URM1_DEBHA
ID URM1_DEBHA Reviewed; 101 AA.
AC Q6BVZ7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Ubiquitin-related modifier 1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN Name=URM1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN OrderedLocusNames=DEHA2B15466g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG85636.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR382134; CAG85636.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_457622.2; XM_457622.2.
DR AlphaFoldDB; Q6BVZ7; -.
DR SMR; Q6BVZ7; -.
DR STRING; 4959.XP_457622.2; -.
DR EnsemblFungi; CAG85636; CAG85636; DEHA2B15466g.
DR GeneID; 2913597; -.
DR KEGG; dha:DEHA2B15466g; -.
DR eggNOG; KOG4146; Eukaryota.
DR HOGENOM; CLU_148208_0_0_1; -.
DR InParanoid; Q6BVZ7; -.
DR OrthoDB; 1541629at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000000599; Chromosome B.
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..101
FT /note="Ubiquitin-related modifier 1"
FT /id="PRO_0000367881"
FT MOD_RES 101
FT /note="1-thioglycine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
SQ SEQUENCE 101 AA; 11050 MW; 0ED1A50C8DCF6FED CRC64;
MGIKVKVEFL GGLDVISNGV REHKCEVPLE EGEATMIDLI KYITATIISD PKDVPVFIEE
GTVRPGILVL INDTDWELEG MEDYVVESGD VLTFTSTLHG G