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Protein

Aspartate--tRNA(Asp) ligase

Gene

aspS

Organism
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
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-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). Is specific for tRNA(Asp) since it aspartylates tRNA(Asn) 3 orders of magnitude less efficiently than tRNA(Asp).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 ‘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

Mg2+UniRule annotation1 PublicationNote: Binds 3 Mg2+ cations per subunit. The strongest magnesium site (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water molecules complete its coordination sphere.UniRule annotation1 Publication

<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 0.061 sec(-1) for tRNA(Asp) aspartylation (at 60 degrees Celsius).
  1. KM=1.4 µM for tRNA(Asp) (at 60 degrees Celsius)1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Sitei26Important for tRNA discrimination1
    Sitei85Important for tRNA discrimination1
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei170Aspartate1
    Binding sitei214Aspartate1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi361Magnesium 21
    Metal bindingi361Magnesium 31
    Binding sitei361ATP1
    Metal bindingi364Magnesium 21
    Binding sitei364Aspartate1
    Binding sitei368Aspartate1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi214 – 216ATP3
    Nucleotide bindingi222 – 224ATP3
    Nucleotide bindingi409 – 412ATP4

    <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

    • aspartate-tRNA ligase activity Source: GO_Central
    • ATP binding Source: UniProtKB-UniRule
    • magnesium ion binding Source: UniProtKB-UniRule
    • RNA binding Source: GO_Central

    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
    Biological processProtein biosynthesis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    TKOD69014:G1G2A-489-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.1.1.12 5246

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q52428

    <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:
    Aspartate--tRNA(Asp) ligaseUniRule annotation (EC:6.1.1.12UniRule annotation)
    Alternative name(s):
    Aspartyl-tRNA synthetaseUniRule annotation
    Short name:
    AspRSUniRule annotation
    Discriminating aspartyl-tRNA synthetaseUniRule annotation
    Short name:
    D-AspRSUniRule 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:aspSUniRule annotation
    Ordered Locus Names:TK0492
    <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>OrganismiThermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
    <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 identifieri69014 [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 lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
    <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
    • UP000000536 <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

    <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

    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>Mutagenesisi26W → H: Gains the ability to form Asp-tRNA(Asn) in vitro. Only 2-fold decrease in catalytic efficiency for Asp-tRNA(Asp) synthesis. 1 Publication1
    Mutagenesisi85K → P: Gains the ability to form Asp-tRNA(Asn) in vitro, and is impaired in its ability to synthesize Asp-tRNA(Asp) due to a 8-fold decrease in affinity for tRNA(Asp). 1 Publication1

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001110051 – 438Aspartate--tRNA(Asp) ligaseAdd BLAST438

    <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.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    69014.TK0492

    <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

    1438
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q52428

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

    More...
    SMRi
    Q52428

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q52428

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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni192 – 195Aspartate4

    <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. Type 2 subfamily.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    arCOG00406 Archaea
    COG0017 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000226032

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q52428

    KEGG Orthology (KO)

    More...
    KOi
    K22503

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    WVHEIRD

    Database of Orthologous Groups

    More...
    OrthoDBi
    POG093Z02FK

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_02075 Asp_tRNA_synth_type2, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR004364 aa-tRNA-synt_II
    IPR006195 aa-tRNA-synth_II
    IPR004523 Asp-tRNA_synthase_2
    IPR002312 Asp/Asn-tRNA-synth_IIb
    IPR012340 NA-bd_OB-fold
    IPR004365 NA-bd_OB_tRNA

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR43450 PTHR43450, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00152 tRNA-synt_2, 1 hit
    PF01336 tRNA_anti-codon, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01042 TRNASYNTHASP

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50249 SSF50249, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00458 aspS_nondisc, 1 hit

    PROSITE; a protein domain and family database

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

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

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

    Q52428-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MYRTHYSSEI TEELNGQKVK VAGWVWEVKD LGGIKFLWIR DRDGIVQITA
    60 70 80 90 100
    PKKKVDPELF KLIPKLRSED VVAVEGVVNF TPKAKLGFEI LPEKIVVLNR
    110 120 130 140 150
    AETPLPLDPT GKVKAELDTR LDNRFMDLRR PEVMAIFKIR SSVFKAVRDF
    160 170 180 190 200
    FHENGFIEIH TPKIIATATE GGTELFPMKY FEEDAFLAQS PQLYKQIMMA
    210 220 230 240 250
    SGLDRVYEIA PIFRAEEHNT TRHLNEAWSI DSEMAFIEDE EEVMSFLERL
    260 270 280 290 300
    VAHAINYVRE HNAKELDILN FELEEPKLPF PRVSYDKALE ILGDLGKEIP
    310 320 330 340 350
    WGEDIDTEGE RLLGKYMMEN ENAPLYFLYQ YPSEAKPFYI MKYDNKPEIC
    360 370 380 390 400
    RAFDLEYRGV EISSGGQREH RHDILVEQIK EKGLNPESFE FYLKAFRYGM
    410 420 430
    PPHGGFGLGA ERLIKQMLDL PNIREVILFP RDRRRLTP
    Length:438
    Mass (Da):50,910
    Last modified:March 29, 2005 - 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:iE03C8766ADD2209A
    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 conflicti413L → V in BAA08115 (PubMed:7590306).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    D45167 Genomic DNA Translation: BAA08115.1
    AP006878 Genomic DNA Translation: BAD84681.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011249447.1, NC_006624.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAD84681; BAD84681; TK0492

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    3235903

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    tko:TK0492

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|69014.16.peg.483

    <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
    D45167 Genomic DNA Translation: BAA08115.1
    AP006878 Genomic DNA Translation: BAD84681.1
    RefSeqiWP_011249447.1, NC_006624.1

    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
    1B8AX-ray1.90A/B1-438[»]
    3NELX-ray1.95A/B1-438[»]
    3NEMX-ray1.89A/B1-438[»]
    3NENX-ray2.40A/B1-438[»]
    ProteinModelPortaliQ52428
    SMRiQ52428
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi69014.TK0492

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAD84681; BAD84681; TK0492
    GeneIDi3235903
    KEGGitko:TK0492
    PATRICifig|69014.16.peg.483

    Phylogenomic databases

    eggNOGiarCOG00406 Archaea
    COG0017 LUCA
    HOGENOMiHOG000226032
    InParanoidiQ52428
    KOiK22503
    OMAiWVHEIRD
    OrthoDBiPOG093Z02FK

    Enzyme and pathway databases

    BioCyciTKOD69014:G1G2A-489-MONOMER
    BRENDAi6.1.1.12 5246
    SABIO-RKiQ52428

    Miscellaneous databases

    EvolutionaryTraceiQ52428

    Family and domain databases

    HAMAPiMF_02075 Asp_tRNA_synth_type2, 1 hit
    InterProiView protein in InterPro
    IPR004364 aa-tRNA-synt_II
    IPR006195 aa-tRNA-synth_II
    IPR004523 Asp-tRNA_synthase_2
    IPR002312 Asp/Asn-tRNA-synth_IIb
    IPR012340 NA-bd_OB-fold
    IPR004365 NA-bd_OB_tRNA
    PANTHERiPTHR43450 PTHR43450, 1 hit
    PfamiView protein in Pfam
    PF00152 tRNA-synt_2, 1 hit
    PF01336 tRNA_anti-codon, 1 hit
    PRINTSiPR01042 TRNASYNTHASP
    SUPFAMiSSF50249 SSF50249, 1 hit
    TIGRFAMsiTIGR00458 aspS_nondisc, 1 hit
    PROSITEiView protein in PROSITE
    PS50862 AA_TRNA_LIGASE_II, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

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

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSYD_THEKO
    <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: Q52428
    Secondary accession number(s): Q5JD76
    <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: November 1, 1997
    Last sequence update: March 29, 2005
    Last modified: December 5, 2018
    This is version 140 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, 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
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