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A8EY49 (SYI_RICCK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:A1E_01685
OrganismRickettsia canadensis (strain McKiel) [Complete proteome] [HAMAP]
Taxonomic identifier293613 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length1079 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 – 10791079Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000022160

Regions

Motif53 – 6311"HIGH" region HAMAP-Rule MF_02003
Motif611 – 6155"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6141ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8EY49 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 10C7C57F24B79612

FASTA1,079124,622
        10         20         30         40         50         60 
MTNTKYYPEV SSNADFAAIE REILKLWQDN NIFQKSIDNR IKDAEFIFYD GPPFANGLPH 

        70         80         90        100        110        120 
YGHLLTGFIK DVYARYQTIK GKKVERRFGW DCHGLPAEMQ SEQELGISGR LAITNFSIEK 

       130        140        150        160        170        180 
FNSHCRASVM KYTGEWEQYV TRQARWVDFK NSYKTMDTHF MESVLWAFKE LYNKGLLYES 

       190        200        210        220        230        240 
MRVMPYSWAC ETPLSHFETR LDNSYRERAD KAVTVSFMLR DKLPHSEYKE YRIFAWTTTP 

       250        260        270        280        290        300 
WTLPANLALA VGSDIDYALV PKNDICYIIA AASVSKYAKE LELKGDEQFT IIKGSELEGL 

       310        320        330        340        350        360 
RYKPLFNYFE NHPNSFKIFA CDFVVEGDGT GVVHMAPGFG EDDQILCESK GIELVCPVDN 

       370        380        390        400        410        420 
SGKFTKEIPD LEGLQVFDAN DKIIIKLKEQ GNWLKTEQYI HNYPHCWRTD TPLIYKAVPS 

       430        440        450        460        470        480 
WYVKVTNFKD RIVELNQQIN WIPSHVKDNV FGKWLENARD WSISRNRFWG TPLPVWKSDD 

       490        500        510        520        530        540 
PKYPRIDVYG SIEELEKDFG VKVTDLHRPF IDELTRANPD DPTGKSTMRR IEDVFDCWFE 

       550        560        570        580        590        600 
SGSMPYSQAH YPFENKKWFE DHFPADFIVE YVAQTRGWFY TLMVLSTALF DRPPFLNCIC 

       610        620        630        640        650        660 
HGVILDTTGQ KLSKRLNNYA DPLELFDKYG SDALRITMLS SNVVKGQELL IDKDGKMVFD 

       670        680        690        700        710        720 
TLRLFIKPIW NAYHFFTMYA NADSLKGKSD FASENVLDIY ILSKLKIAVQ KIEKSLDNFD 

       730        740        750        760        770        780 
TQAAYHQVSE FFEVLNNWYI RRSRARFWKS EKDADKQNAY NTLYSCLETM AIAMSALVPM 

       790        800        810        820        830        840 
ISEAIYLGLH NTVIPQLDYG ISGDKPGAQD PIIKSQDGIR GCRNDNLSVH LCNYPKLSNF 

       850        860        870        880        890        900 
EVNHELVATM DTVLDICSNS LFIRSNENVR VRQPLASITI ISKHNDKLKD FEDLIKDEIN 

       910        920        930        940        950        960 
VKAIIYRDDL ENYATTKLSL NFPMLGKRLP YKMKEIIAAS KKGEWEATAS ALAICGETLK 

       970        980        990       1000       1010       1020 
SEEYKLVLEP YSHIKGAASF ADNSSLLILD LELTPELIKE GIARDIVRFI QQARKDADCS 

      1030       1040       1050       1060       1070 
ITDRILIEII SESDLSKIIN IYGDYIKEQT LSEFAKDFTP DYVNEIELEN HKIQLKIKR 

« Hide

References

[1]"Complete genome sequence of Rickettsia canadensis."
Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Dasch G., Eremeeva M.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: McKiel.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000409 Genomic DNA. Translation: ABV73282.1.
RefSeqYP_001492067.1. NC_009879.1.

3D structure databases

ProteinModelPortalA8EY49.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING293613.A1E_01685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV73282; ABV73282; A1E_01685.
GeneID5626461.
KEGGrcm:A1E_01685.
PATRIC17885291. VBIRicCan89738_0367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAMNIRDAN.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycRCAN293613:GHI3-339-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_RICCK
AccessionPrimary (citable) accession number: A8EY49
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 45 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