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Reviewed, UniProtKB/Swiss-Prot O66651 (SYI_AQUAE)

Last modified November 3, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Isoleucyl-tRNA synthetase
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase
      Short name=IleRS
Gene names
Name: ileS
Ordered Locus Names: aq_305
OrganismAquifex aeolicus [Complete proteome] [HAMAP]
Taxonomic identifier63363 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

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Protein attributes

Sequence length956 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02002

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

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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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 956956Isoleucyl-tRNA synthetase HAMAP MF_02002
PRO_0000098341

Regions

Motif60 – 7011"HIGH" region HAMAP MF_02002
Motif624 – 6285"KMSKS" region HAMAP MF_02002

Sites

Metal binding9211Zinc By similarity
Metal binding9241Zinc By similarity
Metal binding9381Zinc By similarity
Metal binding9411Zinc By similarity
Binding site5831Aminoacyl-adenylate By similarity
Binding site6271ATP By similarity

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Sequences

Sequence LengthMass (Da)Tools
O66651-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: E34E14CAB46C8AFD

FASTA956111,315
        10         20         30         40         50         60 
MEEKKVDLKD TLNLPRTEFP MKANLPQREP QILEKWKGLY EKIQKERKGR EVFVLHDGPP 

        70         80         90        100        110        120 
YANGHIHVGH ALNKILKDVI NKYNLLIGKN VNFIPGWDCH GLPIERAVEK ELSKKKIKKE 

       130        140        150        160        170        180 
SLPKTEFREL CREYAKKYVN IQREDFVRLG VLGDWEHPYL TMDPKYEAQE IRELGKFFER 

       190        200        210        220        230        240 
GLAYRSKKPV YWCIYDKTAE AEAEVEYYEK EDPSIYVKFP LKSGEKFGIK DKKVFAIIWT 

       250        260        270        280        290        300 
TTPWTLPANL GIMVKEDADY VLVEVEDEVW IVAKELMDKF FETVNRPEGL VLETVKGKDL 

       310        320        330        340        350        360 
VGLEYTHPFV EKEKLKGHLS EETLKNMWKI YPSEFVSLDT GTGLVHMAPG HGQEDYVVGQ 

       370        380        390        400        410        420 
RYGLEPYAPV SDEGRFVEPA PEFLINVRVF DANHLIVGVL KEKGFLVHEE KIRHSYPHCW 

       430        440        450        460        470        480 
RCKNPVIFRA TPQWFIGMDI EFFGKTLRQR ALEEIEKVKW IPEYGKNRIK SMVENRPDWC 

       490        500        510        520        530        540 
ISRQRFWGVP ITVFYCENCG EIIKDREVFE RVAQLVENSE KGSDVWFELT SSQLLPEGYK 

       550        560        570        580        590        600 
CPKCGGDSFT KEEDILDVWF DSGCSHAAVI RPLGFQKADL YLEGSDQHRG WFQASLLESV 

       610        620        630        640        650        660 
GSYLEAPYKA VLTHGFIVDE KGRKMSKSLG NVISPQEVVK EFGADILRLW VVSEDYTEDV 

       670        680        690        700        710        720 
KLGKNLLKKI ADDYRKIRNT LRFIIGNLYD FNPRTNALPF EKLHHFDRWI ISELQNLLKK 

       730        740        750        760        770        780 
VHENYEKFLF YRVHNHIKNF VITTLSAIYL DVLKDRLYVY APASWERRSA QTALWHLLIA 

       790        800        810        820        830        840 
LTTSTAPYLS FTAEELWEHV GKLDPSLPES VFLYEMPKPD ENLKDEEVLK DYEILLKVRD 

       850        860        870        880        890        900 
EVMRALEVAR KEKGIIKHPY EAKVYIRGDE SVESLLKKYE DYLNFFFTVS QVELREGGEV 

       910        920        930        940        950 
QIEGEELPVK VGVNKAEGEK CPRCWIYYQK EEFVGCVCKR CAKALSEMGI ELNAVC

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References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

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Cross-references

Sequence databases

AE000657 Genomic DNA. Translation: AAC06614.1.
PIRG70327.
RefSeqNP_213211.1.

3D structure databases

HSSPHSSP built from PDB template 1FFY based on UniProtKB P41972.
ModBaseSearch...

Genome annotation databases

GeneID1192885.
GenomeReviewsGene locus aq_305 in contig AE000657_GR.
KEGGaae:aq_305.
NMPDRfig|224324.1.peg.226.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO66651.
OMAFPMRGNL.

Enzyme and pathway databases

BioCycAAEO224324:AQ_305-MON.
BRENDA6.1.1.5. 189781.

Family and domain databases

HAMAPMF_02002.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR010663. DNA_glyclase/IsotRNA_synth_Znf.
IPR002301. Ile-tRNA-synt_Ia.
IPR015905. Ile-tRNA-synt_Ia_N.
IPR018353. Isoleucyl-tRNA_synthetase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSYI_AQUAE
AccessionPrimary (citable) accession number: O66651
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents