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Q8G3I2 (SYI_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. 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:BL1777
OrganismBifidobacterium longum (strain NCC 2705) [Reference proteome] [HAMAP]
Taxonomic identifier206672 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length1103 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 – 11031103Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098524

Regions

Motif65 – 7511"HIGH" region HAMAP-Rule MF_02003
Motif649 – 6535"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8G3I2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: B09FBEA401C18C28

FASTA1,103124,066
        10         20         30         40         50         60 
MSENVYPKAN EGGETAHVAP NPSFPDMEET VLDYWDKDDT FQKSVERNPS GDHSQNEFVF 

        70         80         90        100        110        120 
FDGPPFANGL PHYGHLLTGY AKDVIPRYQT MKGRKVNRVF GWDTHGLPAE LEAQKELGID 

       130        140        150        160        170        180 
SVDQIEKMGI DKFNDACRAS VLKYTNEWQN YVHRQARWVD FEHGYKTLNI PYMESVMWAF 

       190        200        210        220        230        240 
KQLYDKGLAY QGYRVLPYCP KDRTPLSAHE LRMDADVYQD RQDTTVSVAV KMRDEDDAYA 

       250        260        270        280        290        300 
VFWTTTPWTV PTNFAIVVGG DIDYVEVRPT EGKFAGKKFY LGKDLLPHYE KELGENYEVV 

       310        320        330        340        350        360 
RELKGSELEG RRYYPVFPYF AGDEAESEGH VPGPNGYTIF TADYVDTVEG TGLVHQAPYG 

       370        380        390        400        410        420 
EDDMNTLNAK GIKSTDVLDD GCRFTAQCPD YEGDFVFDAN LPILRNLRAG DGPLAEIPEE 

       430        440        450        460        470        480 
RRAILFQEKS YVHSYPHCWR CATPLIYKPV SSWFVSVTKI KPRLLELNQQ INWIPGNVKD 

       490        500        510        520        530        540 
GQFGKWLANA RDWSISRNRF WGSPIPVWVS DDPKYPRVDV YGSLEELKAD FGDYPRDKDG 

       550        560        570        580        590        600 
NINMHRPWID NLVRVNPDDP TGKSHMHRIS DVLDCWFESG SMSFAQFHYP FENKEKFEQH 

       610        620        630        640        650        660 
FPADYIVEYI GQTRGWFYLL HVMATALFDR PAFKNVICHG IVLGSDGQKM SKHLRNYPDV 

       670        680        690        700        710        720 
NGVFDKYGSD AMRWFLMSSP ILRGGNLIVT ADGIRDTVRQ VMLPVWSSYY FFTLYANAAN 

       730        740        750        760        770        780 
GGAGFDARQL RADEVAGLPE MDRYLLARTR RLVLAAEKSL NEFAISDACD AVSDFIDVLT 

       790        800        810        820        830        840 
NWYIRNTRDR FWNEDASAFN TLYTVLEAFM RVLAPLAPME AESVWRGLTG GESVHLAEWP 

       850        860        870        880        890        900 
FVVDEKTGAD TELGRVLVDD PALVDAMEKV REVVSGTLSL RKAAKIRVRQ PLSKLTVVAG 

       910        920        930        940        950        960 
NVEAVKAYDD LLKAELNIKN IEFSTLQDAA AHGLKIVHEL RVNARAAGPR LGKQVQFAIK 

       970        980        990       1000       1010       1020 
ASKSGDWHVD AASGAPVVST PSGDLALVEG EYELINRVEE ENATEAAASV SAALPTGGFV 

      1030       1040       1050       1060       1070       1080 
ILDTALDADL LAEGYARDVI RSVQDARKAA DLDIADRISL VLTVPAVDVA KVEQFRDLIA 

      1090       1100 
HETLATSFEV KEGAELGVEV VKA 

« Hide

References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014295 Genomic DNA. Translation: AAN25560.1.
RefSeqNP_696924.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G3I2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING206672.BL1777.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN25560; AAN25560; BL1777.
GeneID1022079.
KEGGblo:BL1777.
PATRIC21120828. VBIBifLon107831_1832.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycBLON206672:GI1E-1762-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.
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]
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_BIFLO
AccessionPrimary (citable) accession number: Q8G3I2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 69 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