ID   URM1_VANPO              Reviewed;         103 AA.
AC   A7TQ77;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Ubiquitin-related modifier 1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN   Name=URM1 {ECO:0000255|HAMAP-Rule:MF_03048}; ORFNames=Kpol_487p2;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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 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; DS480454; EDO15569.1; -; Genomic_DNA.
DR   RefSeq; XP_001643427.1; XM_001643377.1.
DR   AlphaFoldDB; A7TQ77; -.
DR   SMR; A7TQ77; -.
DR   STRING; 436907.A7TQ77; -.
DR   EnsemblFungi; EDO15569; EDO15569; Kpol_487p2.
DR   GeneID; 5543658; -.
DR   KEGG; vpo:Kpol_487p2; -.
DR   eggNOG; KOG4146; Eukaryota.
DR   HOGENOM; CLU_148208_0_0_1; -.
DR   InParanoid; A7TQ77; -.
DR   OMA; DYELQPN; -.
DR   OrthoDB; 1541629at2759; -.
DR   PhylomeDB; A7TQ77; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000000267; 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; 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..103
FT                   /note="Ubiquitin-related modifier 1"
FT                   /id="PRO_0000367889"
FT   MOD_RES         103
FT                   /note="1-thioglycine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT   CROSSLNK        103
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
SQ   SEQUENCE   103 AA;  11598 MW;  63F58C4F73378D7A CRC64;
     MVNVKVEFLG GLDAIFKKQR VHKLTLKKNN SDDEPVTVGD LIDYIVENMI EDKNDVEVFL
     QNGTVRAGIL TLINDTDWEL EGEKEYELED GDIISFTSTL HGG