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Q47BK5 (SYI_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. 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:Daro_3046
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length932 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 – 932932Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098378

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif611 – 6155"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8951Zinc By similarity
Metal binding8981Zinc By similarity
Metal binding9151Zinc By similarity
Metal binding9181Zinc By similarity
Binding site5701Aminoacyl-adenylate By similarity
Binding site6141ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47BK5 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 06C1ECF9BC461869

FASTA932104,052
        10         20         30         40         50         60 
MADYKDSLNL PDTAFPMRGD LPKREPQWVA QWQEKKLYQR IREICAGRPR FTLHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHAV NKVLKDIIVR SKTLSGFDAP YVPGWDCHGL PIEHQIEKLH GKAIPADKVR 

       130        140        150        160        170        180 
ELSRAYAAEQ VERQKKDFIR LGVLGDWGNP YLTMNFSAEA GEIRALGKIL EQGYLYQGLK 

       190        200        210        220        230        240 
PVNWCLDCGS ALAEAEVEYE DKNSPAIDVA FEVHENHTAK LAAAFGLTHL RGPAFAVIWT 

       250        260        270        280        290        300 
TTPWTLPANE AVSVHPDLTY DLIETEKGAL ILVRELAEAA LKRYGLEGTV AGSCTGDKLD 

       310        320        330        340        350        360 
QMLLKHPFQN RDVAIICGTH VTTEAGTGLV HTAPAHGVDD YNIGKKYGLP VNNPVGNDGK 

       370        380        390        400        410        420 
FISTTPALSV GELAGKTVWE ANPQVLQELE ARARLLKNER IQHSYPHCWR HKTPIIFRAT 

       430        440        450        460        470        480 
TQWFIGMENK KNEDASTLRW IAERAVDETQ FFPAWGRARL EGMMKTRPDW CVSRQRNWGV 

       490        500        510        520        530        540 
PIPFFLHKET GQPHPRTAEL IEQVALRVEK SGIEAWFSLD AAELLGAEAD QYVKMKDTLD 

       550        560        570        580        590        600 
VWFDSGTTHW HVMRGSHAAD HTYPADLYLE GSDQHRGWFQ SSLLSGCAID GRAPYKGLLT 

       610        620        630        640        650        660 
HGFVVDGKGH KMSKSKGNVI APQQVSDKMG ADILRLWTAS TDYSGELTIS DEILKRVVEG 

       670        680        690        700        710        720 
YRRIRNTLRF LLANVSDFDA ATDMLPIDQW LEIDRYALAL TRELQDGCRA DFDKYEFHRV 

       730        740        750        760        770        780 
VQALQTFCSE DLGGFYLDIL KDRLYTTAPK SVARRSAQSA LWHITQAFVR LLAPITAFTA 

       790        800        810        820        830        840 
EEVWQVLTGK ADDSVMFQVW HDLPALAGEG DLLAKWALIR TARADVTKAL EAQREAGKIG 

       850        860        870        880        890        900 
SALQAAVEIH CGGEKYEALA SLGDDLKFVF ICSSTVAVRD DNEQVIATPL EHAKCERCWH 

       910        920        930 
VREDVGANTE HPTLCGRCVS NLYGEGEVRG CA 

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References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ47776.1.
RefSeqYP_286246.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ47BK5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_3046.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ47776; AAZ47776; Daro_3046.
GeneID3568250.
KEGGdar:Daro_3046.
PATRIC21604760. VBIDecAro89105_3025.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycDARO159087:GI5B-3119-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_DECAR
AccessionPrimary (citable) accession number: Q47BK5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: September 13, 2005
Last modified: April 16, 2014
This is version 68 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