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Entry version 148 (23 Feb 2022)
Sequence version 1 (07 Jun 2005)
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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%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sec(-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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei309Adenosine residue; binds 2'-OH of adenine 76 of tRNA(Thr), the tRNA acceptor baseCombined sources1 Publication1
Binding sitei325tRNA(Thr)1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei3633'-CCA residue; binds 3'-CCA of tRNA1 Publication1
Binding sitei3753'-CCA residue; binds 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 sitei4623'-CCA residue; binds 3'-CCA of tRNA1 Publication1
Binding sitei4843'-CCA residue; binds 3'-CCA of tRNA1 Publication1
Metal bindingi511Zinc; via pros nitrogenUniRule annotation3 Publications1
Binding sitei517AMPCombined sources1 Publication1
Binding sitei520AMP1 Publication1
Binding sitei589tRNA; binds anticodon region of tRNA1 Publication1
Binding sitei609mRNA; binds mRNA operator1 Publication1
Binding sitei609tRNA; binds anticodon region of tRNA1 Publication1
Binding sitei615mRNA; binds mRNA operator1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.1.1.3, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0A8M3

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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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

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%5Fand%5Fbiotech%5Fsection">'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 or proteolytic cleavage.<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

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P0A8M3

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

More...
PaxDbi
P0A8M3

PRoteomics IDEntifications database

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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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262193, 27 interactors
850582, 2 interactors

Database of interacting proteins

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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
511145.b1719

<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

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

More...
SMRi
P0A8M3

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 61TGSPROSITE-ProRule annotationAdd BLAST61

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 – 219tRNA binding; binds tRNA acceptor stem1 PublicationAdd BLAST20
Regioni243 – 534CatalyticUniRule annotation1 PublicationAdd BLAST292
Regioni246 – 249mRNA binding; binds mRNA operator1 Publication4
Regioni313 – 3173'-CCA residue binding; binds 3'-CCA of tRNA1 Publication5
Regioni342 – 349mRNA binding; binds mRNA operator1 Publication8
Regioni348 – 349tRNA(Thr) binding1 Publication2
Regioni489 – 503mRNA binding; binds mRNA operator1 PublicationAdd BLAST15
Regioni535 – 642Anticodon recognition1 PublicationAdd BLAST108
Regioni547 – 549mRNA binding; binds mRNA operator1 Publication3
Regioni547 – 549tRNA binding; binds anticodon region of tRNA1 Publication3
Regioni575 – 586mRNA binding; binds mRNA operator1 PublicationAdd BLAST12
Regioni575 – 583tRNA binding; binds anticodon region of tRNA1 Publication9
Regioni595 – 600mRNA binding; binds mRNA operator1 Publication6
Regioni595 – 600tRNA binding; binds anticodon region of tRNA1 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
COG0441, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_008554_0_1_6

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0A8M3

Database for complete collections of gene phylogenies

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PhylomeDBi
P0A8M3

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00771, ThrRS_core, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.10.20.30, 1 hit
3.30.930.10, 1 hit
3.40.50.800, 1 hit

HAMAP database of protein families

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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
IPR045864, aa-tRNA-synth_II/BPL/LPL
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

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PANTHERi
PTHR11451, PTHR11451, 1 hit

Pfam protein domain database

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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

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PRINTSi
PR01047, TRNASYNTHTHR

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00863, tRNA_SAD, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55186, SSF55186, 1 hit
SSF55681, SSF55681, 1 hit
SSF81271, SSF81271, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00418, thrS, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50862, AA_TRNA_LIGASE_II, 1 hit
PS51880, TGS, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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

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EMBLi

GenBank nucleotide sequence database

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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

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PIRi
G64930, SYECTT

NCBI Reference Sequences

More...
RefSeqi
NP_416234.1, NC_000913.3
WP_001144202.1, NZ_SSZK01000001.1

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

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GeneIDi
58460397
946222

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1709
eco:b1719

Pathosystems Resource Integration Center (PATRIC)

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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_SSZK01000001.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
SMRiP0A8M3
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262193, 27 interactors
850582, 2 interactors
DIPiDIP-35823N
IntActiP0A8M3, 50 interactors
MINTiP0A8M3
STRINGi511145.b1719

Protein family/group databases

MoonProtiP0A8M3

PTM databases

iPTMnetiP0A8M3

Proteomic databases

jPOSTiP0A8M3
PaxDbiP0A8M3
PRIDEiP0A8M3

Genome annotation databases

EnsemblBacteriaiAAC74789; AAC74789; b1719
BAA15498; BAA15498; BAA15498
GeneIDi58460397
946222
KEGGiecj:JW1709
eco:b1719
PATRICifig|1411691.4.peg.538

Organism-specific databases

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

More...
EchoBASEi
EB0994

Phylogenomic databases

eggNOGiCOG0441, Bacteria
HOGENOMiCLU_008554_0_1_6
InParanoidiP0A8M3
PhylomeDBiP0A8M3

Enzyme and pathway databases

BioCyciEcoCyc:THRS-MONOMER
BRENDAi6.1.1.3, 2026
SABIO-RKiP0A8M3

Miscellaneous databases

EvolutionaryTraceiP0A8M3

Protein Ontology

More...
PROi
PR:P0A8M3

Family and domain databases

CDDicd00771, ThrRS_core, 1 hit
Gene3Di3.10.20.30, 1 hit
3.30.930.10, 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
IPR045864, aa-tRNA-synth_II/BPL/LPL
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
SSF55681, SSF55681, 1 hit
SSF81271, SSF81271, 1 hit
TIGRFAMsiTIGR00418, thrS, 1 hit
PROSITEiView protein in PROSITE
PS50862, AA_TRNA_LIGASE_II, 1 hit
PS51880, TGS, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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%5Fand%5Fisoforms">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: February 23, 2022
This is version 148 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, Reference proteome

Documents

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