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Q1LJB8 (SYI_RALME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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:Rmet_2885
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length959 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 – 959959Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022112

Regions

Motif66 – 7611"HIGH" region HAMAP-Rule MF_02002
Motif633 – 6375"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9221Zinc By similarity
Metal binding9251Zinc By similarity
Metal binding9421Zinc By similarity
Metal binding9451Zinc By similarity
Binding site5921Aminoacyl-adenylate By similarity
Binding site6361ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LJB8 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 39E25FBF00894BFC

FASTA959107,836
        10         20         30         40         50         60 
MSDDKRAKPE KSKYPVNLLD TPFPMRGDLP KREPQWVKQW QDKQLYKKIR AARHGAKKFV 

        70         80         90        100        110        120 
LHDGPPYANG DIHIGHAVNK VLKDMIIKAR GLTGLDAVYV PGWDCHGMPI EIQIEKQFGK 

       130        140        150        160        170        180 
GLPVQEVQSK ARAYATEQIA RQRKDFERLG VLGDWENPYL TMNFSNEADE LRALGKIMER 

       190        200        210        220        230        240 
GYVFRGLKPV NWCFDCGSAL AEAEVEYKDK VDLSIDVGFP FAETDKIAHA FHVPLAQLEG 

       250        260        270        280        290        300 
KPGWIVIWTT TPWTIPSNQA LNMHPEVEYA LVDTPRGFLI LAKDRVEEQL KTYALEGTIV 

       310        320        330        340        350        360 
ATARGDALTE VRFHHPLAKM DAGYVRTSPV YLGDYVTTDT GTGIVHSAPA YGVEDFQSCK 

       370        380        390        400        410        420 
AHGMPDSDII SPVMGDGVYA STLPLFGGLS IWDANPKIVE VLRESGNLFN SHKYEHSYMH 

       430        440        450        460        470        480 
CWRHKTPIIY RATSQWFAGM DVDPVDNGPT LRETALAGIE ATEFYPAWGK QRLHNMIANR 

       490        500        510        520        530        540 
PDWTLSRQRQ WGVPMAFFVH KETGALHPRT PELLEEVAKL VEKHGIEAWQ TLDPKDLLGD 

       550        560        570        580        590        600 
EAAQYEKNRD TLDVWFDSGT THWTVIRGSH RDELYDPAAD LPDGRLADLY LEGSDQHRGW 

       610        620        630        640        650        660 
FHSSLLTASM LYGKPPYKAL LTHGFTVDGE GRKMSKSVGN TVSPQDISNK MGAEIIRLWV 

       670        680        690        700        710        720 
ASTDYSGELS ISDEILKRVV EGYRRIRNTL RFLLANLTDY DHAKHALPAS EWLEIDRYAV 

       730        740        750        760        770        780 
ALTDRLQKEV LSHYQAYEFH PVVAKLQTFC SEDLGGFYLD VLKDRLYTTA ADSKARRGAQ 

       790        800        810        820        830        840 
NALYHITQAM LHWMAPFLTF TAEEAWQIFA HGTEHKDTIF TSTYYAIPSV DDGDTLLQKW 

       850        860        870        880        890        900 
HEIRTVRAEV TRQLEAVRVE GDIGSSLQAE VTIAAGGPVL AALQSLEDDL RFVLLTSAAK 

       910        920        930        940        950 
VTPAPEGGDL LVTVTPSQHA KCERCWHYRA DVGHNPEHPT ICGRCDSNLF GAGEHRSHA 

« Hide

References

[1]"Complete sequence of the chromosome of Ralstonia metallidurans CH34."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH34 / ATCC 43123 / DSM 2839.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000352 Genomic DNA. Translation: ABF09758.1.
RefSeqYP_585027.1. NC_007973.1.

3D structure databases

ProteinModelPortalQ1LJB8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266264.Rmet_2885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF09758; ABF09758; Rmet_2885.
GeneID4039713.
PATRIC20290399. VBIRalMet4734_3275.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycCMET266264:GJ5G-3081-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_RALME
AccessionPrimary (citable) accession number: Q1LJB8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: April 16, 2014
This is version 61 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