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Protein

Threonylcarbamoyl-AMP synthase

Gene

SUA5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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 translation Source: UniProtKB-KW
  • regulation of translational fidelity Source: SGD
  • telomere maintenance Source: SGD
  • tRNA threonylcarbamoyladenosine metabolic process Source: SGD
  • tRNA threonylcarbamoyladenosine modification Source: SGD

Keywordsi

Molecular functionDNA-binding, Nucleotidyltransferase, Transferase
Biological processTranslation regulation, tRNA processing
LigandATP-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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP32579
PRIDEiP32579

Interactioni

Protein-protein interaction databases

BioGridi33085, 74 interactors
DIPiDIP-2794N
IntActiP32579, 2 interactors
MINTiP32579
STRINGi4932.YGL169W

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

Phylogenomic databases

HOGENOMiHOG000076160
InParanoidiP32579
KOiK07566
OMAiGMLKSHY
OrthoDBiEOG092C2HER

Family and domain databases

Gene3Di3.40.50.11030, 1 hit
InterProiView protein in InterPro
IPR017945 DHBP_synth_RibB-like_a/b_dom
IPR005145 SUA5
IPR038385 Sua5/YwlC_C
IPR010923 t(6)A37_SUA5
IPR006070 YrdC-like_dom
PfamiView protein in Pfam
PF03481 SUA5, 1 hit
PF01300 Sua5_yciO_yrdC, 1 hit
PIRSFiPIRSF004930 Tln_factor_SUA5, 1 hit
SUPFAMiSSF55821 SSF55821, 1 hit
TIGRFAMsiTIGR00057 TIGR00057, 1 hit
PROSITEiView protein in PROSITE
PS51163 YRDC, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiSUA5_YEAST
AccessioniPrimary (citable) accession number: P32579
Secondary accession number(s): D6VTY3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: March 28, 2018
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health