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Q5JJ31 (SYI_THEKO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. 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:TK1748
OrganismThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) [Reference proteome] [HAMAP]
Taxonomic identifier69014 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length1065 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 – 10651065Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098591

Regions

Motif49 – 5911"HIGH" region HAMAP-Rule MF_02003
Motif625 – 6295"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6281ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5JJ31 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 2BC6601CFF79D3A6

FASTA1,065125,512
        10         20         30         40         50         60 
MIREPEFREY NPGQLEEKIE AFWKENNTYE KVKKLRENGP KYYFLDGPPY VSGAIHLGTA 

        70         80         90        100        110        120 
WNKIIKDMII RFRSMQGYNV RRQPGFDMHG LPIEVKVEQA LKLKNKREIE TKIGVDNFIK 

       130        140        150        160        170        180 
KCKEFALNNL KIMTEQFKQL GVWMDWDNPY MTIKNEYIES GWFTLKRAWE KGLLEKDKRV 

       190        200        210        220        230        240 
LHWCPRCQTA LAEHEVRGEY KMRKDPSIYV KFPIEWKEKE YLLIWTTTPW TLPANLAVAA 

       250        260        270        280        290        300 
HPEYEYAKVK VETENGEEYW IMAKALVERV LSEVGVKGEI VETFKGEELE GIRYTHVLLE 

       310        320        330        340        350        360 
EYPAQKEFRE KYEWAHRVIL GEHVTLEDGT GLVHTAPGHG EEDFEVGQRY GLPVYSPVDD 

       370        380        390        400        410        420 
AGRYTEGKWK GVYVKDADPE IIEYLKEKGY LVKAGEIEHK YPHCWRCKTP LIFRATDQWF 

       430        440        450        460        470        480 
LKVSKVKDQI IKENDEKVTW YPEWVKVRYD NGVMNSGDWV ISRQRYWGIP LPIWESEDGE 

       490        500        510        520        530        540 
YYVVGSFEEL VKLAVAIEVN GERIDLPEGY EEKLKIIEEK LGPEDLHRPY VDAFIIKVNG 

       550        560        570        580        590        600 
KEMKRVKDVV DVWFDSGIAS WASLDYPRNK ELFEKLWPAD FIVEGEDQVT KWFYSQQAAS 

       610        620        630        640        650        660 
VIAFDTVPYR AVAMHGYVLD EKGDKMSKSL GNIIRPEEVV QKEGRDPFRF YMLWATNPWE 

       670        680        690        700        710        720 
NLRFSWKGLE QVKRMLNILW NVYVLSATYM SLDNFNPTKV NPEELPFREE DRWILSRVNS 

       730        740        750        760        770        780 
LIGEVTDGIE TFRLTRATRG IYNFVVEDLS RWYIRLIRKR MWVEGDDPDK LAAYYTVWKV 

       790        800        810        820        830        840 
FDVLLRLMAP FTPYIAEEIY QNLIRPFVGV ESVHMLDWPE ADEKAIDEEL EKEMEYARKI 

       850        860        870        880        890        900 
VEAGSSARQK ARIKLRYPVR RIIIETEDET VKKAVERINR ILRDQLNAKE VVVGKVEREL 

       910        920        930        940        950        960 
IIKPNFAKVG PEFKGDAKKV IAWISEHGRE LYEKGEMDVE IEGKTFHITR EHVTIEEKLP 

       970        980        990       1000       1010       1020 
DFFVAEEFDG GRVFVDKTLT RELLAEGLAR EFVRRIQEMR KRLDLDVNDR IVVTIETTDE 

      1030       1040       1050       1060 
NRELLQENLD YIMRETRAVE VRFEEAKGYV VEWPEVQAKI GIEKV 

« Hide

References

[1]"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006878 Genomic DNA. Translation: BAD85937.1.
RefSeqYP_184161.1. NC_006624.1.

3D structure databases

ProteinModelPortalQ5JJ31.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING69014.TK1748.

Proteomic databases

PRIDEQ5JJ31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD85937; BAD85937; TK1748.
GeneID3235480.
KEGGtko:TK1748.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAPSWYIRT.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycTKOD69014:GH72-1784-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. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_THEKO
AccessionPrimary (citable) accession number: Q5JJ31
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 70 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