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Q3BW42 (SYI_XANC5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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:XCV1290
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length943 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 – 943943Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098507

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif618 – 6225"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9061Zinc By similarity
Metal binding9091Zinc By similarity
Metal binding9261Zinc By similarity
Metal binding9291Zinc By similarity
Binding site5771Aminoacyl-adenylate By similarity
Binding site6211ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3BW42 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: CBBD85760B29492C

FASTA943104,593
        10         20         30         40         50         60 
MTQDYKATLH LPATEFPMRG DLPKREPAML ERWEREGFYA QLRANAAGRP LFVLHDGPPY 

        70         80         90        100        110        120 
ANGQIHLGHA VNKILKDIIV KSKYLAGFDA PYIPGWDCHG LPIEIAIEKK YGKVGVKLDA 

       130        140        150        160        170        180 
AQFRQKCREY ATEQIDLQRR DFKRLGVIGD WDNPYKTLDF RFEANEIRAL AKVVDNGHLT 

       190        200        210        220        230        240 
RGVKPVHWCF DCGSALAEAE IEYADKVSPT VDIAYPARDP GAVAAAFGAR LPAGVGVAVP 

       250        260        270        280        290        300 
IWTTTPWTLP ASLAVSLGAE LDYVLVEGPA DRGQPRWLVI AEALAAKALA RYGVDAVVVH 

       310        320        330        340        350        360 
GHAKGAALEQ MLLNHPFYAE REIPLLLGDH VSAEDGTGAV HTAPGHGQED YQVSRHYGLL 

       370        380        390        400        410        420 
ERYGAAQINP VDGRGVYLPS TPPLGDTALA GLHIWKANDV IIDALRGTGV LLAASKMEHS 

       430        440        450        460        470        480 
YPHCWRHKTP IAFRATPQWF ISMEQANLRA DALKAIENVH WYPSWGQARI AGMVDGRPDW 

       490        500        510        520        530        540 
TISRQRTWGV PIALFVHRET GEPHPRSTEL LRQVADRVEQ GGVDVWYTLD ASELLGSEAA 

       550        560        570        580        590        600 
DYEKITDILD VWFDSGVTHE AVLPDRGLPK PADLYLEGSD QHRGWFQSSL LSGVAMDKAA 

       610        620        630        640        650        660 
PYKQCLTHGF TVDEHGRKMS KSLGNGIEPQ DIMKTLGADI LRLWIASADY SNEMSLSQEI 

       670        680        690        700        710        720 
LKRNADAYRR LRNTARFLLG NLHGFDPLRH LVALDQMVLL DRWIVHRAHA LQEKIVAAYA 

       730        740        750        760        770        780 
RYDFAEIVQA LLNFCSVDLG SLYLDVTKDR LYTMAEDARG RRSAQSAMYH VAEAFVRWIA 

       790        800        810        820        830        840 
PVLSFTAEEL WSYLPGQHVD NVLFATWYDG LAPLPADAAL TSADFDKLLV LREQVAKVLE 

       850        860        870        880        890        900 
PMRANGAIGA ALEAEITVAA DAQTAARWQP LAEELRFLFI SGDVTVTAAS TDDIFVSAQP 

       910        920        930        940 
TTKAKCVRCW HHQASVGSDP RHPELCSRCV SNIEGPGEQR RWF 

« Hide

References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 85-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM039952 Genomic DNA. Translation: CAJ22921.1.
RefSeqYP_363021.1. NC_007508.1.

3D structure databases

ProteinModelPortalQ3BW42.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316273.XCV1290.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ22921; CAJ22921; XCV1290.
GeneID3732867.
KEGGxcv:XCV1290.
PATRIC24092038. VBIXanCam71633_1515.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycXCAM316273:GJF8-1325-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_XANC5
AccessionPrimary (citable) accession number: Q3BW42
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 22, 2005
Last modified: April 16, 2014
This is version 61 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