Reviewed, UniProtKB/Swiss-Prot P53088 (CTU1_YEAST)

Names and origin

Protein names

Recommended name:
    Cytoplasmic tRNA 2-thiolation protein 1
    EC=2.7.7.-
Alternative name(s):
    Cytoplasmic tRNA adenylyltransferase 1
    Thiolation of uridine in cytoplasmic tRNA protein 1
    Needs CLA4 to survive protein 6

Gene names

Name:	NCS6
Synonyms:	CTU1, TUC1
Ordered Locus Names:	YGL211W
ORF Names:	YGL210W-A

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm5 tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation. May also be involved in protein urmylation and in invasive and pseudohyphal growth. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Pathway	tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Subunit structure	Interacts with NCS2 and URM1. May act by forming a heterodimer with NCS2. Component of a large molecular weight complex of more than 250 kDa. Ref.8 Ref.11
Subcellular location	Cytoplasm. Mitochondrion. Ref.8 Ref.6
Sequence similarities	Belongs to the ttcA family. CTU1/NCS6/ATPBD3 subfamily.
Sequence caution	The sequence AAC49498.1 differs from that shown. Reason: Frameshift at position 318. The sequence CAA96927.1 differs from that shown. Reason: Frameshift at positions 175, 247 and 304.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm Mitochondrion
Ligand	RNA-binding tRNA-binding
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein urmylation Ref.5 Inferred from mutant phenotype. Source: SGD response to drug Inferred from mutant phenotype. Source: SGD wobble position uridine thiolation Ref.8 Ref.12 Inferred from mutant phenotype. Source: SGD
Cellular component	cytosol Ref.8 Inferred from direct assay. Source: UniProtKB mitochondrion Ref.6 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro nucleotidyltransferase activity Ref.8 Inferred from direct assay. Source: UniProtKB protein binding Ref.11 Inferred from physical interaction. Source: UniProtKB tRNA binding Ref.11 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESS1	P22696	1	EBI-24137,EBI-6679

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	Cytoplasmic tRNA 2-thiolation protein 1		PRO_0000219889
Experimental info
	Sequence conflict	356 – 359	4	KLSF → NSA in AAC49498. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P53088-1 [UniParc]. Last modified October 3, 2006. Version 3. Checksum: F04BB5B93F642CC6	FASTA	359	39,987
	10 20 30 40 50 60 MSFTAPSDPV NKPTKVKVSQ LCELCHSRKA LIRRPKNLSK LCKQCFCLVF ETEIHNTIVA 70 80 90 100 110 120 NNLFQRGEKV AVGASGGKDS TVLAHMLKLL NDRYDYGIEI VLLSIDEGII GYRDDSLATV 130 140 150 160 170 180 KRNQQQYGLP LEIFSFKDLY DWTMDEIVSV AGIRNSCTYC GVFRRQSLDR GAAKLGISHV 190 200 210 220 230 240 VTGHNADDMA ETVLMNILRG DVARLEKSTA IITQSSGSPI KRSKPFKYSY QKEIVLYAHY 250 260 270 280 290 300 MKLDYFSTEC TYAPEAFRGT AREYMKNLEA VRPSCIIDII QSGENLALKA KKSNAGKRVV 310 320 330 340 350 KFVDGNRCAR CGYLSSNNIC KACMLLEGLE KSRAQVAIEN DTSADGAALK LRALEKLSF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lambda clone B22 contains a 7676 bp genomic fragment of Saccharomyces cerevisiae chromosome VII spanning the VAM7-SPM2 intergenic region and containing three novel transcribed open reading frames." Kail M., Juettner E., Vaux D. Yeast 12:799-807(1996) [PubMed: 8813766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII reveals 11 open reading frames: two correspond to new genes." Feuermann M., Simeonava L., Souciet J.-L., Potier S. Yeast 13:475-477(1997) [PubMed: 9153757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii." Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P. Genome Biol. 4:RESEARCH45.1-RESEARCH45.13(2003) [PubMed: 12844361] [Abstract] Cited for: IDENTIFICATION OF FRAMESHIFTS.
[5]	"Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast." Goehring A.S., Rivers D.M., Sprague G.F. Jr. Mol. Biol. Cell 14:4329-4341(2003) [PubMed: 14551258] [Abstract] Cited for: FUNCTION.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"A conserved modified wobble nucleoside (mcm5s2U) in lysyl-tRNA is required for viability in yeast." Bjoerk G.R., Huang B., Persson O.P., Bystroem A.S. RNA 13:1245-1255(2007) [PubMed: 17592039] [Abstract] Cited for: FUNCTION.
[8]	"Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems." Nakai Y., Nakai M., Hayashi H. J. Biol. Chem. 283:27469-27476(2008) [PubMed: 18664566] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[9]	"Eukaryotic wobble uridine modifications promote a functionally redundant decoding system." Johansson M.J.O., Esberg A., Huang B., Bjoerk G.R., Bystroem A.S. Mol. Cell. Biol. 28:3301-3312(2008) [PubMed: 18332122] [Abstract] Cited for: FUNCTION.
[10]	"A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae." Huang B., Lu J., Bystroem A.S. RNA 14:2183-2194(2008) [PubMed: 18755837] [Abstract] Cited for: FUNCTION IN 2-THIOLATION OF TRNA.
[11]	"Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA." Leidel S., Pedrioli P.G.A., Bucher T., Brost R., Costanzo M., Schmidt A., Aebersold R., Boone C., Hofmann K., Peter M. Nature 458:228-233(2009) [PubMed: 19145231] [Abstract] Cited for: FUNCTION IN 2-THIOLATION OF TRNA, TRNA-BINDING, INTERACTION WITH NCS2 AND URM1.
[12]	"Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions." Noma A., Sakaguchi Y., Suzuki T. Nucleic Acids Res. 37:1335-1352(2009) [PubMed: 19151091] [Abstract] Cited for: FUNCTION IN 2-THIOLATION OF TRNA.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U33754 Genomic DNA. Translation: AAC49498.1. Frameshift. Z72733 Genomic DNA. Translation: CAA96927.1. Frameshift.
PIR	S64230. S71668.
RefSeq	NP_011304.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P53088. 4 interactions.
STRING	P53088.
Proteomic databases
PeptideAtlas	P53088.
PRIDE	P53088.
Genome annotation databases
Ensembl	YGL211W; YGL211W; YGL211W; Saccharomyces cerevisiae. [Genome view]
GeneID	852661.
GenomeReviews	Gene locus YGL211W in contig Y13135_GR.
KEGG	sce:YGL211W.
NMPDR	fig|4932.3.peg.2407.
Organism-specific databases
CYGD	YGL211w.
SGD	S000003179. NCS6.
Phylogenomic databases
HOGENOM	P53088.
OMA	ARLRRCT.
Gene expression databases
ArrayExpress	P53088.
Genevestigator	P53088.
GermOnline	YGL211W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR012089. 2-thiocytidine_tRNA_synth_TtcA. IPR011063. PP_loop. IPR014729. Rossmann-like_a/b/a_fold. IPR020554. UPF0021_CS. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
Pfam	PF01171. ATP_bind_3. 1 hit. [Graphical view]
PIRSF	PIRSF004976. ATPase_YdaO. 1 hit.
PROSITE	PS01263. UPF0021. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	971945.

Entry information

Entry name

CTU1_YEAST

Accession

Primary (citable) accession number: P53088
Secondary accession number(s): Q92322

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 3, 2006
Last modified:	November 3, 2009
This is version 70 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)