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B5RQH0 (SYI_BORRA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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:BRE_844
OrganismBorrelia recurrentis (strain A1) [Complete proteome] [HAMAP]
Taxonomic identifier412418 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorrelia

Protein attributes

Sequence length1044 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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 – 10441044Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000216251

Regions

Motif48 – 5811"HIGH" region HAMAP-Rule MF_02003
Motif594 – 5985"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5971ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B5RQH0 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: C333F3692BF3F771

FASTA1,044122,975
        10         20         30         40         50         60 
MFKKVENKVH FPQLEEKILQ FWNHNKIFEK SMKQREGCEE FTFYDGPPFA TGLPHFGHFV 

        70         80         90        100        110        120 
PNTIKDIIPR YQTMKGKNVK RYFGWDTHGL PVEYEVEKSL KLSGRYEIEQ YGIDKFNEEC 

       130        140        150        160        170        180 
RNIVLRYTKE WKKIITRLGR WVDFENNYKT MDLTFMESVW WVFKTLYNKG LIYESYYVLP 

       190        200        210        220        230        240 
YSPKLATPLS NFEVNLGEYK EIHDPSLTIK FKIKDKNEYL LAWTTTPWTL PTNLGIAVGK 

       250        260        270        280        290        300 
DIDYSKVVDQ EKNEIYIIGT KRLNHYYQDE NKYVIIEQFK GEHLKGIEYE PLFDYFVNQR 

       310        320        330        340        350        360 
NKGAFKIHTA EYVTTDDGTG IVHIAPFGEE DYQILKKNTQ TDMITPIDAE CKFTSEVKDF 

       370        380        390        400        410        420 
EGLFVKDADN KIIEKLKSMN LLFKRENYLH RYPFCYRTNS PLIYRPISSW FVNIEKIKEK 

       430        440        450        460        470        480 
LIRSNEQINW IPEHLKKGRF GKWLENARDW AISRNRFWGN PIPIWKCSKT GNKICIGSRE 

       490        500        510        520        530        540 
ELEKLSGQKI IDLHKDKIDK ITWPSKYGGT YVRTSEVLDC WFESGSMPYA SKHYPFKDKD 

       550        560        570        580        590        600 
KFQNIFPADF IAEGLDQTRG WFYTLTILGT ALFEKTAFKN VIVNGLVLSS DGKKMSKSLK 

       610        620        630        640        650        660 
NYTDPIQIIN TFGADALRLY LIMSPVIKAD DLKYSDDGVK DVLKNIIIPI WNAYSFFITY 

       670        680        690        700        710        720 
AIIDKFTPNN YVNLYKTNIL DKWIISEIES LKQILNEEID KYNLTKSIEV LLTFIDKLNN 

       730        740        750        760        770        780 
WYIRRSRRRF WKSENDNDKI DAYETLYYTL KNLMLMLAPF IPFLTEEIYQ NLKTKNEKES 

       790        800        810        820        830        840 
IHLNNYPQSI KELINIELEE KMNFTRKVIT IARALRASHN IKIRKPIKTI YIITKNHKEQ 

       850        860        870        880        890        900 
NTLREMTEII LEEINAKEIK IKSNEEELVT YKAKANFKEL GSKLGTNMKS VALAITKLSN 

       910        920        930        940        950        960 
EDILEIINGN KHTITINNNT YDITLKDIIL ERHERKNLKV INEDSITIGL DTLITEELYL 

       970        980        990       1000       1010       1020 
EGLSRELIRK VQNLRKESNF NVTDRIILYT NNDEILTKII NNFENYIKTE TLAITIEINN 

      1030       1040 
KKALTTLELD EEISVNIGIE KCLN 

« Hide

References

[1]"The genome of Borrelia recurrentis, the agent of deadly louse-borne relapsing fever, is a degraded subset of tick-borne Borrelia duttonii."
Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J., Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.
PLoS Genet. 4:E1000185-E1000185(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000993 Genomic DNA. Translation: ACH95054.1.
RefSeqYP_002223275.1. NC_011244.1.

3D structure databases

ProteinModelPortalB5RQH0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412418.BRE_844.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH95054; ACH95054; BRE_844.
GeneID6919469.
KEGGbre:BRE_844.
PATRIC20570870. VBIBorRec40566_0853.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycBREC412418:GJIA-844-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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.
[Graphical view]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_BORRA
AccessionPrimary (citable) accession number: B5RQH0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: November 4, 2008
Last modified: April 16, 2014
This is version 46 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