URM1_CANAL
ID URM1_CANAL Reviewed; 101 AA.
AC Q59WK2; A0A1D8PF27; Q59JW3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ubiquitin-related modifier 1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN Name=URM1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN OrderedLocusNames=CAALFM_C111160CA;
GN ORFNames=CaO19.1016, CaO19.2299, CaO19.9835;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017623; AOW26742.1; -; Genomic_DNA.
DR RefSeq; XP_713904.2; XM_708811.2.
DR AlphaFoldDB; Q59WK2; -.
DR SMR; Q59WK2; -.
DR STRING; 237561.Q59WK2; -.
DR GeneID; 3644399; -.
DR KEGG; cal:CAALFM_C111160CA; -.
DR CGD; CAL0000198786; orf19.9835.
DR VEuPathDB; FungiDB:C1_11160C_A; -.
DR eggNOG; KOG4146; Eukaryota.
DR HOGENOM; CLU_148208_0_0_1; -.
DR InParanoid; Q59WK2; -.
DR OMA; SLIHFMA; -.
DR OrthoDB; 1541629at2759; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q59WK2; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblFungi.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
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; IBA:GO_Central.
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..101
FT /note="Ubiquitin-related modifier 1"
FT /id="PRO_0000367876"
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; 11171 MW; 14E69AC8D4CD1466 CRC64;
MAIKIKVEFL GGLDIISNSV REHKCVIPFE EGEATVADLI TYITKNIISD PKDIPVFIED
GTVRPGILVL INDTDWELEG MEEYVIESGD VFTFTSTLHG G
