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B2FTJ0 (SYI_STRMK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 48. 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:Smlt1340
OrganismStenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]
Taxonomic identifier522373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

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_1000189200

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
B2FTJ0 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: B1B1C87F4A4328A1

FASTA943104,911
        10         20         30         40         50         60 
MSQDYKTTLN LPATEFPMRG DLPKREPGIL ARWEAQGLYQ QLRDNAAGRP LFVLHDGPPY 

        70         80         90        100        110        120 
ANGRIHLGHA VNKILKDIIV KSRYLAGFDA PYVPGWDCHG LPIEIAVEKK WGKVGTKLDA 

       130        140        150        160        170        180 
VEFRQKCREF AEEQINIQRV DFKRLGVTGD WDNPYKTLSF DFEANEIRAL SKVVANGHLV 

       190        200        210        220        230        240 
RGAKPVYWCF DCGSALAEAE IEYQEKESPA IDVAYAARDA QAIGQAFGVS VPADVEVAVP 

       250        260        270        280        290        300 
IWTTTPWTLP ASLAVSLGAE ITYVLAEGPA HNGKRRWLVL AAALAERALQ RYGVENLVLH 

       310        320        330        340        350        360 
GETTGAALEN QLLAHPFYPE REILVLNGDH VSDEDGTGAV HTAPGHGQED FVVSQKYGLL 

       370        380        390        400        410        420 
DKYNAGQVTP IDGRGVYLES TPPAGDVVLA GQHLWKAQEA IVGVLRDNGS LLAFHPIRHS 

       430        440        450        460        470        480 
YPHCWRHKTP VVFRATPQWF ISMDKANLRN DALAAIDTVG WFPTWGKARI QSMVDGRPDW 

       490        500        510        520        530        540 
TISRQRTWGV PIALFTHRQT GEIHPRSVEL MQQVADRVEA EGIDVWYSLD ATELLGAEAA 

       550        560        570        580        590        600 
DYEKVTDILD VWFDSGVTHE GVLAARGFGK PADLYLEGSD QHRGWFQSSL LTGVAIDKRA 

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

       670        680        690        700        710        720 
LKRNADAYRR LRNTARFLLG NLDGFDPAQH LRPLDQMVAL DRWIVHRAWE LQEKIKAAYD 

       730        740        750        760        770        780 
GYNMAEIVQL LLNFCSVDLG SLYLDVTKDR LYTMPTDSHG RRSAQSAMYH IAEAFTRWVA 

       790        800        810        820        830        840 
PILTFTADEL WGYLPGEHAG HVLFTTWYDG LAPLPADAQL NATDFDQLLA VREQVAKVLE 

       850        860        870        880        890        900 
PMRANGAIGA ALEAEITIAA NEEQAAKWQP LADELRFLFI SGDVQVRPAT TDEVFVSAQP 

       910        920        930        940 
TTKAKCVRCW HHRADVGRNA DHPELCGRCV SNVTGAGEVR SWF 

« Hide

References

[1]"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. expand/collapse author list , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K279a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM743169 Genomic DNA. Translation: CAQ44887.1.
RefSeqYP_001971197.1. NC_010943.1.

3D structure databases

ProteinModelPortalB2FTJ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING522373.Smlt1340.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ44887; CAQ44887; Smlt1340.
GeneID6395039.
KEGGsml:Smlt1340.
PATRIC23698397. VBISteMal45202_1288.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSMAL522373:GJE8-1306-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_STRMK
AccessionPrimary (citable) accession number: B2FTJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 10, 2008
Last modified: April 16, 2014
This is version 48 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