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ubiquitin-like (Ubl) domain found in ubiquitin-related modifier 1 (Urm1) Urm1 acts as a sulfur carrier in the thiolation of eukaryotic tRNA via a mechanism that requires the formation of a thiocarboxylated Urm1, which is similar to that of prokaryotic sulfur carrier proteins such as ThiS and MoaD, containing the beta-grasp ubiquitin-like (Ubl) fold. Urm1 can be covalently conjugated to lysine residues of other proteins through a mechanism involving the E1-like protein Uba4. Urm1 is involved in yeast bioprocesses such as budding, nutrient sensing, high temperature sensitivity, antioxidant stress response and post-translation modification of the elongator subunit.
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Jiyao W et al.(2023). "The conserved domain database in 2023.",