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P32579 (SUA5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Threonylcarbamoyl-AMP synthase

Short name=TC-AMP synthase
EC=2.7.7.87
Alternative name(s):
L-threonylcarbamoyladenylate synthase
Suppressor of upstream AUG protein 5
t(6)A37 threonylcarbamoyladenosine biosynthesis protein SUA5
tRNA threonylcarbamoyladenosine biosynthesis protein SUA5
Gene names
Name:SUA5
Ordered Locus Names:YGL169W
ORF Names:G1660
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Likely catalyzes the conversion of L-threonine, bicarbonate/CO2 and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of pyrophosphate. 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 Ref.10 Ref.11 Ref.12

Catalytic activity

L-threonine + ATP + bicarbonate = L-threonylcarbamoyladenylate + diphosphate + H2O. Ref.12

Subcellular location

Cytoplasm. Nucleus By similarity. Chromosometelomere 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Threonylcarbamoyl-AMP synthase
PRO_0000202013

Regions

Domain49 – 252204YrdC-like
Compositional bias225 – 31389Gly-rich

Sites

Binding site721L-threonine By similarity
Binding site951ATP By similarity
Binding site991ATP By similarity
Binding site1041L-threonine By similarity
Binding site1701ATP By similarity
Binding site1741L-threonine By similarity
Binding site1941L-threonine; via carbonyl oxygen By similarity
Binding site1961ATP; via amide nitrogen By similarity
Binding site2041ATP By similarity
Binding site2341L-threonine By similarity
Binding site2481ATP By similarity
Binding site2921ATP By similarity

Experimental info

Mutagenesis701T → A: Reduces t(6)A37 formation. Ref.12
Mutagenesis931K → A: Severely impairs t(6)A37 formation. Ref.12
Mutagenesis951R → A: Severely impairs t(6)A37 formation. Ref.12
Mutagenesis1071S → F in SUA5-1; suppresses a translation initiation defect in a CYC1 allele at an aberrant ATG codon. Ref.1
Mutagenesis1741R → E: Severely impairs t(6)A37 formation. Ref.12
Mutagenesis1961S → A: Severely impairs t(6)A37 formation. Ref.12
Mutagenesis1981N → A: Severely impairs t(6)A37 formation. Ref.12
Mutagenesis2341S → V: Severely impairs t(6)A37 formation. Ref.12
Mutagenesis4231C → S: No phenotypes.

Sequences

Sequence LengthMass (Da)Tools
P32579 [UniParc].

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

FASTA42646,538
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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.
[10]"The highly conserved KEOPS/EKC complex is essential for a universal tRNA modification, t6A."
Srinivasan M., Mehta P., Yu Y., Prugar E., Koonin E.V., Karzai A.W., Sternglanz R.
EMBO J. 30:873-881(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya."
Perrochia L., Crozat E., Hecker A., Zhang W., Bareille J., Collinet B., van Tilbeurgh H., Forterre P., Basta T.
Nucleic Acids Res. 41:1953-1964(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN T(6)A TRNA MODIFICATION.
[12]"Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system."
Wan L.C., Mao D.Y., Neculai D., Strecker J., Chiovitti D., Kurinov I., Poda G., Thevakumaran N., Yuan F., Szilard R.K., Lissina E., Nislow C., Caudy A.A., Durocher D., Sicheri F.
Nucleic Acids Res. 41:6332-6346(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-70; LYS-93; ARG-95; ARG-174; SER-196; ASN-198 AND SER-234.
+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.
PIRS41991.
RefSeqNP_011346.1. NM_001181034.1.

3D structure databases

ProteinModelPortalP32579.
SMRP32579. Positions 18-425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33085. 15 interactions.
DIPDIP-2794N.
IntActP32579. 1 interaction.
MINTMINT-497166.
STRING4932.YGL169W.

Proteomic databases

MaxQBP32579.
PaxDbP32579.
PeptideAtlasP32579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL169W; YGL169W; YGL169W.
GeneID852707.
KEGGsce:YGL169W.

Organism-specific databases

CYGDYGL169w.
SGDS000003137. SUA5.

Phylogenomic databases

eggNOGCOG0009.
HOGENOMHOG000076160.
KOK07566.
OMAKYLREVD.
OrthoDBEOG7WDNC2.

Enzyme and pathway databases

BioCycYEAST:G3O-30657-MONOMER.

Gene expression databases

GenevestigatorP32579.

Family and domain databases

Gene3D3.90.870.10. 1 hit.
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR005145. SUA5.
IPR010923. t(6)A37_SUA5.
IPR006070. YrdC-like_dom.
[Graphical view]
PfamPF03481. SUA5. 1 hit.
PF01300. Sua5_yciO_yrdC. 1 hit.
[Graphical view]
PIRSFPIRSF004930. Tln_factor_SUA5. 1 hit.
SUPFAMSSF55821. SSF55821. 1 hit.
TIGRFAMsTIGR00057. TIGR00057. 1 hit.
PROSITEPS51163. YRDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972064.
PROP32579.

Entry information

Entry nameSUA5_YEAST
AccessionPrimary (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: June 11, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families