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P32579

- SUA5_YEAST

UniProt

P32579 - SUA5_YEAST

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Protein
Threonylcarbamoyl-AMP synthase
Gene
SUA5, YGL169W, G1660
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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-threonine By similarity
Binding sitei95 – 951ATP By similarity
Binding sitei99 – 991ATP By similarity
Binding sitei104 – 1041L-threonine By similarity
Binding sitei170 – 1701ATP By similarity
Binding sitei174 – 1741L-threonine By similarity
Binding sitei194 – 1941L-threonine; via carbonyl oxygen By similarity
Binding sitei196 – 1961ATP; via amide nitrogen By similarity
Binding sitei204 – 2041ATP By similarity
Binding sitei234 – 2341L-threonine By similarity
Binding sitei248 – 2481ATP By similarity
Binding sitei292 – 2921ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. double-stranded RNA binding Source: InterPro
  3. nucleotidyltransferase activity Source: UniProtKB-KW
  4. single-stranded telomeric DNA binding Source: SGD

GO - Biological processi

  1. regulation of translational fidelity Source: SGD
  2. telomere maintenance Source: SGD
  3. threonylcarbamoyladenosine biosynthetic process Source: SGD
  4. 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.

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: Chromosome VII

Organism-specific databases

CYGDiYGL169w.
SGDiS000003137. SUA5.

Subcellular locationi

Cytoplasm. Nucleus By similarity. Chromosometelomere 1 Publication

GO - Cellular componenti

  1. chromosome, telomeric region Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
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 synthase
PRO_0000202013Add
BLAST

Proteomic databases

MaxQBiP32579.
PaxDbiP32579.
PeptideAtlasiP32579.

Expressioni

Gene expression databases

GenevestigatoriP32579.

Interactioni

Protein-protein interaction databases

BioGridi33085. 15 interactions.
DIPiDIP-2794N.
IntActiP32579. 1 interaction.
MINTiMINT-497166.
STRINGi4932.YGL169W.

Structurei

3D structure databases

ProteinModelPortaliP32579.
SMRiP32579. Positions 18-425.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 252204YrdC-like
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the SUA5 family.
Contains 1 YrdC-like domain.

Phylogenomic databases

eggNOGiCOG0009.
HOGENOMiHOG000076160.
KOiK07566.
OMAiKYLREVD.
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

MYLGRHFLAM TSKALFDTKI LKVNPLSIIF SPDAHIDGSL PTITDPETEA    50
ALVEAARIIR DTDETVAFPT ETVYGLGGSA LNDNSVLSIY RAKNRPSDNP 100
LITHVSSIDQ LNRKVFNQPH LSGTSLFDNI PSIYRPLISS LWPGPLTILL 150
PVPSSEHSAL SKLTTADQPT FAVRIPANPV ARALIALSDT PIAAPSANAS 200
TRPSPTLASH VYHDLKDKIP IILDGGACKV GVESTVVDGL CNPPTLLRPG 250
GFTYEEIVKL GGEAWSLCKV ENKKTVEKGE KVRTPGMKYR HYSPSAKVVL 300
LVPHCEGDGI LKGVDRMERL KRLIETELKA NSNIKKIAIL TSLKLRDSDL 350
QSKIFNEPDF SSKTFIIERL GQSGEEIQTN LFAALRKVDE NDKVDLIFVE 400
GINEEGEGLA VMNRLRKAAA NNCIQF 426
Length:426
Mass (Da):46,538
Last modified:October 1, 1993 - v1
Checksum:iF7B54D4A07BCF8A0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S41991.
RefSeqi NP_011346.1. NM_001181034.1.

3D structure databases

ProteinModelPortali P32579.
SMRi P32579. Positions 18-425.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33085. 15 interactions.
DIPi DIP-2794N.
IntActi P32579. 1 interaction.
MINTi MINT-497166.
STRINGi 4932.YGL169W.

Proteomic databases

MaxQBi P32579.
PaxDbi P32579.
PeptideAtlasi P32579.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL169W ; YGL169W ; YGL169W .
GeneIDi 852707.
KEGGi sce:YGL169W.

Organism-specific databases

CYGDi YGL169w.
SGDi S000003137. SUA5.

Phylogenomic databases

eggNOGi COG0009.
HOGENOMi HOG000076160.
KOi K07566.
OMAi KYLREVD.
OrthoDBi EOG7WDNC2.

Enzyme and pathway databases

BioCyci YEAST:G3O-30657-MONOMER.

Miscellaneous databases

NextBioi 972064.
PROi P32579.

Gene expression databases

Genevestigatori P32579.

Family and domain databases

Gene3Di 3.90.870.10. 1 hit.
InterProi IPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR005145. SUA5.
IPR010923. t(6)A37_SUA5.
IPR006070. YrdC-like_dom.
[Graphical view ]
Pfami PF03481. SUA5. 1 hit.
PF01300. Sua5_yciO_yrdC. 1 hit.
[Graphical view ]
PIRSFi PIRSF004930. Tln_factor_SUA5. 1 hit.
SUPFAMi SSF55821. SSF55821. 1 hit.
TIGRFAMsi TIGR00057. TIGR00057. 1 hit.
PROSITEi PS51163. YRDC. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 109 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.

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

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