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B3R6E8 (SYI_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:RALTA_A2521
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length966 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 – 966966Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189144

Regions

Motif69 – 7911"HIGH" region HAMAP-Rule MF_02002
Motif640 – 6445"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9291Zinc By similarity
Metal binding9321Zinc By similarity
Metal binding9491Zinc By similarity
Metal binding9521Zinc By similarity
Binding site5991Aminoacyl-adenylate By similarity
Binding site6431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3R6E8 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: F81651D467BAC7F6

FASTA966108,366
        10         20         30         40         50         60 
MSDDKRAKSD KNEKNKYPVN LLDTPFPMRG DLPKREPQWV KQWQDKQLYK KIRAARKGAK 

        70         80         90        100        110        120 
KFVLHDGPPY ANGDIHIGHA VNKVLKDMII KARGLTGLDA VYVPGWDCHG MPIEIQIEKK 

       130        140        150        160        170        180 
FGKGLPVQEV QAKARAYATE QIKRQMVDFE RLGVLGDWDH PYLTMNYRNE ADELRALGKI 

       190        200        210        220        230        240 
MEKGYVFRGL KPVNWCFDCG SALAEAEVEY KDKVDLSIDV GFPFAEADKL AHAFKVPVEQ 

       250        260        270        280        290        300 
IDARPGWIVI WTTTPWTIPS NQALNVHPEV EYALVDTPRG HLILATERVE EQLKVYALEG 

       310        320        330        340        350        360 
KVIATATGAA LSEIRFHHPL AKMDGGYDRL SPIYLGDYVT TDTGSGIVHS APAYGVEDFQ 

       370        380        390        400        410        420 
SCKAHGMPDS DIISPVMGNG VYAGTLPLFG GLSIWDANPR IVEALQESGN LFNSHKYTHS 

       430        440        450        460        470        480 
YMHCWRHKTP IIYRATSQWF AGMDVDPAEE NGKPVPTLRE TALAGIDATE FYPAWGKQRL 

       490        500        510        520        530        540 
HNMIANRPDW TLSRQRQWGV PMAFFVHKET GALHPRTPEL LEAIAKRVEQ QGIEAWQTLD 

       550        560        570        580        590        600 
PAELLGDEAS QYEKNRDTLD VWFDSGTTHW TVIRGSHRDD LYDPSADEAD GRLADLYLEG 

       610        620        630        640        650        660 
SDQHRGWFHS SLLTASMLYG KPPYKALLTH GFTVDGEGRK MSKSIGNTVS PQDIANKMGA 

       670        680        690        700        710        720 
EIIRLWVAST DYSGELSISD EILKRVVESY RRIRNTLRFL LSNLSDYDHG KHALPAAEWL 

       730        740        750        760        770        780 
EIDRYAVALT AQLQKEVLSH YEAYEFHPVV AKLQTFCSED LGGFYLDVLK DRLYTTAPDS 

       790        800        810        820        830        840 
KARRAAQNAL YHITQAMLHW MAPFLSFTAE EAWQVFAHGT AHTDTIFTST YYAVPEVDDA 

       850        860        870        880        890        900 
DDLLQKWHTL REVRAEVTRQ LEAVRVEGEI GSSLQAELTI QAGGPVLEAL QSLGDDLRFV 

       910        920        930        940        950        960 
LLTSAAKVTA APEAGDLLVT VTPSAHAKCE RCWHYRADVG HNPDHPTLCG RCDSNLFGAG 


EHRSHA 

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU633749 Genomic DNA. Translation: CAQ70452.1.
RefSeqYP_002006513.1. NC_010528.1.

3D structure databases

ProteinModelPortalB3R6E8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING164546.RALTA_A2521.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ70452; CAQ70452; RALTA_A2521.
GeneID6454989.
KEGGcti:RALTA_A2521.
PATRIC21531684. VBICupTai42494_2481.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKKRIELM.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCTAI164546:GJNE-2515-MONOMER.
CTAI977880:GLC7-2515-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_CUPTR
AccessionPrimary (citable) accession number: B3R6E8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 2, 2008
Last modified: May 14, 2014
This is version 48 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