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Q17ZG3 (SYI_HELAH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. 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:Hac_0108
OrganismHelicobacter acinonychis (strain Sheeba) [Complete proteome] [HAMAP]
Taxonomic identifier382638 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length921 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 – 921921Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022077

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif610 – 6145"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8951Zinc By similarity
Metal binding8981Zinc By similarity
Metal binding9101Zinc By similarity
Metal binding9131Zinc By similarity
Binding site5691Aminoacyl-adenylate By similarity
Binding site6131ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q17ZG3 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 7D8E6D990DE08006

FASTA921106,190
        10         20         30         40         50         60 
MKEYKDTLNL NTTTFSMKGN LSVNEPKTYA KWQEQQAFKR MQNRKDHHGD FTLHDGPPYA 

        70         80         90        100        110        120 
NGHLHLGHAL NKILKDIVVK REYFKGKKVY FTPGWDCHGL PIEQQILEQL EKEKTSLENP 

       130        140        150        160        170        180 
TLFREKCRDH AKKFLEIQKN EFLQLGVLGD FEDPYKTMDF KFEASIYRAL VEVAKKGLLK 

       190        200        210        220        230        240 
ERHKPIYWSY ACESALAEAE VEYKMKKSPS IFVAFGLKKE SLEKLKIKKA SLVIWTTTPW 

       250        260        270        280        290        300 
TLCANVAIAL KKDALYALTQ KGYLVAKALH EKLVALGVVD SKITHEFNAN DLEYLVATNP 

       310        320        330        340        350        360 
LNQRDSLVIL GEHVSLEDGT GAVHTAPGHG EDDYHLGLKY HLEVLMPVDE KGCYDESIIH 

       370        380        390        400        410        420 
KKLLDESYLG EHIFKAQKRI MEQLGDSLLL EQEIEHSYPH CWRTHKPVIY RATTQWFILM 

       430        440        450        460        470        480 
DEPFIQNDGS QKTLREVALN AIEKVEFVPS SGKNRLKIMI ENRPDWCLSR QRKWGVPLAF 

       490        500        510        520        530        540 
FIDKRTNKPC FESEVLEHAA NLFEEKGCDV WWEYDIKDLL PPSCQDNAKH YEKVMHILDV 

       550        560        570        580        590        600 
WFDSASTFKA VLEDYHGEKG KSPSNVVLEG SDQHRGWFQS SLLLGCILNN QAPFKKVITH 

       610        620        630        640        650        660 
GFIVDEKGEK MSKSKGNVVS LDNLLKKHGS DVVRLWVAFN DYQNDLRVSQ TFFTQTEQHY 

       670        680        690        700        710        720 
KKFRNTLKFL LANFSDMDLK NLERSHDFSP LDHFLLETLE TISNEVNSVF EEHDFVKGLN 

       730        740        750        760        770        780 
ILMAFVTNEL SGIYLDACKD SLYCDSISSE KRQAIQMVLL VVASKLCYFL APILTHTIEE 

       790        800        810        820        830        840 
VLEHSEVLCA FLQAKDVFDL KDINVLEKLH LKECKKPENF EALLALRSAF NEELDRLKKE 

       850        860        870        880        890        900 
GVVKNSLECT IEVEEKALCE NLVEELLMVS SVGSANEKIS ETPTFTLFKA PFFKCPRCWR 

       910        920 
FKSELENTPC KRCKQVLKER Q 

« Hide

References

[1]"Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
PLoS Genet. 2:1097-1110(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sheeba.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260522 Genomic DNA. Translation: CAJ98963.1.
RefSeqYP_663962.1. NC_008229.1.

3D structure databases

ProteinModelPortalQ17ZG3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382638.Hac_0108.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ98963; CAJ98963; Hac_0108.
GeneID4177677.
KEGGhac:Hac_0108.
PATRIC20584142. VBIHelAci71660_0104.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycHACI382638:GJAU-97-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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
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_HELAH
AccessionPrimary (citable) accession number: Q17ZG3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 25, 2006
Last modified: April 16, 2014
This is version 63 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