Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein] ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-73 binds ATP and competes with ATP-binding at Arg-209, thereby preventing adenylyltransferase activity. Activation dissociates ATP-binding from Glu-73, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain. Homodimer. Defined as class II fido-domain containing proteins, in which the inhibitory helix is present at the N-terminus of the Fido domain.