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Q3YRX3 (SYI_EHRCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. 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:Ecaj_0495
OrganismEhrlichia canis (strain Jake) [Complete proteome] [HAMAP]
Taxonomic identifier269484 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length1120 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 – 11201120Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098543

Regions

Motif64 – 7411"HIGH" region HAMAP-Rule MF_02003
Motif647 – 6515"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6501ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3YRX3 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: E982615B4B75549D

FASTA1,120131,115
        10         20         30         40         50         60 
MCIVKYLSLI INTMTEHYSQ LTGEPDFPSI EENVLKFWQE NNIFKKSVDN RDENKRFIFY 

        70         80         90        100        110        120 
DGPPFANGLP HYGHLLTGFI KDTVARYKTM AGFKVERRFG WDCHGLPAEM LSEKELGISG 

       130        140        150        160        170        180 
KLAIEKFGIE KFNNHCRNSV MKFSKEWKQY VDRQARWVDF ENDYKTMNSS FMESIIWSFH 

       190        200        210        220        230        240 
ELWNKGLIYE SIKIVPYSWA CQTPLSNFET RMDNAYREKT SKTVTVAFEL LESPKFITVE 

       250        260        270        280        290        300 
NVKTYKILVW TTTPWTLPCN LALAISKNIK YCGAIIKHEM LIFATGYLKI FQEHCKKNNI 

       310        320        330        340        350        360 
EYQLYNQDIS SVNLEDLHYK PLFKYFADVK NAFKILTADF VVEGEGTGIV HIAPGFGEDD 

       370        380        390        400        410        420 
FILCKMQDIP HIEGDTSNLL SIICPIDDGA KFTDKISDFK NMHVFDTNDQ IINILKQKNL 

       430        440        450        460        470        480 
CFKIDQYLHN YPHCWRTDTP LIYRAMSSWY VEVTKIKDKM IELNKTVNWI PNHICNGQFG 

       490        500        510        520        530        540 
KWLENAKDWA ISRNRFWGTP LPVWKSDNPN YPRIDVYGSI RKVFNNVKAL EEDFDISSIN 

       550        560        570        580        590        600 
DLHRPYIDNL VRPNPDDPTG KSMMRRVSDV FDCWFESGSM PYAQLHYPFE NKEFFENYFP 

       610        620        630        640        650        660 
ADFITEYIAQ TRGWFYTLFI LSTALFNKPP FINCICHGVV LDTQGQKLSK RLNNYADPME 

       670        680        690        700        710        720 
IFNQYGSDAM RFLMLSHTVL YGGDLLLDKE GVMIKDVLRN VIKPIWNSYN FFTIYANIDH 

       730        740        750        760        770        780 
ITAEIITELN ELSNIMDRYI ICECINTIHS IFNAMEELDQ CSNNLGYNIK LACNNITKFF 

       790        800        810        820        830        840 
EILNNWYIRR CRSRFWSSEI TQDKQDAYNT LYTVIYYMIK VSAPFLPIIT EAIWQRLNFQ 

       850        860        870        880        890        900 
KEESVHLSSL PNISNFILNN EDKQNIQYMK LITCICNYVL SIRSTHNIRI RQPLNKIVIY 

       910        920        930        940        950        960 
SHNCPDLLNL PAEYQNILLE EVNVKSISFK SDISDIASFQ LKLNFPELGK RIPDKVKRLI 

       970        980        990       1000       1010       1020 
FLLKNDQWKI LENDKLLLGT IEAEHYVINN NEYTLALKVH NDFACTINLD QHLLGVVLLD 

      1030       1040       1050       1060       1070       1080 
NELSNELIME GIARDIIRTI QHSRKDNKFN ISDKIDVIIH TKDNIVKDSI KTWSQYIIQQ 

      1090       1100       1110       1120 
TLSTSFAIHE EISDIQDINE YYKTTMKDKE VSVFLKKSHT 

« Hide

References

[1]"The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies."
Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.
J. Bacteriol. 188:4015-4023(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Jake.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000107 Genomic DNA. Translation: AAZ68532.1.
RefSeqYP_303130.2. NC_007354.1.

3D structure databases

ProteinModelPortalQ3YRX3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269484.Ecaj_0495.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ68532; AAZ68532; Ecaj_0495.
GeneID3618203.
KEGGecn:Ecaj_0495.
PATRIC20574574. VBIEhrCan118076_0540.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycECAN269484:GI02-524-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.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. 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. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_EHRCJ
AccessionPrimary (citable) accession number: Q3YRX3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: September 27, 2005
Last modified: April 16, 2014
This is version 62 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