tRNA threonylcarbamoyladenosine biosynthesis protein SUA5 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32579 (SUA5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
tRNA threonylcarbamoyladenosine biosynthesis protein SUA5

Alternative name(s):
Suppressor of upstream AUG protein 5
t(6)A37 threonylcarbamoyladenosine biosynthesis protein SUA5

Gene names

Name:	SUA5
Ordered Locus Names:	YGL169W
ORF Names:	G1660

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	426 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t₆A37) in tRNAs that read codons beginning with adenine. Required for normal translation, by ensuring translation fidelity at the level of codon recognition, appropriate translation initiation selection and maintenance of reading frame. Also involved in telomere replication. Binds to single-stranded telomeric (ssTG) DNA and positively regulates telomere length. Ref.7 Ref.8 Ref.9
Subcellular location	Cytoplasm. Nucleus By similarity. Chromosome › telomere Ref.5.
Disruption phenotype	Causes increased leaky scanning through AUG codons, +1 frameshifting, and read-through of stop codons. Also causes progressive telomere shortening. Ref.7 Ref.9
Miscellaneous	Present with 538 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SUA5 family. Contains 1 YrdC-like domain.

Ontologies

Keywords
Biological process	Translation regulation tRNA processing
Cellular component	Chromosome Cytoplasm Nucleus Telomere
Ligand	DNA-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of translational fidelity Inferred from mutant phenotype Ref.9. Source: SGD tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW telomere maintenance Inferred from mutant phenotype Ref.7. Source: SGD threonylcarbamoyladenosine metabolic process Inferred from mutant phenotype Ref.8 PubMed 21183954. Source: SGD
Cellular_component	chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay Ref.5. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	double-stranded RNA binding Inferred from electronic annotation. Source: InterPro single-stranded telomeric DNA binding Inferred from direct assay Ref.7. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 426

426

tRNA threonylcarbamoyladenosine biosynthesis protein SUA5

PRO_0000202013

Regions

Domain

49 – 252

204

YrdC-like

Compositional bias

225 – 313

Gly-rich

Experimental info

Mutagenesis

107

S → F in SUA5-1; suppresses a translation initiation defect in a CYC1 allele at an aberrant ATG codon. Ref.1

Mutagenesis

423

C → S: No phenotypes.

Sequences

Sequence

Length

Mass (Da)

Tools

P32579 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: F7B54D4A07BCF8A0
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FASTA

426

46,538

        10         20         30         40         50         60 
MYLGRHFLAM TSKALFDTKI LKVNPLSIIF SPDAHIDGSL PTITDPETEA ALVEAARIIR 

        70         80         90        100        110        120 
DTDETVAFPT ETVYGLGGSA LNDNSVLSIY RAKNRPSDNP LITHVSSIDQ LNRKVFNQPH 

       130        140        150        160        170        180 
LSGTSLFDNI PSIYRPLISS LWPGPLTILL PVPSSEHSAL SKLTTADQPT FAVRIPANPV 

       190        200        210        220        230        240 
ARALIALSDT PIAAPSANAS TRPSPTLASH VYHDLKDKIP IILDGGACKV GVESTVVDGL 

       250        260        270        280        290        300 
CNPPTLLRPG GFTYEEIVKL GGEAWSLCKV ENKKTVEKGE KVRTPGMKYR HYSPSAKVVL 

       310        320        330        340        350        360 
LVPHCEGDGI LKGVDRMERL KRLIETELKA NSNIKKIAIL TSLKLRDSDL QSKIFNEPDF 

       370        380        390        400        410        420 
SSKTFIIERL GQSGEEIQTN LFAALRKVDE NDKVDLIFVE GINEEGEGLA VMNRLRKAAA 


NNCIQF

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of SUA5, a novel gene required for normal growth in Saccharomyces cerevisiae." Na J.G., Pinto I., Hampsey M. Genetics 131:791-801(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-107.
[2]	"A putative helicase, the SUA5, PMR1, tRNALys1 genes and four open reading frames have been detected in the DNA sequence of an 8.8 kb fragment of the left arm of chromosome VII of Saccharomyces cerevisiae." Klima R., Coglievina M., Zaccaria P., Bertani I., Bruschi C.V. Yeast 12:1033-1040(1996) [PubMed] [Europe PMC] [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. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Sua5p a single-stranded telomeric DNA-binding protein facilitates telomere replication." Meng F.-L., Hu Y., Shen N., Tong X.-J., Wang J., Ding J., Zhou J.-Q. EMBO J. 28:1466-1478(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TELOMERE REPLICATION, DISRUPTION PHENOTYPE.
[8]	"The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA." El Yacoubi B., Lyons B., Cruz Y., Reddy R., Nordin B., Agnelli F., Williamson J.R., Schimmel P., Swairjo M.A., de Crecy-Lagard V. Nucleic Acids Res. 37:2894-2909(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRNA MODIFICATION.
[9]	"The Sua5 protein is essential for normal translational regulation in yeast." Lin C.A., Ellis S.R., True H.L. Mol. Cell. Biol. 30:354-363(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSLATION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X64319 Genomic DNA. Translation: CAA45598.1. X85757 Genomic DNA. Translation: CAA59760.1. Z72691 Genomic DNA. Translation: CAA96881.1. BK006941 Genomic DNA. Translation: DAA07944.1.
PIR	S41991.
RefSeq	NP_011346.1. NM_001181034.1.
3D structure databases
ProteinModelPortal	P32579.
SMR	P32579. Positions 18-425.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2794N.
IntAct	P32579. 1 interaction.
MINT	MINT-497166.
STRING	4932.YGL169W.
Proteomic databases
PaxDb	P32579.
PeptideAtlas	P32579.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL169W; YGL169W; YGL169W.
GeneID	852707.
KEGG	sce:YGL169W.
Organism-specific databases
CYGD	YGL169w.
SGD	S000003137. SUA5.
Phylogenomic databases
eggNOG	COG0009.
GeneTree	ENSGT00390000015364.
HOGENOM	HOG000076160.
KO	K07566.
OMA	LLITKET.
OrthoDB	EOG4C8C27.
Enzyme and pathway databases
BioCyc	YEAST:G3O-30657-MONOMER.
Gene expression databases
Genevestigator	P32579.
GermOnline	YGL169W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.90.870.10. 1 hit.
InterPro	IPR017945. DHBP_synth_RibB-like_a/b_dom. IPR005145. SUA5. IPR010923. t(6)A37_SUA5. IPR006070. YrdC-like_dom. [Graphical view]
Pfam	PF03481. SUA5. 1 hit. PF01300. Sua5_yciO_yrdC. 1 hit. [Graphical view]
PIRSF	PIRSF004930. Tln_factor_SUA5. 1 hit.
SUPFAM	SSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit.
TIGRFAMs	TIGR00057. TIGR00057. 1 hit.
PROSITE	PS51163. YRDC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972064.

Entry information

Entry name

SUA5_YEAST

Accession

Primary (citable) accession number: P32579
Secondary accession number(s): D6VTY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 29, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents