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Q0VSE1 (SYI_ALCBS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS
Gene names
Name:ileS
Ordered Locus Names:ABO_0459
OrganismAlcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]
Taxonomic identifier393595 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesAlcanivoracaceaeAlcanivorax

Protein attributes

Sequence length937 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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) By similarity. HAMAP-Rule MF_02002

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002.

Domain

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)) By similarity. HAMAP-Rule MF_02002

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 937937Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022039

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif602 – 6065"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9001Zinc By similarity
Metal binding9031Zinc By similarity
Metal binding9201Zinc By similarity
Metal binding9231Zinc By similarity
Binding site5611Aminoacyl-adenylate By similarity
Binding site6051ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VSE1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: DB713DE4653A6E4C

FASTA937104,314
        10         20         30         40         50         60 
MTDYKATLNL PQTGFPMKAG LSQREPARLK EWQQKQLYQK IREAFAGRPK FILHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHAV NKILKDMIVK SRTLAGFDAP YVPGWDCHGL PIELMVEKKV GKAGHKVDAG 

       130        140        150        160        170        180 
TFRKKCREYA SKQVAGQKSD FMRLGVLGDW DNPYLTMDFT FEANIIRSLG KIVDNGHLQQ 

       190        200        210        220        230        240 
GFKPVHWCLD CGSALAEAEV EYEDKISPAI DVAFPVVDVA DFVARSGIEA SAPALVIWTT 

       250        260        270        280        290        300 
TPWTLPANRA VAVHPELDYV LLSGELSGVA RELLVAEALA DDLVTRWGLE NVTRSAAVAG 

       310        320        330        340        350        360 
SKLEMLALQH PFLEAQVPVV FGEHVTTDAG TGLVHTAPGH GVDDFMVGKQ YDLDPISPVL 

       370        380        390        400        410        420 
DNGLFREDLP VVGGLHVSKA NEPVIEALKD SGNLVKLAKI EHSYPHCWRH KTPLIFRATA 

       430        440        450        460        470        480 
QWFVSMDQAG LLPRARQEID KVQWLPEWGK ARIEGMLTDR PDWCISRQRT WGVPIALFVN 

       490        500        510        520        530        540 
KETSELHPQT PALIEQVAQR VEKAGVDAWF DLDPAELLGD EADQYSKVTD TLDVWFDSGV 

       550        560        570        580        590        600 
THYCVLDQRE QLRAPADLYL EGSDQHRGWF QSSLLTSLAI RDAAPYSTVL THGFTVDEHG 

       610        620        630        640        650        660 
RKMSKSVGNV IAPQEVWNDL GADILRLWVC ATDYRGEMSV SKDILKQMGD SYRRIRNTSR 

       670        680        690        700        710        720 
FLLSNLSGFE PATDALQPEQ MLALDRYIVD RALQVQAEIQ DLYDGYHFHQ VYQKLHNFCA 

       730        740        750        760        770        780 
LDLGGFYLDI IKDRQYTTQA DSVARRSCQT ALYHIAQALV RWMAPVLSFT AEEIYENLPG 

       790        800        810        820        830        840 
ERLDSVFLAE WYDGLFALAD NADMGRAFWD KVQDAKQAVN KAIEGARAAK LIKGSLSAEV 

       850        860        870        880        890        900 
VLFVDAEQNA LLQRLGDELR FVTITSAAVL KPLAEAPAEL EDTSVAGLKV QVLASDHAKC 

       910        920        930 
ARCWHHQPDV GSHAEHPELC GRCITNVEGD GEVRHYA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286690 Genomic DNA. Translation: CAL15907.1.
RefSeqYP_692179.1. NC_008260.1.

3D structure databases

ProteinModelPortalQ0VSE1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393595.ABO_0459.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL15907; CAL15907; ABO_0459.
GeneID4211348.
KEGGabo:ABO_0459.
PATRIC20838551. VBIAlcBor124741_0481.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycABOR393595:GHRI-471-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_ALCBS
AccessionPrimary (citable) accession number: Q0VSE1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: April 16, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries