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P32579

- SUA5_YEAST

UniProt

P32579 - SUA5_YEAST

Protein

Threonylcarbamoyl-AMP synthase

Gene

SUA5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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

    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

    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 1 Publication. 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

    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.

    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.
    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.
    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

    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: October 1, 2014
    This is version 110 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