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Q9YF67 (SYI_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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:APE_0374
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length1064 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 – 10641064Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098574

Regions

Motif53 – 6412"HIGH" region HAMAP-Rule MF_02003
Motif603 – 6075"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6061ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YF67 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: DCB292AD67031978

FASTA1,064123,482
        10         20         30         40         50         60 
MGSVPRVLEG ERYDQFALES FVKSYWEENS IYRKVKEKSS RAPRKFYFLD GPPYASAKSI 

        70         80         90        100        110        120 
HIGTAWNKVV KDVVLRFYRM TGYNVWDKPG YDTHGLPIEV KIEQSLGVRV KREIEEKVGV 

       130        140        150        160        170        180 
ENFIAACKRF VDENMEAMTR QFKEIGVFMD WENPYVTYRD EYIESGWWLV KKAWEKGLLY 

       190        200        210        220        230        240 
KGYRVLHWCP RCETTLADYE VSEYRELEDP SIYVKFPVEG REGEYLLVWT TTPWTLPANA 

       250        260        270        280        290        300 
FVMAHPDMEY VKVRVGRDTL ILAKARLDHV MREAGVSEYE VLEVLKGSQL EGLRYRHPLE 

       310        320        330        340        350        360 
DVVDAQRELS KWHKVVMAPE AVTPHEGSGL VHSAPGHGTI DYEIAQRIGA PVVSLVDERG 

       370        380        390        400        410        420 
FMTEAAGKYS GLYFRGEANK AIVEDLRARG ALFHAATIVH RYPVCWRCKT PLLLRATTQW 

       430        440        450        460        470        480 
FVAVTRLKNQ LMREAEKVEW QPGWAKTRFM NMLRELRDWV ISRQRYWGIP LPVWRCSSCG 

       490        500        510        520        530        540 
YEHVVGSVEE LESMGGRRPE NLHRPWVDRV ELKCPRCGGS MKRVPDVLDV WFDSGIAFYA 

       550        560        570        580        590        600 
SLGYPRDRET WERLKPVDFI VEGHDQIRGW FFSLLRSGVI GFGETPYRRV LVHGFALDEQ 

       610        620        630        640        650        660 
GREMHKSLGN YVDFEELIAK VPRDVVRFWV LQNTVWEDLR FSWKGLDLMR RDFNVIWNVY 

       670        680        690        700        710        720 
AFASIYMGLD RFDPRRTSLS SVEDSLEVED RWILSRLASL KRRYLTAMED LRIHDAARAL 

       730        740        750        760        770        780 
RSFIIEDVSH WYLRIIRRRV WEEVDTPSKR AAYATLYKVL WEWLLMAAPL IPYTAEYLYI 

       790        800        810        820        830        840 
KVFREAEERP EESIHMLDMP EPEDHLIDST LEEDMEKARM VLEAILSARN EAGLKLRRPV 

       850        860        870        880        890        900 
RRVIIAASNP GVEGSLRRLE GLIRLMANAK EIEFAPASAL EATRIYRVEP DYGRLGPKYK 

       910        920        930        940        950        960 
RDMPKVLRLI EEKGGEIGRV LAEKGVYEGE YEGLPVKLTL EDVSLKAEYP EWLKVRDTPL 

       970        980        990       1000       1010       1020 
GLVAVDTRLT KEEVLEGLAR DIVRRIQAMR KEAGYSVEDY VEVWIQGGED VVEAVNALKE 

      1030       1040       1050       1060 
YIKRETRALK LEVGEPPSGV EVLREWELDG EKVVIALKRA AASG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA79329.1.
PIRE72729.
RefSeqNP_147189.1. NC_000854.2.

3D structure databases

ProteinModelPortalQ9YF67.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272557.APE_0374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA79329; BAA79329; APE_0374.
GeneID1444584.
KEGGape:APE_0374.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAERLMLHQ.

Enzyme and pathway databases

BioCycAPER272557:GJD6-283-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.
InterProIPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
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]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
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.
ProtoNetSearch...

Entry information

Entry nameSYI_AERPE
AccessionPrimary (citable) accession number: Q9YF67
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: May 14, 2014
This is version 83 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