Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Threonylcarbamoyl-AMP synthase

Gene

SUA5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

L-threonine + ATP + bicarbonate = L-threonylcarbamoyladenylate + diphosphate + H2O.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721L-threonineBy similarity
Binding sitei95 – 951ATPBy similarity
Binding sitei99 – 991ATPBy similarity
Binding sitei104 – 1041L-threonineBy similarity
Binding sitei170 – 1701ATPBy similarity
Binding sitei174 – 1741L-threonineBy similarity
Binding sitei194 – 1941L-threonine; via carbonyl oxygenBy similarity
Binding sitei196 – 1961ATP; via amide nitrogenBy similarity
Binding sitei204 – 2041ATPBy similarity
Binding sitei234 – 2341L-threonineBy similarity
Binding sitei248 – 2481ATPBy similarity
Binding sitei292 – 2921ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • regulation of translational fidelity Source: SGD
  • telomere maintenance Source: SGD
  • threonylcarbamoyladenosine biosynthetic process Source: SGD
  • threonylcarbamoyladenosine metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Translation regulation, tRNA processing

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30657-MONOMER.
BRENDAi2.7.7.87. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonylcarbamoyl-AMP synthase (EC:2.7.7.87)
Short name:
TC-AMP synthase
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 namesi
Name:SUA5
Ordered Locus Names:YGL169W
ORF Names:G1660
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL169w.
EuPathDBiFungiDB:YGL169W.
SGDiS000003137. SUA5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

Pathology & Biotechi

Disruption phenotypei

Causes increased leaky scanning through AUG codons, +1 frameshifting, and read-through of stop codons. Also causes progressive telomere shortening.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi70 – 701T → A: Reduces t(6)A37 formation. 1 Publication
Mutagenesisi93 – 931K → A: Severely impairs t(6)A37 formation. 1 Publication
Mutagenesisi95 – 951R → A: Severely impairs t(6)A37 formation. 1 Publication
Mutagenesisi107 – 1071S → F in SUA5-1; suppresses a translation initiation defect in a CYC1 allele at an aberrant ATG codon. 1 Publication
Mutagenesisi174 – 1741R → E: Severely impairs t(6)A37 formation. 1 Publication
Mutagenesisi196 – 1961S → A: Severely impairs t(6)A37 formation. 1 Publication
Mutagenesisi198 – 1981N → A: Severely impairs t(6)A37 formation. 1 Publication
Mutagenesisi234 – 2341S → V: Severely impairs t(6)A37 formation. 1 Publication
Mutagenesisi423 – 4231C → S: No phenotypes.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Threonylcarbamoyl-AMP synthasePRO_0000202013Add
BLAST

Proteomic databases

MaxQBiP32579.
PaxDbiP32579.
PeptideAtlasiP32579.

Interactioni

Protein-protein interaction databases

BioGridi33085. 16 interactions.
DIPiDIP-2794N.
IntActiP32579. 1 interaction.
MINTiMINT-497166.

Structurei

3D structure databases

ProteinModelPortaliP32579.
SMRiP32579. Positions 18-425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 252204YrdC-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi225 – 31389Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the SUA5 family.Curated
Contains 1 YrdC-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0009.
HOGENOMiHOG000076160.
InParanoidiP32579.
KOiK07566.
OMAiYRAKNRP.
OrthoDBiEOG7WDNC2.

Family and domain databases

Gene3Di3.90.870.10. 1 hit.
InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR005145. SUA5.
IPR010923. t(6)A37_SUA5.
IPR006070. YrdC-like_dom.
[Graphical view]
PfamiPF03481. SUA5. 1 hit.
PF01300. Sua5_yciO_yrdC. 1 hit.
[Graphical view]
PIRSFiPIRSF004930. Tln_factor_SUA5. 1 hit.
SUPFAMiSSF55821. SSF55821. 1 hit.
TIGRFAMsiTIGR00057. TIGR00057. 1 hit.
PROSITEiPS51163. YRDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32579-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYLGRHFLAM TSKALFDTKI LKVNPLSIIF SPDAHIDGSL PTITDPETEA
60 70 80 90 100
ALVEAARIIR DTDETVAFPT ETVYGLGGSA LNDNSVLSIY RAKNRPSDNP
110 120 130 140 150
LITHVSSIDQ LNRKVFNQPH LSGTSLFDNI PSIYRPLISS LWPGPLTILL
160 170 180 190 200
PVPSSEHSAL SKLTTADQPT FAVRIPANPV ARALIALSDT PIAAPSANAS
210 220 230 240 250
TRPSPTLASH VYHDLKDKIP IILDGGACKV GVESTVVDGL CNPPTLLRPG
260 270 280 290 300
GFTYEEIVKL GGEAWSLCKV ENKKTVEKGE KVRTPGMKYR HYSPSAKVVL
310 320 330 340 350
LVPHCEGDGI LKGVDRMERL KRLIETELKA NSNIKKIAIL TSLKLRDSDL
360 370 380 390 400
QSKIFNEPDF SSKTFIIERL GQSGEEIQTN LFAALRKVDE NDKVDLIFVE
410 420
GINEEGEGLA VMNRLRKAAA NNCIQF
Length:426
Mass (Da):46,538
Last modified:October 1, 1993 - v1
Checksum:iF7B54D4A07BCF8A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64319 Genomic DNA. Translation: CAA45598.1.
X85757 Genomic DNA. Translation: CAA59760.1.
Z72691 Genomic DNA. Translation: CAA96881.1.
BK006941 Genomic DNA. Translation: DAA07944.1.
PIRiS41991.
RefSeqiNP_011346.1. NM_001181034.1.

Genome annotation databases

EnsemblFungiiYGL169W; YGL169W; YGL169W.
GeneIDi852707.
KEGGisce:YGL169W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64319 Genomic DNA. Translation: CAA45598.1.
X85757 Genomic DNA. Translation: CAA59760.1.
Z72691 Genomic DNA. Translation: CAA96881.1.
BK006941 Genomic DNA. Translation: DAA07944.1.
PIRiS41991.
RefSeqiNP_011346.1. NM_001181034.1.

3D structure databases

ProteinModelPortaliP32579.
SMRiP32579. Positions 18-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33085. 16 interactions.
DIPiDIP-2794N.
IntActiP32579. 1 interaction.
MINTiMINT-497166.

Proteomic databases

MaxQBiP32579.
PaxDbiP32579.
PeptideAtlasiP32579.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL169W; YGL169W; YGL169W.
GeneIDi852707.
KEGGisce:YGL169W.

Organism-specific databases

CYGDiYGL169w.
EuPathDBiFungiDB:YGL169W.
SGDiS000003137. SUA5.

Phylogenomic databases

eggNOGiCOG0009.
HOGENOMiHOG000076160.
InParanoidiP32579.
KOiK07566.
OMAiYRAKNRP.
OrthoDBiEOG7WDNC2.

Enzyme and pathway databases

BioCyciYEAST:G3O-30657-MONOMER.
BRENDAi2.7.7.87. 984.

Miscellaneous databases

NextBioi972064.
PROiP32579.

Family and domain databases

Gene3Di3.90.870.10. 1 hit.
InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR005145. SUA5.
IPR010923. t(6)A37_SUA5.
IPR006070. YrdC-like_dom.
[Graphical view]
PfamiPF03481. SUA5. 1 hit.
PF01300. Sua5_yciO_yrdC. 1 hit.
[Graphical view]
PIRSFiPIRSF004930. Tln_factor_SUA5. 1 hit.
SUPFAMiSSF55821. SSF55821. 1 hit.
TIGRFAMsiTIGR00057. TIGR00057. 1 hit.
PROSITEiPS51163. YRDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. 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.

Entry informationi

Entry nameiSUA5_YEAST
AccessioniPrimary (citable) accession number: P32579
Secondary accession number(s): D6VTY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 22, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 538 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.