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O29622 (SYI_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. 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:AF_0633
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length1018 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
Reference 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 – 10181018Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098575

Regions

Motif43 – 5311"HIGH" region HAMAP-Rule MF_02003
Motif586 – 5905"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5891ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O29622 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 58C8BBE472FF1D0F

FASTA1,018118,885
        10         20         30         40         50         60 
MLPAKYSPKD VESEIFKFWE DNDIYRKVKE KGGRKFYFVD GPPYTTGRIH LGTAWNKVLK 

        70         80         90        100        110        120 
DTILRYKRMM GFAPTDTPGW DMHGLPIEVK VEQELGFRTK RDIESFGIDK FIERCMNYAL 

       130        140        150        160        170        180 
ANKDAMTEQF KSLAVWMDWE NPYMTIKAEY MNAAWFAIKR AHERGLLERK KMVVNWCHRC 

       190        200        210        220        230        240 
ETALADAEVE YWDEEDPSIY VKFPVKGEKD TYIVIWTTTP WTLPANMAVA VHPSLEYAKF 

       250        260        270        280        290        300 
RAVKDGKVEY LILAKELADS VLGKGDYDSW EVVETYLGED LEGLEYEHPL ADEVPLQKNW 

       310        320        330        340        350        360 
KHQVFFADFV TAENTGCVHI APGHGVEDYE LGVEKGLEVF NPVDDRGVYT EEAGKYAGKH 

       370        380        390        400        410        420 
VKEANDDIID DLYRKDLLLA EERIVHRYGH CWRCKTPIIY RATEQWFIKI SELKDEMLEE 

       430        440        450        460        470        480 
IDKVMWIPEW AGSARFKDWV SNAKDWCISR QRYWGIPIPV WICEKCGEMK VVGSINEIEW 

       490        500        510        520        530        540 
ENDLDLHRPK IDAVTFSCQC GGVMRRVPDV FDVWFDSGVA SWGSIAYPLR KDKFEELWPA 

       550        560        570        580        590        600 
DFITEGHDQT RGWFYSQLGT SVVCFDKAPY KAVLMHGFTL DEQGRKMSKS LGNVVEPEEV 

       610        620        630        640        650        660 
VGQIGVDGFR LYVLYSAPWE DLRFSWEEAR NINRMLNVVW NAVRFAHTYM SLDNYSFGEK 

       670        680        690        700        710        720 
GELKIEDRWI LSRLESFIKE ANEAMEGYQV HRVVRAFFDF FVEDFSRWYI QIIRPRVWEE 

       730        740        750        760        770        780 
RDSPSKLAAY YTMFRVIDRS LRAIAPFAPL IAEWFYQHVV KEFREGEESI FMEEYSTAEV 

       790        800        810        820        830        840 
EMIDGELEAA MKVAKEIVEA AANARNKAKR KLRWPLRELV IESGSEKVRK AVEMLEETIL 

       850        860        870        880        890        900 
SQCNVKQVRV VDSFEKEIEI KPNYKYIGPL LKEKAGEFAK YVASLKEIPE KLVFDGVELD 

       910        920        930        940        950        960 
PKQAIVVDYR LPEGYEYAEF SGGVVYIYKE LDDELVREAF AREVIRRIQE MRKELDLDVE 

       970        980        990       1000       1010 
EFIETTVEMD AELVKGWEDY IKSETRSQKL VFGKAEGYVR EWNIEGKKVK IGIKRLRG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB90608.1.
PIRA69329.
RefSeqNP_069467.1. NC_000917.1.

3D structure databases

ProteinModelPortalO29622.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF0633.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB90608; AAB90608; AF_0633.
GeneID1483851.
KEGGafu:AF0633.

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKPVHWCL.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-648-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.
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. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_ARCFU
AccessionPrimary (citable) accession number: O29622
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 93 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