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B0BB05 (SYI_CHLTB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:CTLon_0269
OrganismChlamydia trachomatis serovar L2b (strain UCH-1/proctitis) [Complete proteome] [HAMAP]
Taxonomic identifier471473 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length1036 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
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 – 10361036Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000216255

Regions

Motif46 – 5611"HIGH" region HAMAP-Rule MF_02003
Motif589 – 5935"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5921ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0BB05 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 3EC21D4DEC10D32B

FASTA1,036118,774
        10         20         30         40         50         60 
MDNEDKISIS AKEEKILSFW KEQDIFQKTL DNREGCPTFS FYDGPPFATG LPHYGHLLAG 

        70         80         90        100        110        120 
TIKDVVCRYA SMDGHYVPRR FGWDCHGVPV EYEVEKSLGL TEPGAIERFG VANFNEECRK 

       130        140        150        160        170        180 
IVFRYADEWK YFVDRIGRWV DFSATWRTMD LSFMESVWWV FRSLYDQGLV YEGTKVVPFS 

       190        200        210        220        230        240 
TKLGTPLSNF EAGQNYKEVD DPSVVVKFAL QDNQGFLLAW TTTPWTLVSN MALAVHPELT 

       250        260        270        280        290        300 
YVRIKDKESG DEYILGQESL PRWFPDRESY EWIGQLSGKS LVGQSYEPLF PYFQDKKELG 

       310        320        330        340        350        360 
AFRILPADFI EESEGTGIVH MAPAFGEADF FACQEHNVPL VCPVDNQGCY TAEVKDFVGE 

       370        380        390        400        410        420 
YIKSADKGIA RRLKNENKLF YQGTVRHRYP FCWRTDSPLI YKAVNSWFVA VEKVKSKMLK 

       430        440        450        460        470        480 
ANESIHWTPG HIKQGRFGKW LEGARDWAIS RNRYWGTPIP IWRSDDGELL VIGSIQELEA 

       490        500        510        520        530        540 
LSGQKIVDLH RHFIDEIEIN QNGKSFRRIP YVFDCWFDSG AMPYAQNHYP FERAEETEAC 

       550        560        570        580        590        600 
FPADFIAEGL DQTRGWFYTL TVIAAALFDQ PAFKNVIVNG IILAEDGNKM SKRLNNYPSP 

       610        620        630        640        650        660 
KMIMDAYGAD ALRLYLLNSV VVKAEDLRFS DKGVESVLKQ VLLPLSNALA FYKTYAELYG 

       670        680        690        700        710        720 
FDPKETDNIE LAEIDRWILS SLYSLLGKTR ESMSQYDLHA AVNPFVDFIE DLTNWYIRRS 

       730        740        750        760        770        780 
RRRFWDAEDS ADRRAAFSTL YEVLVVFSKV IAPFIPFISE DMYQQLRGET DPESVHLCDF 

       790        800        810        820        830        840 
PHVVLEKILP NLERKMQDIR EIVALGHSLR KEHKLKVRQP LQNVYIVGSQ ERMEALAQVG 

       850        860        870        880        890        900 
SLIGEELNVK DVHFCSETPE YVTTLIKPNF RTLGKKVGNR LPEIQRALAG LPQEQIQAFM 

       910        920        930        940        950        960 
HKGQMVVSLG EETISLDKED ITVSWASAEG FVARSSASFV AVLDCQLTEP LIMEGIAREL 

       970        980        990       1000       1010       1020 
VNKINTMRRN GKLHVSDRIA IRLHAPVIVQ EAFALHKEYI CEETLTTSVS VIDYKEGEEW 

      1030 
DINGHAVSFV LERVER 

« Hide

References

[1]"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates."
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.
Genome Res. 18:161-171(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCH-1/proctitis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM884177 Genomic DNA. Translation: CAP06667.1.
RefSeqYP_001653370.1. NC_010280.2.

3D structure databases

ProteinModelPortalB0BB05.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471473.CTLon_0269.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP06667; CAP06667; CTLon_0269.
GeneID5859265.
KEGGctl:CTLon_0269.
PATRIC20382111. VBIChlTra68089_0297.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARVEHMVE.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCTRA471473:GHJK-288-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. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_CHLTB
AccessionPrimary (citable) accession number: B0BB05
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 26, 2008
Last modified: May 14, 2014
This is version 53 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