Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B0RY28 (SYI_XANCB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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:xcc-b100_3183
OrganismXanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]
Taxonomic identifier509169 [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_1000189216

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
B0RY28 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 5C5D14E3FFEA0CB4

FASTA943104,524
        10         20         30         40         50         60 
MTQDYKATLH LPATDFPMRG DLPKREPAML ERWEREGLYA QVRANAAGRP LFVLHDGPPY 

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

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

       190        200        210        220        230        240 
RGVKPVHWCF DCGSALAEAE IEYADKVSPT VDIAYPARDP AAVAAAFGVT LSAGTQVAVP 

       250        260        270        280        290        300 
IWTTTPWTLP ASLAVSLGAE LDYVLVEGAA DHGQPRWLVI AEALAGKALA RYGVDAVVVH 

       310        320        330        340        350        360 
GHAKGAALDQ LLLAHPFYAE RDIPLILGDH VSDDDGTGAV HTAPGHGQED YQVSKQYGLL 

       370        380        390        400        410        420 
ERYSAAQINP IDGRGVYLPS TPPLGDTVLA GLHIWKANDV IIDALRDTGA LLAASKMEHS 

       430        440        450        460        470        480 
YPHCWRHKTP IAFRATPQWF ISMEQANLRA DALKAIETVH WYPSWGQARI AGMIDGRPDW 

       490        500        510        520        530        540 
TISRQRTWGV PIALFVHRET GEPHPRSTEL MRQVAERVEQ GGVDVWYTLD AAELLGDEAG 

       550        560        570        580        590        600 
DYDKITDILD VWFDSGVTHE TVLVDRGLPK PADLYLEGSD QHRGWFQSSL LTGVAMDKVA 

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

       670        680        690        700        710        720 
LKRNADAYRR LRNTARFLLG NLHGFDPLQH LVALDDMVLL DRWIVHRAHE LQEKITAAYA 

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

       790        800        810        820        830        840 
PVLSFTAEEL WAYLPGEHSG NVLFATWYDG LAPMPADAAL TSADVDKLLA LREQVAKVLE 

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

       910        920        930        940 
TTKAKCVRCW HHQASVGSDP RHPELCSRCV SNIEGPGEER RWF 

« Hide

References

[1]"The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM920689 Genomic DNA. Translation: CAP52548.1.
RefSeqYP_001904588.1. NC_010688.1.

3D structure databases

ProteinModelPortalB0RY28.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509169.xccb100_3183.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP52548; CAP52548; xcc-b100_3183.
GeneID6323119.
KEGGxca:xccb100_3183.
PATRIC24086268. VBIXanCam108527_3211.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycXCAM509169:GHW4-3250-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_XANCB
AccessionPrimary (citable) accession number: B0RY28
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 8, 2008
Last modified: April 16, 2014
This is version 50 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