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UniProtKB - P00956 (SYI_ECOLI)

Entry version 203 (23 Feb 2022)
Sequence version 5 (23 Jan 2007)
Previous versions | rss
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Protein

Isoleucine--tRNA ligase

Gene

ileS

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 isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).

Miscellaneous

Strain PS102 is resistant to the antibiotic mupirocin (pseudomonic acid A), an Ile-analog that competitively inhibits activation by Ile-tRNA synthetase, thus inhibiting protein biosynthesis.

<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 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

Zn2+Note: Binds 1 zinc ion per subunit.

<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=5 µM for isoleucine1 Publication
  2. KM=0.4 mM for ATP1 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 sitei561Isoleucyl-adenylateBy similarity1
Binding sitei605ATPBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi901ZincBy similarity1
Metal bindingi904ZincBy similarity1
Metal bindingi921ZincBy similarity1
Metal bindingi924ZincBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase
Biological processAntibiotic resistance, Protein biosynthesis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:ILES-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		6.1.1.5, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P00956

<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:
Isoleucine--tRNA ligase (EC:6.1.1.5)
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name:
IleRS
<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:ileS
Synonyms:ilvS
Ordered Locus Names:b0026, JW0024
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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>Mutagenesisi94G → R: 6000-fold increase in Km for isoleucine and 4-fold increase in Km for ATP, with no effect on activity. 1 Publication1
Mutagenesisi97C → S: No effect on activity. 1 Publication1
Mutagenesisi102I → N: No significant effect on activity. 1 Publication1
Mutagenesisi183K → A: Abolishes translocation from the aminoacylation site to the editing site, without effect on aminoacylation activity and posttransfer editing; when associated with A-421. 1 Publication1
Mutagenesisi241T → A: Nearly the same editing activity as the wild-type. 1 Publication1
Mutagenesisi242T → A: Abolishes editing activity against valine, with little change in aminoacylation activity; when associated with A-250. 1 Publication1
Mutagenesisi242T → P: Abolishes editing activity against valine, with little change in aminoacylation activity. 1 Publication1
Mutagenesisi243T → A: Abolishes editing activity against valine, with little change in aminoacylation activity. 2 Publications1
Mutagenesisi243T → R: Abolishes pretransfer editing. 2 Publications1
Mutagenesisi246T → A: Nearly the same editing activity as the wild-type. 1 Publication1
Mutagenesisi250N → A: Abolishes editing activity against valine, with little change in aminoacylation activity. 2 Publications1
Mutagenesisi333H → A: Alters the specificity for hydrolysis of the aminoacyl tRNA ester, with no effect on pretransfer editing. 1 Publication1
Mutagenesisi342D → A or N: Strong decrease in total editing and deacylation activities. Severely deficient in translocation from the aminoacylation site to the editing site. 1 Publication1
Mutagenesisi342D → E: Reduces 2- to 3-fold the total editing activity and 2-fold the deacylation activity. Moderately reduces translocation from the aminoacylation site to the editing site. 1 Publication1
Mutagenesisi421W → A: Abolishes translocation from the aminoacylation site to the editing site, without effect on aminoacylation activity and posttransfer editing; when associated with A-183. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3657

DrugCentral

More...DrugCentrali		P00956

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000983842 – 938Isoleucine--tRNA ligaseAdd BLAST937

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 residuei183N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P00956

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

More...PaxDbi		P00956

PRoteomics IDEntifications database

More...PRIDEi		P00956

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P00956

<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

Monomer.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261375, 35 interactors
849163, 6 interactors

Database of interacting proteins

More...DIPi		DIP-10017N

Protein interaction database and analysis system

More...IntActi		P00956, 17 interactors

STRING: functional protein association networks

More...STRINGi		511145.b0026

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P00956

<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

3D structure databases

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

More...SMRi		P00956

Database of comparative protein structure models

More...ModBasei		Search...

<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

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>Motifi58 – 68'HIGH' regionAdd BLAST11
Motifi602 – 606'KMSKS' region5

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).

<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. IleS type 1 subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0060, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001493_7_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00956

Database for complete collections of gene phylogenies

More...PhylomeDBi		P00956

Family and domain databases

Conserved Domains Database

More...CDDi		cd07960, Anticodon_Ia_Ile_BEm, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.620, 2 hits
3.90.740.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_02002, Ile_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
IPR002300, aa-tRNA-synth_Ia
IPR033708, Anticodon_Ile_BEm
IPR002301, Ile-tRNA-ligase
IPR023585, Ile-tRNA-ligase_type1
IPR013155, M/V/L/I-tRNA-synth_anticd-bd
IPR014729, Rossmann-like_a/b/a_fold
IPR009080, tRNAsynth_Ia_anticodon-bd
IPR009008, Val/Leu/Ile-tRNA-synth_edit
IPR010663, Znf_FPG/IleRS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08264, Anticodon_1, 1 hit
PF00133, tRNA-synt_1, 1 hit
PF06827, zf-FPG_IleRS, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00984, TRNASYNTHILE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47323, SSF47323, 1 hit
SSF50677, SSF50677, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00392, ileS, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P00956-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDYKSTLNL PETGFPMRGD LAKREPGMLA RWTDDDLYGI IRAAKKGKKT 
        60         70         80         90        100
FILHDGPPYA NGSIHIGHSV NKILKDIIVK SKGLSGYDSP YVPGWDCHGL 
       110        120        130        140        150
PIELKVEQEY GKPGEKFTAA EFRAKCREYA ATQVDGQRKD FIRLGVLGDW 
       160        170        180        190        200
SHPYLTMDFK TEANIIRALG KIIGNGHLHK GAKPVHWCVD CRSALAEAEV 
       210        220        230        240        250
EYYDKTSPSI DVAFQAVDQD ALKAKFAVSN VNGPISLVIW TTTPWTLPAN 
       260        270        280        290        300
RAISIAPDFD YALVQIDGQA VILAKDLVES VMQRIGVTDY TILGTVKGAE 
       310        320        330        340        350
LELLRFTHPF MGFDVPAILG DHVTLDAGTG AVHTAPGHGP DDYVIGQKYG 
       360        370        380        390        400
LETANPVGPD GTYLPGTYPT LDGVNVFKAN DIVVALLQEK GALLHVEKMQ 
       410        420        430        440        450
HSYPCCWRHK TPIIFRATPQ WFVSMDQKGL RAQSLKEIKG VQWIPDWGQA 
       460        470        480        490        500
RIESMVANRP DWCISRQRTW GVPMSLFVHK DTEELHPRTL ELMEEVAKRV 
       510        520        530        540        550
EVDGIQAWWD LDAKEILGDE ADQYVKVPDT LDVWFDSGST HSSVVDVRPE 
       560        570        580        590        600
FAGHAADMYL EGSDQHRGWF MSSLMISTAM KGKAPYRQVL THGFTVDGQG 
       610        620        630        640        650
RKMSKSIGNT VSPQDVMNKL GADILRLWVA STDYTGEMAV SDEILKRAAD 
       660        670        680        690        700
SYRRIRNTAR FLLANLNGFD PAKDMVKPEE MVVLDRWAVG CAKAAQEDIL 
       710        720        730        740        750
KAYEAYDFHE VVQRLMRFCS VEMGSFYLDI IKDRQYTAKA DSVARRSCQT 
       760        770        780        790        800
ALYHIAEALV RWMAPILSFT ADEVWGYLPG EREKYVFTGE WYEGLFGLAD 
       810        820        830        840        850
SEAMNDAFWD ELLKVRGEVN KVIEQARADK KVGGSLEAAV TLYAEPELSA 
       860        870        880        890        900
KLTALGDELR FVLLTSGATV ADYNDAPADA QQSEVLKGLK VALSKAEGEK 
       910        920        930 
CPRCWHYTQD VGKVAEHAEI CGRCVSNVAG DGEKRKFA
Length:938
Mass (Da):104,297
Last modified:January 23, 2007 - v5
<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:i238CEDAF461F01D5
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 conflicti243 – 264TPWTL…DYALV → RRGLCLPTAQSLLHQISTMR WW AA sequence (PubMed:6390679).CuratedAdd BLAST22
Sequence conflicti300 – 301EL → DV AA sequence (PubMed:6390679).Curated2
Sequence conflicti587R → C AA sequence (PubMed:6390679).Curated1
Sequence conflicti637E → Q AA sequence (PubMed:6390679).Curated1
Sequence conflicti724G → V AA sequence (PubMed:6390679).Curated1
Sequence conflicti738A → P AA sequence (PubMed:6390679).Curated1
Sequence conflicti740 – 743ADSV → RTVW AA sequence (PubMed:6390679).Curated4
Sequence conflicti787F → L AA sequence (PubMed:6390679).Curated1
Sequence conflicti830K → N AA sequence (PubMed:6390679).Curated1
Sequence conflicti867 – 869GAT → DRRY AA sequence (PubMed:6390679).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti594F → L in strain: PS102. 1

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
U00096 Genomic DNA Translation: AAC73137.1
AP009048 Genomic DNA Translation: BAB96595.2
M10428 Genomic DNA Translation: AAA24606.1
X00776 Genomic DNA Translation: CAA25352.1
K01990 Genomic DNA Translation: AAA24091.1

Protein sequence database of the Protein Information Resource

More...PIRi		B64723, SYECIT

NCBI Reference Sequences

More...RefSeqi		NP_414567.1, NC_000913.3
WP_001286857.1, NZ_STEB01000010.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73137; AAC73137; b0026
BAB96595; BAB96595; BAB96595

Database of genes from NCBI RefSeq genomes

More...GeneIDi		944761

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0024
eco:b0026

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2259

<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
U00096 Genomic DNA Translation: AAC73137.1
AP009048 Genomic DNA Translation: BAB96595.2
M10428 Genomic DNA Translation: AAA24606.1
X00776 Genomic DNA Translation: CAA25352.1
K01990 Genomic DNA Translation: AAA24091.1
PIRiB64723, SYECIT
RefSeqiNP_414567.1, NC_000913.3
WP_001286857.1, NZ_STEB01000010.1

3D structure databases

SMRiP00956
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi4261375, 35 interactors
849163, 6 interactors
DIPiDIP-10017N
IntActiP00956, 17 interactors
STRINGi511145.b0026

Chemistry databases

BindingDBiP00956
ChEMBLiCHEMBL3657
DrugCentraliP00956

PTM databases

iPTMnetiP00956

Proteomic databases

jPOSTiP00956
PaxDbiP00956
PRIDEiP00956

Genome annotation databases

EnsemblBacteriaiAAC73137; AAC73137; b0026
BAB96595; BAB96595; BAB96595
GeneIDi944761
KEGGiecj:JW0024
eco:b0026
PATRICifig|1411691.4.peg.2259

Organism-specific databases

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

More...EchoBASEi		EB0487

Phylogenomic databases

eggNOGiCOG0060, Bacteria
HOGENOMiCLU_001493_7_1_6
InParanoidiP00956
PhylomeDBiP00956

Enzyme and pathway databases

BioCyciEcoCyc:ILES-MONOMER
BRENDAi6.1.1.5, 2026
SABIO-RKiP00956

Miscellaneous databases

Protein Ontology

More...PROi		PR:P00956

Family and domain databases

CDDicd07960, Anticodon_Ia_Ile_BEm, 1 hit
Gene3Di3.40.50.620, 2 hits
3.90.740.10, 1 hit
HAMAPiMF_02002, Ile_tRNA_synth_type1, 1 hit
InterProiView protein in InterPro
IPR001412, aa-tRNA-synth_I_CS
IPR002300, aa-tRNA-synth_Ia
IPR033708, Anticodon_Ile_BEm
IPR002301, Ile-tRNA-ligase
IPR023585, Ile-tRNA-ligase_type1
IPR013155, M/V/L/I-tRNA-synth_anticd-bd
IPR014729, Rossmann-like_a/b/a_fold
IPR009080, tRNAsynth_Ia_anticodon-bd
IPR009008, Val/Leu/Ile-tRNA-synth_edit
IPR010663, Znf_FPG/IleRS
PfamiView protein in Pfam
PF08264, Anticodon_1, 1 hit
PF00133, tRNA-synt_1, 1 hit
PF06827, zf-FPG_IleRS, 1 hit
PRINTSiPR00984, TRNASYNTHILE
SUPFAMiSSF47323, SSF47323, 1 hit
SSF50677, SSF50677, 1 hit
TIGRFAMsiTIGR00392, ileS, 1 hit
PROSITEiView protein in PROSITE
PS00178, AA_TRNA_LIGASE_I, 1 hit

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 nameiSYI_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: P00956
Secondary accession number(s): P78038, Q59429
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 203 of the entry and version 5 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

Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families
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