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Q04QS6 (SYI_LEPBJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. 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:LBJ_2270
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]
Taxonomic identifier355277 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length914 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 – 914914Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022088

Regions

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

Sites

Metal binding8891Zinc By similarity
Metal binding8921Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9091Zinc By similarity
Binding site5571Aminoacyl-adenylate By similarity
Binding site6011ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04QS6 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 32F8806EE48D446C

FASTA914104,458
        10         20         30         40         50         60 
MSETQKENPY SSTVLLPKTD FPMKADLAKR EPEQIRSWKQ NRIFRKMREQ RSGKKEFVLH 

        70         80         90        100        110        120 
DGPPYANGNF HLGHALNKIL KDTIIKSKSL AGFYADMIPG WDCHGLPIEV QVLKNLGKKV 

       130        140        150        160        170        180 
RETGPEELRQ LCRKYAEEFV GKQGDDLSRF LCFWDEGRIY KTMSPDFEAK IVEVFGELFK 

       190        200        210        220        230        240 
KGYVYRGKKP VYWSIDLATA HAEAEIEYYP HISPSIYVKF PIIGEKKRFC LIWTTTPWTL 

       250        260        270        280        290        300 
PANLAICFNR KIEYSIFKTE SSEELILADA LAENVTITTG VALTKLKPIT SEELAALKFQ 

       310        320        330        340        350        360 
HPFVDRISVS LFGDHVTLEA GTGCVHTAPG HGQDDYKVGL AAGLEPFSPV DDYGRYTDEF 

       370        380        390        400        410        420 
PLMQGKKVFD ANPEIIQLLR DKGLLLYHGE LEHSYPHSWR SKKPLIFRAT PQWFFKIDFQ 

       430        440        450        460        470        480 
DLREKSLSAI DGVRWIPSWG ITRIRSMVET RPDWCLSRQR NWGVPIPAFT CESCGQTHID 

       490        500        510        520        530        540 
DASIQFFTKM VREKGIEIWY SEETKDLLPP KTKCGKCGND SFKKGNDILD VWFDSGVSNF 

       550        560        570        580        590        600 
SVLGERKDEP PADLYLEGSD QHRGWFQSSL WPSMALRGIP PYKAVLTHGY VLDEKGRAMS 

       610        620        630        640        650        660 
KSLGNGIDPT ADIIQVYGAD ILRLWVSSLD FRDDIKVGKE SLKIVSEQYR KIRNTFRYLL 

       670        680        690        700        710        720 
GNLDGHTPEQ NLPFEELEEL DRFYLSKLAG FVEDAVASYE TYQFHQIYQK LILFCTVTLS 

       730        740        750        760        770        780 
QDYFDMIRDR MYCDLRDSKS RRSSSTALQY ILDSLCILVA PILSFTAEEV WTSNGKKDSV 

       790        800        810        820        830        840 
FLQTFPDLKS WKNQSLEDKF ESALQAREVV QKALEIARQE GKLGKSLEAA LEIVSKSGLS 

       850        860        870        880        890        900 
FGELLPKETL ELLFVVSQIH EENPGMEVLS SHENEKFSVK VLKPLQGECP RCWRHTEDIS 

       910 
KEGDLCGRCK SVVA 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JB197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000350 Genomic DNA. Translation: ABJ76744.1.
RefSeqYP_801502.1. NC_008510.1.

3D structure databases

ProteinModelPortalQ04QS6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355277.LBJ_2270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ76744; ABJ76744; LBJ_2270.
GeneID4410993.
KEGGlbj:LBJ_2270.
PATRIC22360424. VBILepBor13265_2915.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycLBOR355277:GHYM-2241-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.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 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_LEPBJ
AccessionPrimary (citable) accession number: Q04QS6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: April 16, 2014
This is version 56 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