ID   URM1_YEAS1              Reviewed;          99 AA.
AC   B3LTL7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Ubiquitin-related modifier 1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN   Name=URM1 {ECO:0000255|HAMAP-Rule:MF_03048}; ORFNames=SCRG_05187;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) 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 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   -!- SUBUNIT: Homodimer; homodimerization may provide an autoprotection to
CC       the highly active C-terminal residue before attacking its substrates.
CC       Interacts with NCS2 and NCS6. Forms a conjugate with the target protein
CC       AHP1. {ECO:0000255|HAMAP-Rule:MF_03048}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03048}.
CC       Nucleus {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; CH408055; EDV09498.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LTL7; -.
DR   BMRB; B3LTL7; -.
DR   SMR; B3LTL7; -.
DR   EnsemblFungi; EDV09498; EDV09498; SCRG_05187.
DR   HOGENOM; CLU_148208_0_0_1; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; Nucleus; tRNA processing;
KW   Ubl conjugation pathway.
FT   CHAIN           1..99
FT                   /note="Ubiquitin-related modifier 1"
FT                   /id="PRO_0000367891"
FT   MOD_RES         99
FT                   /note="1-thioglycine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT   CROSSLNK        99
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
SQ   SEQUENCE   99 AA;  11028 MW;  A15356D6C1B6B5BC CRC64;
     MVNVKVEFLG GLDAIFGKQR VHKIKMDKED PVTVGDLIDH IVSTMINNPN DVSIFIEDDS
     IRPGIITLIN DTDWELEGEK DYILEDGDII SFTSTLHGG