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Q5HB43 (SYI_EHRRW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:Erum4870, ERWE_CDS_05090
OrganismEhrlichia ruminantium (strain Welgevonden) [Complete proteome] [HAMAP]
Taxonomic identifier254945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length1117 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.

Sequence caution

The sequence CAH58215.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI27003.1 differs from that shown. Reason: Erroneous initiation.

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 – 11171117Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098545

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
Q5HB43 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: C48E96F5C239C230

FASTA1,117130,645
        10         20         30         40         50         60 
MCIVKTLHLI THVMKEYNSQ FTEGSDFSLI EEQILEFWKE NNIFKKSIEN RDEKRRFIFY 

        70         80         90        100        110        120 
DGPPFANGLP HYGHLLTGFI KDTVARYKTM AGFRVDRRFG WDCHGLPAEM LAEKELGVSG 

       130        140        150        160        170        180 
KLAIEKFGIE KFNNYCRNSV MKFSREWKQY IDRQSRWVDF ENDYKTMNLS FMESIMWSFY 

       190        200        210        220        230        240 
QLWQKGLIYE SIKIVPYSWA CQTPLSNFET RIDNAYRQKT SKTVTLAFEL LDAPKSLIVD 

       250        260        270        280        290        300 
NITAYKILVW TTTPWTLPCN LALAISPNIK YCGAIINKEM YIFSRAYLKN FEDHCRKNNI 

       310        320        330        340        350        360 
EYLIHNGDIC YLSLEYLSYK PVFNYFIDIK NAFKVLVADF VVEDEGTGIV HMAPGFGEDD 

       370        380        390        400        410        420 
FILCKKQGIP DIDDKDTSKL LATICPIDDG GKFTERISDF VNMHVFDTND QIISILKAKN 

       430        440        450        460        470        480 
LCFKTDQYLH NYPHCWRTDT PLIYRAMSSW YVEVTKIKNR MIDLNKDVNW IPSHIRSGQF 

       490        500        510        520        530        540 
GKWLENAKDW AISRNRFWGT PLPVWKSDNP NYPRVDVYGS IKKVFDDIKA LEEDFDIPID 

       550        560        570        580        590        600 
DLHRPYIDNL VRPNPDDPTG KSMMRRVTDV FDCWFESGSM PYAQLHYPFE NKELFENYFP 

       610        620        630        640        650        660 
ADFITEYVAQ TRGWFYTLFV LSTALFDKPP FKNCICHGVV LDTQGQKLSK RLNNYADPME 

       670        680        690        700        710        720 
IFKQYGSDAM RFLMLSHTVS YGGDLLLDKD GVMVRDVIRN VIKPMWNSYN FFTIYADIDK 

       730        740        750        760        770        780 
VNARVISDLD EVDNIMDKYI MCECISTIQS IFNAMEEFDQ SVGNYGYNIK AACNSIVQFF 

       790        800        810        820        830        840 
EVLNNWYIRR CRSRFWSSEI TKDKVNAYNT LYTVMYYMVK VSAPFLPAIT EAIWQKLNFQ 

       850        860        870        880        890        900 
EEESVHLSLL PNIEHITLKD EDQKNIQYMK LIINICGCVL SIRNVRNIRV RQPLNKITIY 

       910        920        930        940        950        960 
SYNNNDLFNL PVKYQNILLD EINVKSIVFK SNIEDIASFQ LKLNFPELGK RIPEKMKNLI 

       970        980        990       1000       1010       1020 
SLLKSNQWKI LENGQLMLGI REGEHYILED NEYTLNLKVH SEFASTITLG PNLLGVLVLD 

      1030       1040       1050       1060       1070       1080 
NTLTDELIME GIARDIVRII QQSRKDNKFN VSDKIDVVIC TQDKMVKNSV QAWYEYIVQQ 

      1090       1100       1110 
TLSLSLVIYE NLDANNVAEY CKTTMKDRNL TLFIKKL 

« Hide

References

[1]"The genome of the heartwater agent Ehrlichia ruminantium contains multiple tandem repeats of actively variable copy number."
Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., Berthier D., Botha M., Joubert F. expand/collapse author list , Corton C.H., Thomson N.R., Allsopp M.T., Allsopp B.A.
Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Welgevonden.
[2]"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
J. Bacteriol. 188:2533-2542(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Welgevonden.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR767821 Genomic DNA. Translation: CAH58215.1. Different initiation.
CR925678 Genomic DNA. Translation: CAI27003.1. Different initiation.
RefSeqYP_180351.1. NC_005295.2.
YP_197385.2. NC_006832.1.

3D structure databases

ProteinModelPortalQ5HB43.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING254945.Erum4870.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH58215; CAH58215; Erum4870.
CAI27003; CAI27003; ERWE_CDS_05090.
GeneID3233369.
3260905.
KEGGeru:Erum4870.
erw:ERWE_CDS_05090.
PATRIC20580862. VBIEhrRum92411_0543.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARVEHMVE.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycERUM254945:GJ2L-536-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. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_EHRRW
AccessionPrimary (citable) accession number: Q5HB43
Secondary accession number(s): Q5FEI3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 68 of the entry and version 2 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