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Protein

Tyrosine--tRNA ligase

Gene

tyrS

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).1 Publication

Catalytic activityi

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).

Kineticsi

  1. KM=15 µM for tRNA(Tyr) (at 45 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei32Tyrosine1 Publication1
    Binding sitei36Tyrosine1 Publication1
    Binding sitei173Tyrosine1 Publication1
    Binding sitei207ATPSequence analysis1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.1. 3260.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine--tRNA ligase (EC:6.1.1.1)
    Alternative name(s):
    Tyrosyl-tRNA synthetase
    Short name:
    TyrRS
    Gene namesi
    Name:tyrS
    Ordered Locus Names:MJ0389
    OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
    Taxonomic identifieri243232 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
    Proteomesi
    • UP000000805 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi32Y → Q: Confers specificity for the non-natural amino acid O-methyl-tyrosine; when associated with T-107; A-158 and P-162. 1
    Mutagenesisi107E → T: Confers specificity for the non-natural amino acid O-methyl-tyrosine; when associated with Q-32; A-158 and P-162. 1
    Mutagenesisi158D → A: Confers specificity for the non-natural amino acid O-methyl-tyrosine; when associated with Q-32; T-107 and P-162. 1
    Mutagenesisi162L → P: Confers specificity for the non-natural amino acid O-methyl-tyrosine; when associated with Q-32; T-107 and A-158. 1
    Mutagenesisi286D → A: Decreases the rate of aminoacylation more than 10-fold, without effect on tyrosyl adenylate synthesis. 2 Publications1
    Mutagenesisi286D → R: Decreases the rate of aminoacylation with wild-type tRNA and increases aminoacylation with amber suppressor tRNA 8-fold. Decreases affinity for wild-type tRNA and increases affinity for amber suppressor tRNA. 2 Publications1
    Mutagenesisi288K → A: Decreases the rate of aminoacylation more than 200-fold, without effect on tyrosyl adenylate synthesis. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000556691 – 306Tyrosine--tRNA ligaseAdd BLAST306

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei143Interaction with t-RNA1

    Protein-protein interaction databases

    STRINGi243232.MJ_0389.

    Structurei

    Secondary structure

    1306
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 8Combined sources6
    Beta strandi12 – 15Combined sources4
    Helixi17 – 24Combined sources8
    Beta strandi26 – 35Combined sources10
    Helixi43 – 57Combined sources15
    Beta strandi60 – 66Combined sources7
    Helixi68 – 73Combined sources6
    Helixi79 – 95Combined sources17
    Beta strandi101 – 104Combined sources4
    Helixi105 – 107Combined sources3
    Turni108 – 110Combined sources3
    Helixi112 – 124Combined sources13
    Helixi127 – 133Combined sources7
    Turni134 – 137Combined sources4
    Helixi147 – 162Combined sources16
    Beta strandi165 – 170Combined sources6
    Helixi171 – 173Combined sources3
    Helixi174 – 183Combined sources10
    Beta strandi184 – 186Combined sources3
    Beta strandi189 – 193Combined sources5
    Beta strandi201 – 204Combined sources4
    Turni207 – 210Combined sources4
    Beta strandi214 – 216Combined sources3
    Helixi219 – 228Combined sources10
    Helixi240 – 248Combined sources9
    Beta strandi251 – 255Combined sources5
    Helixi259 – 261Combined sources3
    Beta strandi265 – 269Combined sources5
    Helixi270 – 278Combined sources9
    Helixi284 – 306Combined sources23

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1J1UX-ray1.95A1-306[»]
    1U7DX-ray2.65A/B1-306[»]
    1U7XX-ray3.00A/B1-306[»]
    1ZH0X-ray1.90A1-306[»]
    1ZH6X-ray2.50A1-306[»]
    2AG6X-ray1.90A1-306[»]
    2HGZX-ray2.50A2-306[»]
    2PXHX-ray1.97A1-306[»]
    2ZP1X-ray1.70A1-306[»]
    3D6UX-ray2.20A1-306[»]
    3D6VX-ray2.20A1-306[»]
    3N2YX-ray2.49A/B1-306[»]
    3QE4X-ray2.30A/B1-306[»]
    4HJRX-ray2.50A/B1-306[»]
    4HJXX-ray2.91A/B1-306[»]
    4HK4X-ray2.30A1-306[»]
    4HPWX-ray2.00A1-306[»]
    4ND6X-ray2.00A1-306[»]
    4ND7X-ray2.00A1-306[»]
    4NDAX-ray1.70A1-306[»]
    4NX2X-ray2.00A1-306[»]
    4PBRX-ray1.90A1-306[»]
    4PBSX-ray2.01A1-306[»]
    4PBTX-ray1.90A1-306[»]
    ProteinModelPortaliQ57834.
    SMRiQ57834.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ57834.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni151 – 158Tyrosine8
    Regioni228 – 231Interaction with t-RNA4
    Regioni283 – 288Interaction with t-RNA6

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi37 – 45"HIGH" region9
    Motifi204 – 208"KMSKS" region5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiarCOG01886. Archaea.
    COG0162. LUCA.
    InParanoidiQ57834.
    KOiK01866.
    OMAiFSKLIYP.
    PhylomeDBiQ57834.

    Family and domain databases

    CDDicd00805. TyrRS_core. 1 hit.
    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_02008. Tyr_tRNA_synth_type3. 1 hit.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR002305. aa-tRNA-synth_Ic.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR002307. Tyr-tRNA-ligase.
    IPR023684. Tyr-tRNA-ligase_3.
    IPR023617. Tyr-tRNA-ligase_arc/euk-type.
    [Graphical view]
    PfamiPF00579. tRNA-synt_1b. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006588. TyrRS_arch_euk. 1 hit.
    PRINTSiPR01040. TRNASYNTHTYR.
    TIGRFAMsiTIGR00234. tyrS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q57834-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDEFEMIKRN TSEIISEEEL REVLKKDEKS AYIGFEPSGK IHLGHYLQIK
    60 70 80 90 100
    KMIDLQNAGF DIIILLADLH AYLNQKGELD EIRKIGDYNK KVFEAMGLKA
    110 120 130 140 150
    KYVYGSEFQL DKDYTLNVYR LALKTTLKRA RRSMELIARE DENPKVAEVI
    160 170 180 190 200
    YPIMQVNDIH YLGVDVAVGG MEQRKIHMLA RELLPKKVVC IHNPVLTGLD
    210 220 230 240 250
    GEGKMSSSKG NFIAVDDSPE EIRAKIKKAY CPAGVVEGNP IMEIAKYFLE
    260 270 280 290 300
    YPLTIKRPEK FGGDLTVNSY EELESLFKNK ELHPMDLKNA VAEELIKILE

    PIRKRL
    Length:306
    Mass (Da):35,049
    Last modified:November 1, 1997 - v1
    Checksum:i1887760ABAF2DD5E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L77117 Genomic DNA. Translation: AAB98375.1.
    PIRiE64348.
    RefSeqiWP_010869888.1. NC_000909.1.

    Genome annotation databases

    EnsemblBacteriaiAAB98375; AAB98375; MJ_0389.
    GeneIDi1451246.
    KEGGimja:MJ_0389.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L77117 Genomic DNA. Translation: AAB98375.1.
    PIRiE64348.
    RefSeqiWP_010869888.1. NC_000909.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1J1UX-ray1.95A1-306[»]
    1U7DX-ray2.65A/B1-306[»]
    1U7XX-ray3.00A/B1-306[»]
    1ZH0X-ray1.90A1-306[»]
    1ZH6X-ray2.50A1-306[»]
    2AG6X-ray1.90A1-306[»]
    2HGZX-ray2.50A2-306[»]
    2PXHX-ray1.97A1-306[»]
    2ZP1X-ray1.70A1-306[»]
    3D6UX-ray2.20A1-306[»]
    3D6VX-ray2.20A1-306[»]
    3N2YX-ray2.49A/B1-306[»]
    3QE4X-ray2.30A/B1-306[»]
    4HJRX-ray2.50A/B1-306[»]
    4HJXX-ray2.91A/B1-306[»]
    4HK4X-ray2.30A1-306[»]
    4HPWX-ray2.00A1-306[»]
    4ND6X-ray2.00A1-306[»]
    4ND7X-ray2.00A1-306[»]
    4NDAX-ray1.70A1-306[»]
    4NX2X-ray2.00A1-306[»]
    4PBRX-ray1.90A1-306[»]
    4PBSX-ray2.01A1-306[»]
    4PBTX-ray1.90A1-306[»]
    ProteinModelPortaliQ57834.
    SMRiQ57834.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243232.MJ_0389.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAB98375; AAB98375; MJ_0389.
    GeneIDi1451246.
    KEGGimja:MJ_0389.

    Phylogenomic databases

    eggNOGiarCOG01886. Archaea.
    COG0162. LUCA.
    InParanoidiQ57834.
    KOiK01866.
    OMAiFSKLIYP.
    PhylomeDBiQ57834.

    Enzyme and pathway databases

    BRENDAi6.1.1.1. 3260.

    Miscellaneous databases

    EvolutionaryTraceiQ57834.

    Family and domain databases

    CDDicd00805. TyrRS_core. 1 hit.
    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_02008. Tyr_tRNA_synth_type3. 1 hit.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR002305. aa-tRNA-synth_Ic.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR002307. Tyr-tRNA-ligase.
    IPR023684. Tyr-tRNA-ligase_3.
    IPR023617. Tyr-tRNA-ligase_arc/euk-type.
    [Graphical view]
    PfamiPF00579. tRNA-synt_1b. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006588. TyrRS_arch_euk. 1 hit.
    PRINTSiPR01040. TRNASYNTHTYR.
    TIGRFAMsiTIGR00234. tyrS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSYY_METJA
    AccessioniPrimary (citable) accession number: Q57834
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: November 30, 2016
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Methanococcus jannaschii
      Methanococcus jannaschii: entries and gene names
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    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.