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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, HCO3-/CO2 and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. 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 + HCO3- = L-threonylcarbamoyladenylate + diphosphate + H2O.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei72L-threonineBy similarity1
Binding sitei95ATPBy similarity1
Binding sitei99ATPBy similarity1
Binding sitei104L-threonineBy similarity1
Binding sitei170ATPBy similarity1
Binding sitei174L-threonineBy similarity1
Binding sitei194L-threonine; via carbonyl oxygenBy similarity1
Binding sitei196ATP; via amide nitrogenBy similarity1
Binding sitei204ATPBy similarity1
Binding sitei234L-threonineBy similarity1
Binding sitei248ATPBy similarity1
Binding sitei292ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

  • regulation of translational fidelity Source: SGD
  • telomere maintenance Source: SGD
  • tRNA threonylcarbamoyladenosine metabolic process Source: SGD
  • tRNA threonylcarbamoyladenosine modification 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
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

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)DescriptionActionsGraphical viewLength
Mutagenesisi70T → A: Reduces t(6)A37 formation. 1 Publication1
Mutagenesisi93K → A: Severely impairs t(6)A37 formation. 1 Publication1
Mutagenesisi95R → A: Severely impairs t(6)A37 formation. 1 Publication1
Mutagenesisi107S → F in SUA5-1; suppresses a translation initiation defect in a CYC1 allele at an aberrant ATG codon. 1 Publication1
Mutagenesisi174R → E: Severely impairs t(6)A37 formation. 1 Publication1
Mutagenesisi196S → A: Severely impairs t(6)A37 formation. 1 Publication1
Mutagenesisi198N → A: Severely impairs t(6)A37 formation. 1 Publication1
Mutagenesisi234S → V: Severely impairs t(6)A37 formation. 1 Publication1
Mutagenesisi423C → S: No phenotypes. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002020131 – 426Threonylcarbamoyl-AMP synthaseAdd BLAST426

Proteomic databases

MaxQBiP32579.
PRIDEiP32579.

Interactioni

Protein-protein interaction databases

BioGridi33085. 16 interactors.
DIPiDIP-2794N.
IntActiP32579. 1 interactor.
MINTiMINT-497166.

Structurei

3D structure databases

ProteinModelPortaliP32579.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini49 – 252YrdC-likePROSITE-ProRule annotationAdd BLAST204

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi225 – 313Gly-richAdd BLAST89

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000076160.
InParanoidiP32579.
KOiK07566.
OMAiRTLDEGP.
OrthoDBiEOG092C2HER.

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33085. 16 interactors.
DIPiDIP-2794N.
IntActiP32579. 1 interactor.
MINTiMINT-497166.

Proteomic databases

MaxQBiP32579.
PRIDEiP32579.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YGL169W.
SGDiS000003137. SUA5.

Phylogenomic databases

HOGENOMiHOG000076160.
InParanoidiP32579.
KOiK07566.
OMAiRTLDEGP.
OrthoDBiEOG092C2HER.

Enzyme and pathway databases

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

Miscellaneous databases

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...

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: November 2, 2016
This is version 128 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

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 one 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.