserved domain consisting beta strands and alpha helixes. Cys residues can be found between these and are crucial for the catalysis of glutamine. Upon binding to glutamine, the ammonia from glutamine will be transferred to an acceptor substrate, which allows Cys to form a Cys-His-Glu triad in the active site for catalytic action. Due to its catalytic function, this superfamily conserved domain can be found in a lot of enzymes, such as transferases and synthases.