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Entry version 124 (16 Oct 2019)
Sequence version 2 (23 Jan 2007)
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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_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 <a href="http://www.uniprot.org/help/function_section">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_section">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

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:TYRS-MONOMER
ECOL316407:JW1629-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_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:
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_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:tyrS1 Publication
Ordered Locus Names:b1637, JW1629
<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
EG11043 tyrS

<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

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_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>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

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_processing_section">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.<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_processing_section">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

Encyclopedia of Proteome Dynamics

More...
EPDi
P0AGJ9

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_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: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

<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_and_domains_section">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
ENOG4105DA0 Bacteria
COG0162 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000242790

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AGJ9

KEGG Orthology (KO)

More...
KOi
K01866

Database for complete collections of gene phylogenies

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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

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HAMAPi
MF_02006 Tyr_tRNA_synth_type1, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR11766 PTHR11766, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01040 TRNASYNTHTYR

Simple Modular Architecture Research Tool; a protein domain database

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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_length">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_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.

<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 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

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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

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GeneIDi
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

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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[»]
SMRiP0AGJ9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4263487, 47 interactors
DIPiDIP-36227N
IntActiP0AGJ9, 8 interactors
STRINGi511145.b1637

Chemistry databases

DrugBankiDB01758 3-Iodo-Tyrosine
DB03325 Tyrosyladenylate

PTM databases

iPTMnetiP0AGJ9

2D gel databases

SWISS-2DPAGEiP0AGJ9

Proteomic databases

EPDiP0AGJ9
jPOSTiP0AGJ9
PaxDbiP0AGJ9
PRIDEiP0AGJ9

Genome annotation databases

EnsemblBacteriaiAAC74709; AAC74709; b1637
BAA15398; BAA15398; BAA15398
GeneIDi948855
KEGGiecj:JW1629
eco:b1637
PATRICifig|1411691.4.peg.623

Organism-specific databases

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

More...
EchoBASEi
EB1036
EcoGeneiEG11043 tyrS

Phylogenomic databases

eggNOGiENOG4105DA0 Bacteria
COG0162 LUCA
HOGENOMiHOG000242790
InParanoidiP0AGJ9
KOiK01866
PhylomeDBiP0AGJ9

Enzyme and pathway databases

BioCyciEcoCyc:TYRS-MONOMER
ECOL316407:JW1629-MONOMER
MetaCyc:TYRS-MONOMER
BRENDAi6.1.1.1 2026
SABIO-RKiP0AGJ9

Miscellaneous databases

EvolutionaryTraceiP0AGJ9

Protein Ontology

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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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_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: January 23, 2007
Last modified: October 16, 2019
This is version 124 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, Complete proteome, Direct protein sequencing, 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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