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Protein

Threonine--tRNA ligase

Gene

thrS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (PubMed:15079065, PubMed:10881191, PubMed:18997014). The rate-limiting step is amino acid activation in the presence of tRNA (PubMed:18997014). The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively (PubMed:18997014). The zinc ion in the active site discriminates against charging of the isosteric amino acid valine (PubMed:10881191). Also activates L-serine, but does not detectably transfer it to tRNA(Thr) (PubMed:15079065). Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain (PubMed:15079065, PubMed:11136973, PubMed:15525511), in a post-transfer reaction probably via water-mediated hydrolysis (PubMed:15525511).6 Publications
ThrS is also a translational repressor protein, it controls binds its own mRNA in the operator region upstream of the start codon (PubMed:3086882). The mRNA region upstream of the start codon has a tRNA-like secondary structure; mRNA and tRNA compete for binding to ThrRS (PubMed:2254931). ThrRS represses translation by preventing the ribosome from to mRNA, and tRNA(Thr) acts as an antirepressor allowing fine level control of enzyme synthesis (PubMed:2254931). X-ray structures prove that operator mRNA and tRNA bind to overlapping sites in the protein (PubMed:10319817, PubMed:11953757).4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit. It helps recognize and select the amino acid substrate, and thus has neither a purely catalytic or structural role (PubMed:10881191).6 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited non-competitively by borrelidin (BN, KI is 3.7 nM) which binds in a 1:1 stoichiometry, inhibiting L-thr activation (PubMed:15507440). BN binds to 4 distinct subsites in the protein, preventing binding of all 3 substrates; BN also inhibits human ThrRS, and thus it is not useful as an antibiotic (PubMed:25824639).2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 36, 22 and 26 s(-1) for L-threonine, beta-hydroxynorvaline and L-serine respectively.1 Publication
  1. KM=94 µM for ATP1 Publication
  2. KM=110 µM for L-threonine activation2 Publications
  3. KM=120 µM for L-threonine activation1 Publication
  4. KM=0.86 µM for L-threonine aminoacylation1 Publication
  5. KM=1.95 mM for beta-hydroxynorvaline activation1 Publication
  6. KM=81.5 mM for L-serine activation1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei309Binds 2'-OH of adenine 76 of tRNA(Thr), the tRNA acceptor baseCombined sources1 Publication1
    Binding sitei325Cross-subunit contacts with tRNA(Thr)1 Publication1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi334ZincUniRule annotation4 Publications1
    Binding sitei363Contacts 3'-CCA of tRNA1 Publication1
    Binding sitei375Contacts 3'-CCA of tRNA1 Publication1
    Binding sitei376AMP; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
    Binding sitei379AMP1 Publication1
    Binding sitei381AMPCombined sources1 Publication1
    Metal bindingi385Zinc; via tele nitrogenUniRule annotation4 Publications1
    Binding sitei462Contacts 3'-CCA of tRNA1 Publication1
    Binding sitei484Contacts 3'-CCA of tRNA1 Publication1
    Metal bindingi511Zinc; via pros nitrogenUniRule annotation3 Publications1
    Binding sitei517AMPCombined sources1 Publication1
    Binding sitei520AMP1 Publication1
    Binding sitei589Contacts anticodon region of tRNA1 Publication1
    Binding sitei609Contacts anticodon region of tRNA1 Publication1
    Binding sitei609Contacts mRNA operator1 Publication1
    Binding sitei615Contacts mRNA operator1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi363 – 365AMPCombined sources1 Publication3
    Nucleotide bindingi479 – 480AMPCombined sources1 Publication2

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAminoacyl-tRNA synthetase, Ligase, Repressor, RNA-binding, tRNA-binding
    Biological processAntibiotic resistance, Protein biosynthesis, Translation regulation
    LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:THRS-MONOMER
    MetaCyc:THRS-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.1.1.3 2026

    Protein family/group databases

    MoonProt database of moonlighting proteins

    More...
    MoonProti
    P0A8M3

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Threonine--tRNA ligaseUniRule annotation (EC:6.1.1.3UniRule annotation1 Publication)
    Alternative name(s):
    Threonyl-tRNA synthetaseUniRule annotation
    Short name:
    ThrRSUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:thrSUniRule annotation
    Ordered Locus Names:b1719, JW1709
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG11001 thrS

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    A number of inhibitors with high affinity for bacterial ThrRS and less affinity for human ThrRS have been identified that might make good antibiotics.1 Publication

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Essential, it cannot be deleted.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi73 – 77HSCAH → ASCAA: No longer edits mischarged L-seryl-tRNA(Thr), mischarges tRNA(Thr) with L-serine, correct acylation is unaffected. 1 Publication5
    Mutagenesisi156K → A: Mischarges tRNA(Thr) with L-serine. 1 Publication1
    Mutagenesisi180D → A: No longer edits mischarged L-seryl-tRNA(Thr), mischarges tRNA(Thr) with L-serine, correct acylation is unaffected. 1 Publication1
    Mutagenesisi182C → A: Very high mischarging of tRNA(Thr) with L-serine. 1 Publication1
    Mutagenesisi186H → A: Mischarges tRNA(Thr) with L-serine. 1 Publication1
    Mutagenesisi296P → S: Confers resistance to borrelidin (BN); KM for L-Thr is unchanged, KM for ATP increases to 187 uM, KI for BN increases to 4.5 nM. 1 Publication1
    Mutagenesisi307T → A: KI for BN increases 10-fold, no change in aminoacylation activity. 1 Publication1
    Mutagenesisi309H → A: 10-fold increase in KM for Thr for activation, 240-fold decrease in aminoacyl transfer. Cells have a long lag phase and reach stationary phase at a lower cell density. KI for BN increases 1000-fold, supports growth in the presence of BN. 2 Publications1
    Mutagenesisi334C → S: Does not complement a deletion strain. 1 Publication1
    Mutagenesisi337H → A: KI for BN increases 12-fold, no change in aminoacylation activity, supports growth in the presence of BN. 1 Publication1
    Mutagenesisi363R → A: 700-fold decrease in kcat for Thr activation, 1000-fold decrease in kcat of aminoacylation, no change in KM. 1 Publication1
    Mutagenesisi381Q → A: 100-fold increase in KM for Thr for activation. 1 Publication1
    Mutagenesisi385H → A or N: Does not complement a deletion strain. 1 Publication1
    Mutagenesisi465K → A: 35-fold decrease in kcat for Thr activation, 570-fold decrease in kcat of aminoacylation, no change in KM. 1 Publication1
    Mutagenesisi479Q → A: Wild-type Thr activation and aminoacylation. 1 Publication1
    Mutagenesisi489L → M: Confers resistance to borrelidin (BN); KM for L-thr is unchanged, KM for ATP increases to 163 uM, KI for BN increases to 7.8 nM, supports growth in the presence of BN. 1 Publication1
    Mutagenesisi489L → W: KI for BN increases 1500-fold, no change in aminoacylation activity, supports growth in the presence of BN. 1 Publication1
    Mutagenesisi511H → A or N: Does not complement a deletion strain, has dominant lethal effect in presence of wild-type gene, probably due to repression of the wild-type gene. 1 Publication1
    Mutagenesisi531G → GEGK: KI for BN increases 8-fold, decreases aminoacylation activity, does not support growth in the presence of BN. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001009731 – 642Threonine--tRNA ligaseAdd BLAST642

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei286N6-acetyllysineUniRule annotation1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0A8M3

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P0A8M3

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A8M3

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P0A8M3

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer (PubMed:10319817, PubMed:11136973, PubMed:10881191, PubMed:11953757, PubMed:23362938, PubMed:25824639); binds 2 tRNA(Thr) per homodimer, each tRNA contacts both monomers and makes specific contacts with the anticodon and acceptor stems (PubMed:10319817).6 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    rplAP0A7L03EBI-551254,EBI-543771

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4262193, 27 interactors
    850582, 1 interactor

    Database of interacting proteins

    More...
    DIPi
    DIP-35823N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A8M3, 50 interactors

    Molecular INTeraction database

    More...
    MINTi
    P0A8M3

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_1855

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1642
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P0A8M3

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P0A8M3

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0A8M3

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 224Correctly edits mischarged seryl-tRNA(Thr)1 PublicationAdd BLAST224
    Regioni1 – 62N1 domain1 PublicationAdd BLAST62
    Regioni2 – 241N-terminal region which includes the editing domain, important for catalytic efficiency, its loss increases mischarging with L-serine, deacylation of incorrectly charged tRNA no longer occurs, partially complements a deletion strain1 PublicationAdd BLAST240
    Regioni63 – 224N2 domain, the editing domain1 PublicationAdd BLAST162
    Regioni200 – 219Contacts tRNA acceptor stem1 PublicationAdd BLAST20
    Regioni243 – 534CatalyticUniRule annotation1 PublicationAdd BLAST292
    Regioni246 – 249Contacts mRNA operator1 Publication4
    Regioni313 – 317Contacts 3'-CCA of tRNA1 Publication5
    Regioni342 – 349Contacts mRNA operator1 Publication8
    Regioni348 – 349Cross-subunit contacts with tRNA(Thr)1 Publication2
    Regioni489 – 503Contacts mRNA operator1 PublicationAdd BLAST15
    Regioni535 – 642Anticodon recognition1 PublicationAdd BLAST108
    Regioni547 – 549Contacts anticodon region of tRNA1 Publication3
    Regioni547 – 549Contacts mRNA operator1 Publication3
    Regioni575 – 586Contacts mRNA operator1 PublicationAdd BLAST12
    Regioni575 – 583Contacts anticodon region of tRNA1 Publication9
    Regioni595 – 600Contacts anticodon region of tRNA1 Publication6
    Regioni595 – 600Contacts mRNA operator1 Publication6

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The protein structure shows 2 N-terminal domains, the central catalytic and C-terminal domain (PubMed:10319817). The C-terminal domain recognizes the anticodon region of the tRNA while the acceptor arm is sandwiched between the N-terminal domains and the catalytic domain (PubMed:10319817). The N-terminal also contributes to the precise recognition of tRNA(Thr) (PubMed:10319817). The editing domain encompasses approximately residues 62-224; when it is removed the protein mischarges tRNA(Thr) with L-serine (PubMed:15079065, PubMed:11136973).2 Publications2 Publications

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the class-II aminoacyl-tRNA synthetase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105C22 Bacteria
    COG0441 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000003880

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A8M3

    KEGG Orthology (KO)

    More...
    KOi
    K01868

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A8M3

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00771 ThrRS_core, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.10.20.30, 1 hit
    3.40.50.800, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00184 Thr_tRNA_synth, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002314 aa-tRNA-synt_IIb
    IPR006195 aa-tRNA-synth_II
    IPR004154 Anticodon-bd
    IPR036621 Anticodon-bd_dom_sf
    IPR012675 Beta-grasp_dom_sf
    IPR004095 TGS
    IPR012676 TGS-like
    IPR002320 Thr-tRNA-ligase_IIa
    IPR018163 Thr/Ala-tRNA-synth_IIc_edit
    IPR033728 ThrRS_core
    IPR012947 tRNA_SAD

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11451 PTHR11451, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03129 HGTP_anticodon, 1 hit
    PF02824 TGS, 1 hit
    PF00587 tRNA-synt_2b, 1 hit
    PF07973 tRNA_SAD, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01047 TRNASYNTHTHR

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00863 tRNA_SAD, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55186 SSF55186, 1 hit
    SSF81271 SSF81271, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00418 thrS, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50862 AA_TRNA_LIGASE_II, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P0A8M3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPVITLPDGS QRHYDHAVSP MDVALDIGPG LAKACIAGRV NGELVDACDL
    60 70 80 90 100
    IENDAQLSII TAKDEEGLEI IRHSCAHLLG HAIKQLWPHT KMAIGPVIDN
    110 120 130 140 150
    GFYYDVDLDR TLTQEDVEAL EKRMHELAEK NYDVIKKKVS WHEARETFAN
    160 170 180 190 200
    RGESYKVSIL DENIAHDDKP GLYFHEEYVD MCRGPHVPNM RFCHHFKLMK
    210 220 230 240 250
    TAGAYWRGDS NNKMLQRIYG TAWADKKALN AYLQRLEEAA KRDHRKIGKQ
    260 270 280 290 300
    LDLYHMQEEA PGMVFWHNDG WTIFRELEVF VRSKLKEYQY QEVKGPFMMD
    310 320 330 340 350
    RVLWEKTGHW DNYKDAMFTT SSENREYCIK PMNCPGHVQI FNQGLKSYRD
    360 370 380 390 400
    LPLRMAEFGS CHRNEPSGSL HGLMRVRGFT QDDAHIFCTE EQIRDEVNGC
    410 420 430 440 450
    IRLVYDMYST FGFEKIVVKL STRPEKRIGS DEMWDRAEAD LAVALEENNI
    460 470 480 490 500
    PFEYQLGEGA FYGPKIEFTL YDCLDRAWQC GTVQLDFSLP SRLSASYVGE
    510 520 530 540 550
    DNERKVPVMI HRAILGSMER FIGILTEEFA GFFPTWLAPV QVVIMNITDS
    560 570 580 590 600
    QSEYVNELTQ KLSNAGIRVK ADLRNEKIGF KIREHTLRRV PYMLVCGDKE
    610 620 630 640
    VESGKVAVRT RRGKDLGSMD VNEVIEKLQQ EIRSRSLKQL EE
    Length:642
    Mass (Da):74,014
    Last modified:June 7, 2005 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i38D8913B19CDAB7B
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti195H → R in CAA23560 (PubMed:6353409).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    V00291 Genomic DNA Translation: CAA23560.1
    U00096 Genomic DNA Translation: AAC74789.1
    AP009048 Genomic DNA Translation: BAA15498.1
    M13549 Genomic DNA Translation: AAA24674.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    G64930 SYECTT

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416234.1, NC_000913.3
    WP_001144202.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74789; AAC74789; b1719
    BAA15498; BAA15498; BAA15498

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946222

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1709
    eco:b1719

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.538

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    V00291 Genomic DNA Translation: CAA23560.1
    U00096 Genomic DNA Translation: AAC74789.1
    AP009048 Genomic DNA Translation: BAA15498.1
    M13549 Genomic DNA Translation: AAA24674.1
    PIRiG64930 SYECTT
    RefSeqiNP_416234.1, NC_000913.3
    WP_001144202.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EVKX-ray2.00A/B242-642[»]
    1EVLX-ray1.55A/B/C/D242-642[»]
    1FYFX-ray1.65A/B242-642[»]
    1KOGX-ray3.50A/B/C/D/E/F/G/H242-642[»]
    1QF6X-ray2.90A1-642[»]
    1TJEX-ray1.50A1-224[»]
    1TKEX-ray1.46A1-224[»]
    1TKGX-ray1.50A1-224[»]
    1TKYX-ray1.48A1-224[»]
    4HWOX-ray1.91A/B242-642[»]
    4HWPX-ray1.81A/B242-642[»]
    4HWRX-ray1.90A/B242-642[»]
    4HWSX-ray1.70A/B242-642[»]
    4P3OX-ray2.50A/B242-642[»]
    4P3PX-ray2.10A/B242-642[»]
    ProteinModelPortaliP0A8M3
    SMRiP0A8M3
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262193, 27 interactors
    850582, 1 interactor
    DIPiDIP-35823N
    IntActiP0A8M3, 50 interactors
    MINTiP0A8M3
    STRINGi316385.ECDH10B_1855

    Protein family/group databases

    MoonProtiP0A8M3

    PTM databases

    iPTMnetiP0A8M3

    Proteomic databases

    EPDiP0A8M3
    PaxDbiP0A8M3
    PRIDEiP0A8M3

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74789; AAC74789; b1719
    BAA15498; BAA15498; BAA15498
    GeneIDi946222
    KEGGiecj:JW1709
    eco:b1719
    PATRICifig|1411691.4.peg.538

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0994
    EcoGeneiEG11001 thrS

    Phylogenomic databases

    eggNOGiENOG4105C22 Bacteria
    COG0441 LUCA
    HOGENOMiHOG000003880
    InParanoidiP0A8M3
    KOiK01868
    PhylomeDBiP0A8M3

    Enzyme and pathway databases

    BioCyciEcoCyc:THRS-MONOMER
    MetaCyc:THRS-MONOMER
    BRENDAi6.1.1.3 2026

    Miscellaneous databases

    EvolutionaryTraceiP0A8M3

    Protein Ontology

    More...
    PROi
    PR:P0A8M3

    Family and domain databases

    CDDicd00771 ThrRS_core, 1 hit
    Gene3Di3.10.20.30, 1 hit
    3.40.50.800, 1 hit
    HAMAPiMF_00184 Thr_tRNA_synth, 1 hit
    InterProiView protein in InterPro
    IPR002314 aa-tRNA-synt_IIb
    IPR006195 aa-tRNA-synth_II
    IPR004154 Anticodon-bd
    IPR036621 Anticodon-bd_dom_sf
    IPR012675 Beta-grasp_dom_sf
    IPR004095 TGS
    IPR012676 TGS-like
    IPR002320 Thr-tRNA-ligase_IIa
    IPR018163 Thr/Ala-tRNA-synth_IIc_edit
    IPR033728 ThrRS_core
    IPR012947 tRNA_SAD
    PANTHERiPTHR11451 PTHR11451, 1 hit
    PfamiView protein in Pfam
    PF03129 HGTP_anticodon, 1 hit
    PF02824 TGS, 1 hit
    PF00587 tRNA-synt_2b, 1 hit
    PF07973 tRNA_SAD, 1 hit
    PRINTSiPR01047 TRNASYNTHTHR
    SMARTiView protein in SMART
    SM00863 tRNA_SAD, 1 hit
    SUPFAMiSSF55186 SSF55186, 1 hit
    SSF81271 SSF81271, 1 hit
    TIGRFAMsiTIGR00418 thrS, 1 hit
    PROSITEiView protein in PROSITE
    PS50862 AA_TRNA_LIGASE_II, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSYT_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A8M3
    Secondary accession number(s): P00955, P78166, P78241
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: June 7, 2005
    Last modified: December 5, 2018
    This is version 129 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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