ID   URM1_DROGR              Reviewed;         104 AA.
AC   B4J272;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Ubiquitin-related modifier 1 homolog {ECO:0000255|HAMAP-Rule:MF_03048};
GN   Name=Urm1 {ECO:0000250|UniProtKB:Q7KU86}; ORFNames=GH16604;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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 MOCS3. The sulfur
CC       is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also
CC       acts as a ubiquitin-like protein (UBL) that is covalently conjugated
CC       via an isopeptide bond to lysine residues of target proteins such as
CC       Jafrac1, Ciao1, Eip71CD and GILT1. The thiocarboxylated form serves as
CC       substrate for conjugation and oxidative stress specifically induces the
CC       formation of UBL-protein conjugates. {ECO:0000255|HAMAP-Rule:MF_03048}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03048}.
CC   -!- SUBUNIT: Interacts with cer. {ECO:0000250|UniProtKB:Q7KU86}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03048}.
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 homolog,
CC       then thiocarboxylated (-COSH) via the rhodanese domain of the MOCS3
CC       homolog. {ECO:0000255|HAMAP-Rule:MF_03048}.
CC   -!- SIMILARITY: Belongs to the URM1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03048}.
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DR   EMBL; CH916366; EDV97023.1; -; Genomic_DNA.
DR   RefSeq; XP_001984675.1; XM_001984639.1.
DR   AlphaFoldDB; B4J272; -.
DR   SMR; B4J272; -.
DR   STRING; 7222.FBpp0150510; -.
DR   EnsemblMetazoa; FBtr0152018; FBpp0150510; FBgn0124075.
DR   GeneID; 6558782; -.
DR   KEGG; dgr:6558782; -.
DR   eggNOG; KOG4146; Eukaryota.
DR   HOGENOM; CLU_148208_0_1_1; -.
DR   InParanoid; B4J272; -.
DR   OMA; DYELQPN; -.
DR   OrthoDB; 1541629at2759; -.
DR   PhylomeDB; B4J272; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000001070; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; IEA:EnsemblMetazoa.
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; PTHR14986; 1.
DR   Pfam; PF09138; Urm1; 1.
DR   PIRSF; PIRSF037379; Ubiquitin-related_modifier_1; 1.
DR   SUPFAM; SSF54285; SSF54285; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isopeptide bond; Reference proteome; tRNA processing;
KW   Ubl conjugation pathway.
FT   CHAIN           1..104
FT                   /note="Ubiquitin-related modifier 1 homolog"
FT                   /id="PRO_0000367857"
FT   MOD_RES         104
FT                   /note="1-thioglycine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT   CROSSLNK        104
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
SQ   SEQUENCE   104 AA;  11675 MW;  B976744066BFFBE4 CRC64;
     MGSKETPDLK IILEFGAGAE LLFGNIKKRQ LSLNGAQKWT IAELLKWMHA NILTERAELF
     IQGDTVRPGI LVLINDTDWE LLGELEYELQ PNDNVLFIST LHGG