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B0SBW4 (SYI_LEPBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:LBF_2221
OrganismLeptospira biflexa serovar Patoc (strain Patoc 1 / Ames) [Complete proteome] [HAMAP]
Taxonomic identifier355278 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length915 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_02002

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002.

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_02002

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 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 – 915915Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189177

Regions

Motif64 – 7411"HIGH" region HAMAP-Rule MF_02002
Motif598 – 6025"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8871Zinc By similarity
Metal binding8901Zinc By similarity
Metal binding9021Zinc By similarity
Metal binding9051Zinc By similarity
Binding site5571Aminoacyl-adenylate By similarity
Binding site6011ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0SBW4 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: F31CD5A61F29C54F

FASTA915104,704
        10         20         30         40         50         60 
MAKPETENPY SKTVLLPETS FPMKADLAKR EPGQIKVWKD QKVFLNMKEI RKSKPSFVLH 

        70         80         90        100        110        120 
DGPPYANGNF HVGHSLNKIL KDIIIKSKTL SGYQTDMIPG WDCHGLPIEV QVLKNLGKEA 

       130        140        150        160        170        180 
RNTGPSELRK KCREYAAEFV GKQGEDLNRF LCFWDENNKY LTMAPEFEAR IVEVFGSLFA 

       190        200        210        220        230        240 
KGYIYKGKKP VYWCIDLATA HAEAEIEYQN HVSPSIYVKF AVKGETDTHC LIWTTTPWTL 

       250        260        270        280        290        300 
PANLAICFNE ELPYSLFQSD AHGRLILADG LKEAVEQKTG ITLTKIKSLS NADLKQMVFL 

       310        320        330        340        350        360 
HPFLDRESIP LFGNHVTLDA GTGCVHTAPG HGTDDYRVGT AAGLPTLSPV DDYGRYTDEF 

       370        380        390        400        410        420 
EMMKGIKIWD ANPKIVELLR EKNALVHFSE FTHSYPHSWR SKKPLIFRAT PQWFFSIDHN 

       430        440        450        460        470        480 
GLRDESLKAI DKVQWIPDWG ITRIRSMVES RPDWCLSRQR NWGVPIPSFT CKSCGLTHLD 

       490        500        510        520        530        540 
DKTIQHFIQI VKKEGIEVWY EKEAKDLLPA DTKCSNCGSE DLKQDKDILD VWFDSGVSSF 

       550        560        570        580        590        600 
AVFGDSIGKE PADLYLEGSD QHRGWFQSSL WPSMAIRKTP PYKSVLTHGY VLDEKGHAMS 

       610        620        630        640        650        660 
KSLGNVINPT TDIINQYGAD ILRLWVSTQD FRDDVKIGKD SIKTVSEAYR KIRNTFRYLL 

       670        680        690        700        710        720 
GNTSAETLTW NLKKEELDTI DKYYLHKLAK LNDEVKKLYD TYQFHQVYHK ILGFCTVDLS 

       730        740        750        760        770        780 
QDYFEIIRDR MYCDAKESKT RRSSEYTLAV ILEVLSKLLA PILSFTTEEV WTSFGKKDSV 

       790        800        810        820        830        840 
FYSDFSDLTE WLDESLESKM KPVFETKEDV QKALEEARKL GKLGKSLEAE VVIDGKKDSL 

       850        860        870        880        890        900 
PFSSEELALF FVVSHVHFET NGIQEVFSEW KGESGSIQIR KPKHFECPRC WRHVSETEGK 

       910 
LCKRCDEVVS KLSPN 

« Hide

References

[1]"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. expand/collapse author list , Davies J.K., Medigue C., Adler B.
PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Patoc 1 / Ames.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000777 Genomic DNA. Translation: ABZ94718.1.
RefSeqYP_001963296.1. NC_010842.1.

3D structure databases

ProteinModelPortalB0SBW4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355278.LBF_2221.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ94718; ABZ94718; LBF_2221.
GeneID6388981.
KEGGlbf:LBF_2221.
PATRIC22343521. VBILepBif95142_2311.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKESHFDE.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycLBIF355278:GHTJ-2219-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
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_LEPBA
AccessionPrimary (citable) accession number: B0SBW4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 47 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