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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311875   7 VKVEFGGGAELLFDGVKKHQVALPGQEePWDIRNLLVWIKKNLLKERPELFIQGDSVRPGILVLINDADWELLGELDYQL 86
Cdd:cd01764   1 ITVEFSGGLELLFGKQKKHEVELPSQK-PWTLRDLLAWIRDNLLKERPELFIQGDTVRPGILVLINDADWELLGELDYEL 79

                        90
                ....*....|....*
gi 21311875  87 QDQDSILFISTLHGG 101
Cdd:cd01764  80 QDGDRITFISTLHGG 94

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311875   7 VKVEFGGGAELLFDGVKKHQVALPGQEePWDIRNLLVWIKKNLLKERPELFIQGDSVRPGILVLINDADWELLGELDYQL 86
Cdd:cd01764   1 ITVEFSGGLELLFGKQKKHEVELPSQK-PWTLRDLLAWIRDNLLKERPELFIQGDTVRPGILVLINDADWELLGELDYEL 79

                        90
                ....*....|....*
gi 21311875  87 QDQDSILFISTLHGG 101
Cdd:cd01764  80 QDGDRITFISTLHGG 94

Ubiquitin-like protein [Posttranslational modification, protein turnover, chaperones];

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21311875  37 DIRNLLvwikKNLLKERpELFIQGDSVRPGILVLINDADWELlgeLDYQLQDQDSILFISTLHGG 101
Cdd:COG5131  25 ELRDVL----KKLDSEK-RLLSEDGKIRPGYLILINGVDWRL---LDTQLNDNDIVEIIPINHGG 81

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311875   7 VKVEFGGGAELLFDGVKKHQVALPGQEePWDIRNLLVWIKKNLLKERPELFIQGDSVRPGILVLINDADWELLGELDYQL 86
Cdd:cd01764   1 ITVEFSGGLELLFGKQKKHEVELPSQK-PWTLRDLLAWIRDNLLKERPELFIQGDTVRPGILVLINDADWELLGELDYEL 79

                        90
                ....*....|....*
gi 21311875  87 QDQDSILFISTLHGG 101
Cdd:cd01764  80 QDGDRITFISTLHGG 94

ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins; Ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins This family includes ThiS, MoaD, CysO, QbsE, and their homologs, which are structurally homologous to ubiquitin (Ub) and may function as the sulfide donor for the biosynthesis of thiamin, molybdopterin, cysteine, thioquinolobactin, and other sulfur-containing natural products. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. Like Ub, small sulfide carrier proteins in this family are adenylated at a diglycyl C-terminus by specific activating proteins. The adenylated C-terminus is subsequently converted to a thiocarboxylate, serving as the sulfide source. Those activating proteins are diverse and show little sequence similarity. This family also includes the small archaeal modifier protein (SAMP), including SAMP1, SAMP2 and SAMP3, which are Ub-like proteins that function as protein modifiers and are required for the production of sulfur-containing biomolecules in the archaeon Haloferax volcanii. SAMP1 and SAMP2 are involved in sulfur transfer during molybdenum cofactor biosynthesis and tRNA thiolation much like MoaD and Urm1, respectively. They can form covalent conjugates with their protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. SAMP2 also forms homo-conjugates through the intermolecular isopeptide bond between the C-terminal Gly and the Lys58 side chain, a feature that likely resembles polyubiquitination. SAMP3 conjugates are dependent on the Ub-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease HvJAMM1.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311875   7 VKVEFGGGAELLFDGVKKHQValpgqEEPWDIRNLLVWIKKNLLKERPELFIQGDsVRPGILVLINDADWELLgELDYQL 86
Cdd:cd17040   1 VKVRLFGALREAGAGEEEIEV-----EGGTTVRDLLDALSERYPGLFEALDEDGE-LRPFILVFVNGRDVRLD-DGLTPL 73

                        90
                ....*....|....*
gi 21311875  87 QDQDSILFISTLHGG 101
Cdd:cd17040  74 KDGDEVDILPPVAGG 88