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Entry version 128 (07 Oct 2020)
Sequence version 1 (21 Jul 1986)
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Protein

Tyrosine--tRNA ligase

Gene

tyrS

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
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 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).

<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 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

  1. KM=1.35 mM for ATP1 Publication
  2. KM=1.8 µM for 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 sitei34TyrosineBy similarity1
    Binding sitei169TyrosineBy similarity1
    Binding sitei173TyrosineBy similarity1
    Binding sitei233ATPBy similarity1

    <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

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.1.1.1, 623

    <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 ligase (EC:6.1.1.1)
    Alternative name(s):
    Tyrosyl-tRNA synthetase
    Short name:
    TyrRS
    <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:tyrS
    <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>OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    <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 identifieri1422 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    <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%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>Mutagenesisi40T → A: Destabilizes the transition states for both steps of the reaction. 1 Publication1
    Mutagenesisi45H → A: Does not affect the second step of the reaction. 2 Publications1
    Mutagenesisi45H → N: Decreases the rate of formation of Tyr-AMP and, as a consequence, abolishes the aminoacylation activity. Strongly increases the toxicity; when associated with A-152. 2 Publications1
    Mutagenesisi48H → A: Does not affect the second step of the reaction. 1 Publication1
    Mutagenesisi78D → A: Does not affect the initial binding of tRNA(Tyr) and the stability of the transition state for the second step of the reaction. 1 Publication1
    Mutagenesisi82K → A: Destabilizes the transition states for both steps of the reaction. 1 Publication1
    Mutagenesisi86R → A: Destabilizes the transition states for both steps of the reaction. 1 Publication1
    Mutagenesisi152E → A: Mischarges tRNA(Phe) with tyrosine in vitro. Toxic for the cell, probably because it alters the discrimination of TyrRS against non-cognate tRNAs. The toxicity is abolished; when associated with N-410 or N-411. Strongly increases toxicity; when associated with N-45. Enhances the toxicity; when associated with A-224. 1 Publication1
    Mutagenesisi152E → D: Does not charge tRNA(Phe) in vitro with tyrosine. 1 Publication1
    Mutagenesisi152E → Q: Mischarges tRNA(Phe) with tyrosine in vitro but this mutation is not toxic in vivo. 1 Publication1
    Mutagenesisi169Y → A: Does not affect the initial binding of tRNA(Tyr) and the stability of the transition state for the second step of the reaction. 1 Publication1
    Mutagenesisi173Q → A: Destabilizes the transition state for the second step of the reaction. 1 Publication1
    Mutagenesisi194D → A: Destabilizes the transition state for the first step of the reaction, but does not affect the transition state for the second step. 1 Publication1
    Mutagenesisi195Q → A: Destabilizes the transition state for the first step of the reaction, but does not affect the transition state for the second step. 1 Publication1
    Mutagenesisi224T → A: Is not toxic in itself. Enhances the toxicity; when associated with A-152. 1 Publication1
    Mutagenesisi230K → A: Decreases the binding affinity between tRNA(Tyr) and TyrRS-Tyr-AMP complex. 1 Publication1
    Mutagenesisi231F → L: No effect on the binding affinity between tRNA(Tyr) and TyrRS-Tyr-AMP complex. 1 Publication1
    Mutagenesisi232G → A: No effect on the binding affinity between tRNA(Tyr) and TyrRS-Tyr-AMP complex. 1 Publication1
    Mutagenesisi233K → A: Decreases the binding affinity between tRNA(Tyr) and TyrRS-Tyr-AMP complex. 1 Publication1
    Mutagenesisi234T → A: No effect on the binding affinity between tRNA(Tyr) and TyrRS-Tyr-AMP complex. 1 Publication1
    Mutagenesisi322L → P: 50-fold decrease in charging of tRNA(Tyr) with tyrosine. 1 Publication1
    Mutagenesisi323F → A: 90-fold decrease in charging of tRNA(Tyr) with tyrosine, without effect on the first step of the reaction. 1 Publication1
    Mutagenesisi323F → L: 67-fold decrease in charging of tRNA(Tyr) with tyrosine, without effect on the first step of the reaction. 1 Publication1
    Mutagenesisi323F → W: Weak decrease in charging of tRNA(Tyr) with tyrosine, without effect on the first step of the reaction. 1 Publication1
    Mutagenesisi323F → Y: 3-fold decrease in charging of tRNA(Tyr) with tyrosine, without effect on the first step of the reaction. 1 Publication1
    Mutagenesisi324S → A: 2-fold increase in charging of tRNA(Tyr) with tyrosine. 1 Publication1
    Mutagenesisi325G → A: 5-fold increase in charging of tRNA(Tyr) with tyrosine. 1 Publication1
    Mutagenesisi339F → L: Has no effect on charging of tRNA(Tyr) with tyrosine. 1 Publication1
    Mutagenesisi410K → N: Decreases the binding of tRNA(Tyr), without affecting the formation of Tyr-AMP. Abolishes the toxicity; when associated with A-152. 1 Publication1
    Mutagenesisi411K → N: Decreases the binding of tRNA(Tyr), without affecting the formation of Tyr-AMP. Abolishes the toxicity; when associated with A-152. 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_00000556421 – 419Tyrosine--tRNA ligaseAdd BLAST419

    <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.

    GO - Molecular functioni

    <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

    1419
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Biological Magnetic Resonance Data Bank

    More...
    BMRBi
    P00952

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

    More...
    SMRi
    P00952

    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
    P00952

    <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>Domaini352 – 419S4 RNA-bindingAdd BLAST68

    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>Motifi39 – 48'HIGH' region10
    Motifi230 – 234'KMSKS' region5

    <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

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00165, S4, 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.

    P00952-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MDLLAELQWR GLVNQTTDED GLRKLLNEER VTLYCGFDPT ADSLHIGHLA
    60 70 80 90 100
    TILTMRRFQQ AGHRPIALVG GATGLIGDPS GKKSERTLNA KETVEAWSAR
    110 120 130 140 150
    IKEQLGRFLD FEADGNPAKI KNNYDWIGPL DVITFLRDVG KHFSVNYMMA
    160 170 180 190 200
    KESVQSRIET GISFTEFSYM MLQAYDFLRL YETEGCRLQI GGSDQWGNIT
    210 220 230 240 250
    AGLELIRKTK GEARAFGLTI PLVTKADGTK FGKTESGTIW LDKEKTSPYE
    260 270 280 290 300
    FYQFWINTDD RDVIRYLKYF TFLSKEEIEA LEQELREAPE KRAAQKTLAE
    310 320 330 340 350
    EVTKLVHGEE ALRQAIRISE ALFSGDIANL TAAEIEQGFK DVPSFVHEGG
    360 370 380 390 400
    DVPLVELLVS AGISPSKRQA REDIQNGAIY VNGERLQDVG AILTAEHRLE
    410
    GRFTVIRRGK KKYYLIRYA
    Length:419
    Mass (Da):47,303
    Last modified:July 21, 1986 - 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:iB9CB64AEEEE2010F
    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
    J01546 Genomic DNA No translation available.
    X04193 Genomic DNA Translation: CAA27784.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A01179, SYBSYF

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_033014498.1, NZ_RCTK01000009.1

    <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
    J01546 Genomic DNA No translation available.
    X04193 Genomic DNA Translation: CAA27784.1
    PIRiA01179, SYBSYF
    RefSeqiWP_033014498.1, NZ_RCTK01000009.1

    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
    1JH3NMR-A321-419[»]
    1TYAX-ray2.80E1-319[»]
    1TYBX-ray2.50E1-319[»]
    1TYCX-ray2.50A1-319[»]
    1TYDX-ray2.50E1-319[»]
    2TS1X-ray2.30A1-419[»]
    3TS1X-ray2.70A1-419[»]
    4TS1X-ray2.50A/B1-317[»]
    BMRBiP00952
    SMRiP00952
    ModBaseiSearch...
    PDBe-KBiSearch...

    Enzyme and pathway databases

    BRENDAi6.1.1.1, 623

    Miscellaneous databases

    EvolutionaryTraceiP00952

    Family and domain databases

    CDDicd00165, S4, 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_GEOSE
    <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: P00952
    <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: July 21, 1986
    Last modified: October 7, 2020
    This is version 128 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

    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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