ID   URM1_CANGA              Reviewed;          98 AA.
AC   Q6FWQ3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Ubiquitin-related modifier 1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN   Name=URM1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN   OrderedLocusNames=CAGL0C03784g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 homolog
CC       UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of
CC       mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is
CC       required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL)
CC       that is covalently conjugated via an isopeptide bond to lysine residues
CC       of target proteins such as AHP1. 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   -!- 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 UBA4, then
CC       thiocarboxylated (-COSH) via the rhodanese domain of UBA4.
CC       {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; CR380949; CAG58247.1; -; Genomic_DNA.
DR   RefSeq; XP_445341.1; XM_445341.1.
DR   AlphaFoldDB; Q6FWQ3; -.
DR   SMR; Q6FWQ3; -.
DR   STRING; 5478.XP_445341.1; -.
DR   EnsemblFungi; CAG58247; CAG58247; CAGL0C03784g.
DR   GeneID; 2886829; -.
DR   KEGG; cgr:CAGL0C03784g; -.
DR   CGD; CAL0127536; CAGL0C03784g.
DR   VEuPathDB; FungiDB:CAGL0C03784g; -.
DR   eggNOG; KOG4146; Eukaryota.
DR   HOGENOM; CLU_148208_0_0_1; -.
DR   InParanoid; Q6FWQ3; -.
DR   OMA; SLIHFMA; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000002428; Chromosome C.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblFungi.
DR   GO; GO:0031386; F:protein tag; IEA:EnsemblFungi.
DR   GO; GO:0097163; F:sulfur carrier activity; IEA:EnsemblFungi.
DR   GO; GO:0007114; P:cell budding; IEA:EnsemblFungi.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR   GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:EnsemblFungi.
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..98
FT                   /note="Ubiquitin-related modifier 1"
FT                   /id="PRO_0000367878"
FT   MOD_RES         98
FT                   /note="1-thioglycine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT   CROSSLNK        98
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
SQ   SEQUENCE   98 AA;  11125 MW;  FB591E7DA6F7A209 CRC64;
     MVKVRVEFLG GLDVIVNKQR VYDLDVPSQV ENVGDLIDYI IENLITNKKD VEVFIENDSI
     RPGIITLIND TDWELENEKE YVIEDGDVIS FTSTLHGG