Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P0AGJ9 (SYY_ECOLI)

Entry version 133 (07 Apr 2021)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Tyrosine--tRNA ligase

Gene

tyrS

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 L-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) (PubMed:4292198, PubMed:4579631). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase (PubMed:4292198). In vitro, can also use the non-natural amino acid azatyrosine (PubMed:11006270).3 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 <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

Magnesium is essential for activity (PubMed:4579631). Inhibited by chloride and sulfate in the presence of 1 mM free Mg2+. When the Mg2+ concentration increases to 10 mM there is almost no chloride inhibition any more. Inhibited by diphosphate and AMP. Chloride strengthens the diphosphate inhibition and weakens the AMP inhibition. Chloride weakens the binding of Mg2+ to the RNA and thereby the interaction between the enzyme and the RNA (PubMed:10572925). Acetylation at certain lysine residues could significantly impair activity (PubMed:28741290). D-tyrosine is a competitive inhibitor of L-tyrosine for the formation of tyrosyl-tRNA(Tyr) (PubMed:4292198).4 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 0.74 sec(-1) with L-tyrosine as substrate. kcat is 0.11 sec(-1) with azatyrosine as substrate.1 Publication
  1. KM=0.027 mM for L-tyrosine1 Publication
  2. KM=0.0033 mM for L-tyrosine1 Publication
  3. KM=0.015 mM for D-tyrosine1 Publication
  4. KM=0.0177 mM for azatyrosine1 Publication
  5. KM=22 nM for tRNA(Tyr) (in the absence of KCl)1 Publication
  6. KM=37 nM for tRNA(Tyr) (in the presence of 50 mM KCl)1 Publication
  7. KM=93 nM for tRNA(Tyr) (in the presence of 100 mM KCl)1 Publication
  8. KM=240 nM for tRNA(Tyr) (in the presence of 150 mM KCl)1 Publication
  1. Vmax=2.6 µmol/min/mg enzyme for L-tyrosine1 Publication
  2. Vmax=0.11 µmol/min/mg enzyme for D-tyrosine1 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 sitei37TyrosineUniRule annotation1 Publication1 Publication1
Binding sitei175TyrosineUniRule annotation1 Publication2 Publications1
Binding sitei179TyrosineUniRule annotation1 Publication2 Publications1
Binding sitei198Tyr-AMP intermediate adenyl group; via amide nitrogen1
Binding sitei200Tyr-AMP intermediate adenyl group1
Binding sitei228Tyr-AMP intermediate adenyl group; via amide nitrogen and carbonyl oxygen1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei231Cross-linked with tRNA by periodate oxidation1
Sitei235Cross-linked with tRNA by periodate oxidation; predominant1
Binding sitei238ATPUniRule annotation1
Sitei238Cross-linked with tRNA by periodate oxidation1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, RNA-binding
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		6.1.1.1, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P0AGJ9

<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:
Tyrosine--tRNA ligaseUniRule annotationCurated (EC:6.1.1.1UniRule annotation4 Publications)
Alternative name(s):
Tyrosyl-tRNA synthetase1 PublicationUniRule annotation
Short name:
TyrRS1 PublicationUniRule 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:tyrS1 Publication
Ordered Locus Names:b1637, JW1629
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

Utilization for in vivo protein biosynthesis of mutants that charge azatyrosine efficiently to tRNA may lead to efficient production of azatyrosine-containing alloproteins, which have immense potential in biotechnology and medicine.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>Mutagenesisi37Y → V: Confers specificity for the non-natural amino acid 3-iodo-tyrosine; when associated with C-195. 1 Publication1
Mutagenesisi130F → S: Utilizes the non-natural amino acid azatyrosine more efficiently than tyrosine. Strong decrease in affinity for tyrosine and small increase in affinity for azatyrosine. Temperature-sensitive. 1 Publication1
Mutagenesisi195Q → C: Confers specificity for the non-natural amino acid 3-iodo-tyrosine; when associated with V-37. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4295572

Drug and drug target database

More...DrugBanki		DB01758, 3-Iodo-Tyrosine
DB03325, Tyrosyladenylate

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00000556522 – 424Tyrosine--tRNA ligaseAdd BLAST423

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 residuei144N6-acetyllysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylated at Lys-144 (PubMed:18723842, PubMed:28741290). Acetylation at Lys-144 leads to slightly decreased activity (PubMed:28741290). In vitro, in the presence of acetyl-phosphate, can also be acetylated at Lys-67, Lys-85, Lys-90, Lys-230, Lys-235, Lys-238, Lys-321 and Lys-377. Acetylation at Lys-85, Lys-235 or Lys-238 causes dramatic decrease in activity (PubMed:28741290).2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0AGJ9

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

More...PaxDbi		P0AGJ9

PRoteomics IDEntifications database

More...PRIDEi		P0AGJ9

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P0AGJ9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0AGJ9

<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:4579631, PubMed:6754952, PubMed:15663931, PubMed:15671170). Binds one molecule of tRNA(Tyr) per homodimer (PubMed:6754952).

4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4263487, 47 interactors

Database of interacting proteins

More...DIPi		DIP-36227N

Protein interaction database and analysis system

More...IntActi		P0AGJ9, 8 interactors

STRING: functional protein association networks

More...STRINGi		511145.b1637

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0AGJ9

<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

1424
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		P0AGJ9

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		P0AGJ9

<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>Domaini357 – 414S4 RNA-bindingPROSITE-ProRule annotationAdd BLAST58

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi42 – 51'HIGH' regionUniRule annotation10
Motifi235 – 239'KMSKS' regionUniRule annotation5

<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-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0162, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0AGJ9

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0AGJ9

Family and domain databases

Conserved Domains Database

More...CDDi		cd00165, S4, 1 hit
cd00805, TyrRS_core, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.10.290.10, 1 hit
3.40.50.620, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_02006, Tyr_tRNA_synth_type1, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001412, aa-tRNA-synth_I_CS
IPR002305, aa-tRNA-synth_Ic
IPR014729, Rossmann-like_a/b/a_fold
IPR002942, S4_RNA-bd
IPR036986, S4_RNA-bd_sf
IPR002307, Tyr-tRNA-ligase
IPR024088, Tyr-tRNA-ligase_bac-type
IPR024107, Tyr-tRNA-ligase_bac_1

The PANTHER Classification System

More...PANTHERi		PTHR11766, PTHR11766, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01479, S4, 1 hit
PF00579, tRNA-synt_1b, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01040, TRNASYNTHTYR

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00363, S4, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00234, tyrS, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00178, AA_TRNA_LIGASE_I, 1 hit
PS50889, S4, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0AGJ9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASSNLIKQL QERGLVAQVT DEEALAERLA QGPIALYCGF DPTADSLHLG 
        60         70         80         90        100
HLVPLLCLKR FQQAGHKPVA LVGGATGLIG DPSFKAAERK LNTEETVQEW 
       110        120        130        140        150
VDKIRKQVAP FLDFDCGENS AIAANNYDWF GNMNVLTFLR DIGKHFSVNQ 
       160        170        180        190        200
MINKEAVKQR LNREDQGISF TEFSYNLLQG YDFACLNKQY GVVLQIGGSD 
       210        220        230        240        250
QWGNITSGID LTRRLHQNQV FGLTVPLITK ADGTKFGKTE GGAVWLDPKK 
       260        270        280        290        300
TSPYKFYQFW INTADADVYR FLKFFTFMSI EEINALEEED KNSGKAPRAQ 
       310        320        330        340        350
YVLAEQVTRL VHGEEGLQAA KRITECLFSG SLSALSEADF EQLAQDGVPM 
       360        370        380        390        400
VEMEKGADLM QALVDSELQP SRGQARKTIA SNAITINGEK QSDPEYFFKE 
       410        420 
EDRLFGRFTL LRRGKKNYCL ICWK
Length:424
Mass (Da):47,527
Last modified:January 23, 2007 - v2
<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:i98E7080D85B356A2
GO

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
J01719 Genomic DNA Translation: AAA24707.1
U00096 Genomic DNA Translation: AAC74709.1
AP009048 Genomic DNA Translation: BAA15398.1
M92351 Genomic DNA Translation: AAA24710.1

Protein sequence database of the Protein Information Resource

More...PIRi		A01178, SYECYT

NCBI Reference Sequences

More...RefSeqi		NP_416154.1, NC_000913.3
WP_001295400.1, NZ_STEB01000003.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74709; AAC74709; b1637
BAA15398; BAA15398; BAA15398

Database of genes from NCBI RefSeq genomes

More...GeneIDi		57731032
948855

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1629
eco:b1637

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.623

<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
J01719 Genomic DNA Translation: AAA24707.1
U00096 Genomic DNA Translation: AAC74709.1
AP009048 Genomic DNA Translation: BAA15398.1
M92351 Genomic DNA Translation: AAA24710.1
PIRiA01178, SYECYT
RefSeqiNP_416154.1, NC_000913.3
WP_001295400.1, NZ_STEB01000003.1

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
1VBMX-ray2.70A/B5-322[»]
1VBNX-ray2.70A/B5-322[»]
1WQ3X-ray2.00A1-322[»]
1WQ4X-ray2.00A2-322[»]
1X8XX-ray2.00A1-322[»]
2YXNX-ray1.80A1-322[»]
6HB5X-ray1.88A/B1-424[»]
6HB6X-ray1.92A/B1-424[»]
6HB7X-ray1.90A/B1-424[»]
6I5YX-ray1.90A/B1-424[»]
6WN2X-ray1.78A/B1-322[»]
7AP3X-ray2.00A/B1-424[»]
SMRiP0AGJ9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263487, 47 interactors
DIPiDIP-36227N
IntActiP0AGJ9, 8 interactors
STRINGi511145.b1637

Chemistry databases

BindingDBiP0AGJ9
ChEMBLiCHEMBL4295572
DrugBankiDB01758, 3-Iodo-Tyrosine
DB03325, Tyrosyladenylate

PTM databases

iPTMnetiP0AGJ9

2D gel databases

SWISS-2DPAGEiP0AGJ9

Proteomic databases

jPOSTiP0AGJ9
PaxDbiP0AGJ9
PRIDEiP0AGJ9

Genome annotation databases

EnsemblBacteriaiAAC74709; AAC74709; b1637
BAA15398; BAA15398; BAA15398
GeneIDi57731032
948855
KEGGiecj:JW1629
eco:b1637
PATRICifig|1411691.4.peg.623

Organism-specific databases

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

More...EchoBASEi		EB1036

Phylogenomic databases

eggNOGiCOG0162, Bacteria
InParanoidiP0AGJ9
PhylomeDBiP0AGJ9

Enzyme and pathway databases

BioCyciEcoCyc:TYRS-MONOMER
MetaCyc:TYRS-MONOMER
BRENDAi6.1.1.1, 2026
SABIO-RKiP0AGJ9

Miscellaneous databases

EvolutionaryTraceiP0AGJ9

Protein Ontology

More...PROi		PR:P0AGJ9

Family and domain databases

CDDicd00165, S4, 1 hit
cd00805, TyrRS_core, 1 hit
Gene3Di3.10.290.10, 1 hit
3.40.50.620, 1 hit
HAMAPiMF_02006, Tyr_tRNA_synth_type1, 1 hit
InterProiView protein in InterPro
IPR001412, aa-tRNA-synth_I_CS
IPR002305, aa-tRNA-synth_Ic
IPR014729, Rossmann-like_a/b/a_fold
IPR002942, S4_RNA-bd
IPR036986, S4_RNA-bd_sf
IPR002307, Tyr-tRNA-ligase
IPR024088, Tyr-tRNA-ligase_bac-type
IPR024107, Tyr-tRNA-ligase_bac_1
PANTHERiPTHR11766, PTHR11766, 1 hit
PfamiView protein in Pfam
PF01479, S4, 1 hit
PF00579, tRNA-synt_1b, 1 hit
PRINTSiPR01040, TRNASYNTHTYR
SMARTiView protein in SMART
SM00363, S4, 1 hit
TIGRFAMsiTIGR00234, tyrS, 1 hit
PROSITEiView protein in PROSITE
PS00178, AA_TRNA_LIGASE_I, 1 hit
PS50889, S4, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiSYY_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: P0AGJ9
Secondary accession number(s): P00951
<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: January 23, 2007
Last modified: April 7, 2021
This is version 133 of the entry and version 2 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, Direct protein sequencing, 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again