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 - P00962 (SYQ_ECOLI)

Protein

Glutamine--tRNA ligase

Gene

glnS

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

<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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei67L-glutamineUniRule annotationCombined sources3 Publications1
Binding sitei212L-glutamineUniRule annotationCombined sources4 Publications1
Binding sitei231ATPUniRule annotationCombined sources3 Publications1

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 bindingi35 – 37ATPUniRule annotationCombined sources1 Publication3
Nucleotide bindingi41 – 47ATPUniRule annotationCombined sources1 Publication7
Nucleotide bindingi261 – 262ATPUniRule annotationCombined sources3 Publications2
Nucleotide bindingi269 – 271ATPUniRule annotationCombined sources3 Publications3

<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

  • ATP binding Source: UniProtKB-UniRule
  • glutamine-tRNA ligase activity Source: EcoCyc
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		6.1.1.18 2026
6.1.1.24 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P00962

<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:
Glutamine--tRNA ligaseUniRule annotation (EC:6.1.1.18UniRule annotation5 Publications)
Alternative name(s):
Glutaminyl-tRNA synthetaseUniRule annotation
Short name:
GlnRSUniRule 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:glnSUniRule annotation
Ordered Locus Names:b0680, JW0666
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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		EG10390 glnS

<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

View the complete GO annotation on QuickGO ...

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>Mutagenesisi31R → A or K: Decreased affinity for glutamine and catalytic activity. 1 Publication1
Mutagenesisi230C → R: Decreases catalytic activity 1000-fold, but has no effect on affinity for glutamine. Loss of catalytic activity; when associated with I-256. 1 Publication1
Mutagenesisi256Q → I: Loss of catalytic activity; when associated with R-230. 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 <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 methionineiRemoved2 Publications
<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_00001958332 – 554Glutamine--tRNA ligaseAdd BLAST553

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P00962

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

More...PaxDbi		P00962

PRoteomics IDEntifications database

More...PRIDEi		P00962

2D gel databases

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

More...SWISS-2DPAGEi		P00962

<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

Monomer.UniRule annotation

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4261207, 52 interactors

Database of interacting proteins

More...DIPi		DIP-9787N

Protein interaction database and analysis system

More...IntActi		P00962, 5 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_0745

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P00962

<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

1554
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		P00962

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

More...SMRi		P00962

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		P00962

<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>Regioni317 – 324Interaction with tRNAUniRule annotation2 Publications8

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>Motifi34 – 44"HIGH" regionUniRule annotationAdd BLAST11
Motifi268 – 272"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.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105CX6 Bacteria
COG0008 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000259232

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00962

KEGG Orthology (KO)

More...KOi		K01886

Database for complete collections of gene phylogenies

More...PhylomeDBi		P00962

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1160.10, 1 hit
2.40.240.10, 2 hits
3.40.50.620, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00126 Gln_tRNA_synth, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001412 aa-tRNA-synth_I_CS
IPR004514 Gln-tRNA-synth
IPR022861 Gln_tRNA_ligase_bac
IPR000924 Glu/Gln-tRNA-synth
IPR020058 Glu/Gln-tRNA-synth_Ib_cat-dom
IPR020059 Glu/Gln-tRNA-synth_Ib_codon-bd
IPR020061 Glu_tRNA_lig_a-bdl
IPR020056 Rbsml_L25/Gln-tRNA_synth_N
IPR011035 Ribosomal_L25/Gln-tRNA_synth
IPR014729 Rossmann-like_a/b/a_fold

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00749 tRNA-synt_1c, 1 hit
PF03950 tRNA-synt_1c_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00987 TRNASYNTHGLU

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50715 SSF50715, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00440 glnS, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00178 AA_TRNA_LIGASE_I, 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.

<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.

P00962-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL 
        60         70         80         90        100
NFGIAQDYKG QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS 
       110        120        130        140        150
SDYFDQLHAY AIELINKGLA YVDELTPEQI REYRGTLTQP GKNSPYRDRS 
       160        170        180        190        200
VEENLALFEK MRAGGFEEGK ACLRAKIDMA SPFIVMRDPV LYRIKFAEHH 
       210        220        230        240        250
QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL YDWVLDNITI 
       260        270        280        290        300
PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR 
       310        320        330        340        350
GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV 
       360        370        380        390        400
KLVIENYQGE GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ 
       410        420        430        440        450
YKRLVLGKEV RLRNAYVIKA ERVEKDAEGN ITTIFCTYDA DTLSKDPADG 
       460        470        480        490        500
RKVKGVIHWV SAAHALPVEI RLYDRLFSVP NPGAADDFLS VINPESLVIK 
       510        520        530        540        550
QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN RTVGLRDTWA 

KVGE
Length:554
Mass (Da):63,478
Last modified:January 23, 2007 - v3
<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:iE720164EF990F335
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 conflicti549 – 554WAKVGE → GRK (PubMed:6288695).Curated6

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
V01575 Genomic DNA Translation: CAA24894.1
U00096 Genomic DNA Translation: AAC73774.1
AP009048 Genomic DNA Translation: BAA35328.1
M16470, M16368 Genomic DNA Translation: AAA69006.1

Protein sequence database of the Protein Information Resource

More...PIRi		G64802 SYECQT
I41235

NCBI Reference Sequences

More...RefSeqi		NP_415206.1, NC_000913.3
WP_001287154.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73774; AAC73774; b0680
BAA35328; BAA35328; BAA35328

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945310

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0666
eco:b0680

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1596

<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
V01575 Genomic DNA Translation: CAA24894.1
U00096 Genomic DNA Translation: AAC73774.1
AP009048 Genomic DNA Translation: BAA35328.1
M16470, M16368 Genomic DNA Translation: AAA69006.1
PIRiG64802 SYECQT
I41235
RefSeqiNP_415206.1, NC_000913.3
WP_001287154.1, NZ_LN832404.1

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
1EUQX-ray3.10A1-548[»]
1EUYX-ray2.60A1-548[»]
1EXDX-ray2.70A1-548[»]
1GSGX-ray2.80P2-554[»]
1GTRX-ray2.50A2-554[»]
1GTSX-ray2.80A2-554[»]
1NYLX-ray2.60A9-547[»]
1O0BX-ray2.70A2-554[»]
1O0CX-ray2.70A2-554[»]
1QRSX-ray2.60A2-554[»]
1QRTX-ray2.70A2-554[»]
1QRUX-ray3.00A2-554[»]
1QTQX-ray2.25A2-554[»]
1ZJWX-ray2.50A2-554[»]
2RD2X-ray2.60A1-548[»]
2RE8X-ray2.60A1-548[»]
4JXXX-ray2.30A2-554[»]
4JXZX-ray2.40A2-554[»]
4JYZX-ray2.50A2-554[»]
ProteinModelPortaliP00962
SMRiP00962
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261207, 52 interactors
DIPiDIP-9787N
IntActiP00962, 5 interactors
STRINGi316385.ECDH10B_0745

Chemistry databases

BindingDBiP00962

2D gel databases

SWISS-2DPAGEiP00962

Proteomic databases

EPDiP00962
PaxDbiP00962
PRIDEiP00962

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73774; AAC73774; b0680
BAA35328; BAA35328; BAA35328
GeneIDi945310
KEGGiecj:JW0666
eco:b0680
PATRICifig|1411691.4.peg.1596

Organism-specific databases

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

More...EchoBASEi		EB0385
EcoGeneiEG10390 glnS

Phylogenomic databases

eggNOGiENOG4105CX6 Bacteria
COG0008 LUCA
HOGENOMiHOG000259232
InParanoidiP00962
KOiK01886
PhylomeDBiP00962

Enzyme and pathway databases

BioCyciEcoCyc:GLNS-MONOMER
MetaCyc:GLNS-MONOMER
BRENDAi6.1.1.18 2026
6.1.1.24 2026
SABIO-RKiP00962

Miscellaneous databases

EvolutionaryTraceiP00962

Protein Ontology

More...PROi		PR:P00962

Family and domain databases

Gene3Di1.10.1160.10, 1 hit
2.40.240.10, 2 hits
3.40.50.620, 1 hit
HAMAPiMF_00126 Gln_tRNA_synth, 1 hit
InterProiView protein in InterPro
IPR001412 aa-tRNA-synth_I_CS
IPR004514 Gln-tRNA-synth
IPR022861 Gln_tRNA_ligase_bac
IPR000924 Glu/Gln-tRNA-synth
IPR020058 Glu/Gln-tRNA-synth_Ib_cat-dom
IPR020059 Glu/Gln-tRNA-synth_Ib_codon-bd
IPR020061 Glu_tRNA_lig_a-bdl
IPR020056 Rbsml_L25/Gln-tRNA_synth_N
IPR011035 Ribosomal_L25/Gln-tRNA_synth
IPR014729 Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF00749 tRNA-synt_1c, 1 hit
PF03950 tRNA-synt_1c_C, 1 hit
PRINTSiPR00987 TRNASYNTHGLU
SUPFAMiSSF50715 SSF50715, 1 hit
TIGRFAMsiTIGR00440 glnS, 1 hit
PROSITEiView protein in PROSITE
PS00178 AA_TRNA_LIGASE_I, 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 nameiSYQ_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: P00962
Secondary accession number(s): Q59403
<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: December 5, 2018
This is version 190 of the entry and version 3 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
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