ID   A0A154PAJ9_DUFNO        Unreviewed;        91 AA.
AC   A0A154PAJ9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   02-APR-2025, entry version 32.
DE   RecName: Full=Ubiquitin-related modifier 1 homolog {ECO:0000256|HAMAP-Rule:MF_03048};
GN   ORFNames=WN55_09298 {ECO:0000313|EMBL:KZC08394.1};
OS   Dufourea novaeangliae (Sweat bee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Halictidae; Rophitinae; Dufourea.
OX   NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC08394.1, ECO:0000313|Proteomes:UP000076502};
RN   [1] {ECO:0000313|EMBL:KZC08394.1, ECO:0000313|Proteomes:UP000076502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0120121106 {ECO:0000313|EMBL:KZC08394.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KZC08394.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Dufourea novaeangliae.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a sulfur carrier required for 2-thiolation of
CC       mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu)
CC       and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by
CC       being thiocarboxylated (-COSH) at its C-terminus by the MOCS3/UBA4
CC       homolog. The sulfur is then transferred to tRNA to form 2-thiolation of
CC       mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is
CC       covalently conjugated via an isopeptide bond to lysine residues of
CC       target proteins. The thiocarboxylated form serves as substrate for
CC       conjugation and oxidative stress specifically induces the formation of
CC       UBL-protein conjugates. {ECO:0000256|HAMAP-Rule:MF_03048}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03048,
CC       ECO:0000256|RuleBase:RU361182}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03048,
CC       ECO:0000256|RuleBase:RU361182}.
CC   -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC       adenylated (-COAMP) via the hesA/moeB/thiF part of the MOCS3/UBA4
CC       homolog, then thiocarboxylated (-COSH) via the rhodanese domain of the
CC       MOCS3/UBA4 homolog. {ECO:0000256|HAMAP-Rule:MF_03048}.
CC   -!- SIMILARITY: Belongs to the URM1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03048, ECO:0000256|RuleBase:RU361182}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03048}.
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DR   EMBL; KQ434846; KZC08394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A154PAJ9; -.
DR   STRING; 178035.A0A154PAJ9; -.
DR   EnsemblMetazoa; XM_015574558.1; XP_015430044.1; LOC107186644.
DR   OrthoDB; 10248987at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000076502; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01764; Ubl_Urm1; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   HAMAP; MF_03048; Urm1; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR   InterPro; IPR015221; Urm1.
DR   PANTHER; PTHR14986; RURM1 PROTEIN; 1.
DR   Pfam; PF09138; Urm1; 1.
DR   SUPFAM; SSF54285; MoaD/ThiS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03048};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499, ECO:0000256|HAMAP-
KW   Rule:MF_03048}; Reference proteome {ECO:0000313|Proteomes:UP000076502};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_03048};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, ECO:0000256|HAMAP-
KW   Rule:MF_03048}.
SQ   SEQUENCE   91 AA;  10527 MW;  E6D97012D4408DD3 CRC64;
     MSSENSETPL TIEFGGGAEL LFDKKKKYEV NLPGNDWTIQ KLLFWIKDNL LKERPELFLQ
     GETVRPGILV LVNDTDWELL VSTLFIFEII K
//