UniProt functional annotation for P40554



	UniProt functional annotation for P40554

UniProt code: P40554.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

Function: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2- thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth. {ECO:0000269|PubMed:10713047, ECO:0000269|PubMed:14551258, ECO:0000269|PubMed:14555475, ECO:0000269|PubMed:18664566, ECO:0000269|PubMed:18755837, ECO:0000269|PubMed:19017811, ECO:0000269|PubMed:19145231, ECO:0000269|PubMed:19151091, ECO:0000269|PubMed:21209336}.

Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03048}.

Subunit: Homodimer; homodimerization may provide an autoprotection to the highly active C-terminal residue before attacking its substrates. Interacts with NCS2 and NCS6. Forms a conjugate with the target protein AHP1. {ECO:0000255|HAMAP-Rule:MF_03048, ECO:0000269|PubMed:10713047, ECO:0000269|PubMed:14555475, ECO:0000269|PubMed:19145231, ECO:0000269|PubMed:19151091}.

Subcellular location: Cytoplasm. Nucleus.

Ptm: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl- adenylated (-COAMP) via the hesA/moeB/thiF part of UBA4, then thiocarboxylated (-COSH) via the rhodanese domain of UBA4. {ECO:0000255|HAMAP-Rule:MF_03048, ECO:0000269|PubMed:18491921, ECO:0000269|PubMed:19145231, ECO:0000269|PubMed:19151091}.

Miscellaneous: Present with 1240 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Similarity: Belongs to the URM1 family. {ECO:0000255|HAMAP- Rule:MF_03048}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



Function:		Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2- thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. Indirectly involved in regulation of budding and haploid invasive growth. {ECO:0000269\|PubMed:10713047, ECO:0000269\|PubMed:14551258, ECO:0000269\|PubMed:14555475, ECO:0000269\|PubMed:18664566, ECO:0000269\|PubMed:18755837, ECO:0000269\|PubMed:19017811, ECO:0000269\|PubMed:19145231, ECO:0000269\|PubMed:19151091, ECO:0000269\|PubMed:21209336}.


Pathway:		tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255\|HAMAP-Rule:MF_03048}.
Subunit:		Homodimer; homodimerization may provide an autoprotection to the highly active C-terminal residue before attacking its substrates. Interacts with NCS2 and NCS6. Forms a conjugate with the target protein AHP1. {ECO:0000255\|HAMAP-Rule:MF_03048, ECO:0000269\|PubMed:10713047, ECO:0000269\|PubMed:14555475, ECO:0000269\|PubMed:19145231, ECO:0000269\|PubMed:19151091}.
Subcellular location:		Cytoplasm. Nucleus.
Ptm:		C-terminal thiocarboxylation occurs in 2 steps, it is first acyl- adenylated (-COAMP) via the hesA/moeB/thiF part of UBA4, then thiocarboxylated (-COSH) via the rhodanese domain of UBA4. {ECO:0000255\|HAMAP-Rule:MF_03048, ECO:0000269\|PubMed:18491921, ECO:0000269\|PubMed:19145231, ECO:0000269\|PubMed:19151091}.
Miscellaneous:		Present with 1240 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Similarity:		Belongs to the URM1 family. {ECO:0000255\|HAMAP- Rule:MF_03048}.