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B8CSC1 (SYI_SHEPW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:swp_3728
OrganismShewanella piezotolerans (strain WP3 / JCM 13877) [Complete proteome] [HAMAP]
Taxonomic identifier225849 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length940 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 – 940940Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189195

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9031Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9231Zinc By similarity
Metal binding9261Zinc By similarity
Binding site5641Aminoacyl-adenylate By similarity
Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B8CSC1 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: F23DFCF6DF1F28A0

FASTA940105,982
        10         20         30         40         50         60 
MSDYKSTLNL PETEFPMRGN LANREPEMLK SWNEKGLYQQ IRESRKDSKP FILHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHSV NKILKDIIIK SKTMSGFDAP YIPGWDCHGL PIELKVEQKV GKPGHKVTAS 

       130        140        150        160        170        180 
EFRQKCREYA AKQVDGQRDD FIRLGVFADW QNPYLTMDYN TEANIVRSLS KVIDSGHLHK 

       190        200        210        220        230        240 
GVKPVHWCTD CGSALAEAEV EYEDKMSPAI DVAFTAVDKP ALLAKFGLTE YAHPISMVIW 

       250        260        270        280        290        300 
TTTPWTLPAN RALSVAGQLE YTLVEMVKDG QTQALVLAQE LVESCVERFG AETHKVLANV 

       310        320        330        340        350        360 
LGSELELLRF NHPFYDFDVP VILGEHVTVE SGTGVVHTAP GHGQDDFVVG QKYGLEVANP 

       370        380        390        400        410        420 
VGDNGVYKAD TEIFAGQHVF KANKAVVALL EEKGALLNHV AINHSYPHCW RHKTPIIFRA 

       430        440        450        460        470        480 
TPQWFISMDQ KGLRTQALSE IEKTQWIPDW GQSRIEKMVE NRPDWCISRQ RTWGVPITLF 

       490        500        510        520        530        540 
VHRETEELHP DSVSLMERVA NRIEQEGIQA WWDLDAAELL GDEAEQYRKV TDTLDVWYDS 

       550        560        570        580        590        600 
GSTFSSVVAS RPEFNGHEVD LYLEGSDQHR GWFMSSLMIS TAMNGKAPYK QVLTHGFTVD 

       610        620        630        640        650        660 
GKGRKMSKSV GNVIAPQHVT NKLGADILRL WVAATDYSGE MTVSDEILKR SADAYRRIRN 

       670        680        690        700        710        720 
TARFLLANIN GFNPETDMVA VEDMVALDRW VVRRAAALQQ ELLEAYDQYN FHLVTQKLMQ 

       730        740        750        760        770        780 
FCSVELGSFY LDIIKDRQYT AKDDSNARRS CQSALYLISE AMVRWIAPVL SFTADEIWKL 

       790        800        810        820        830        840 
LPGERGEFVF TETWYEGLQS VTLDSDLSDE FWEQLLTVRA EVNKVIENAR REKQIGGSLE 

       850        860        870        880        890        900 
AEIMLFADEA LSTALSTLGD ELRFVLLTSK TDVVALSEAP ADAIETELAS LKLGLKKSEA 

       910        920        930        940 
EKCERCWHHR EEVGQVAEHP TLCTRCVTNI EGEGETRQFA 

« Hide

References

[1]"Environmental adaptation: genomic analysis of the piezotolerant and psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans WP3."
Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L., Bartlett D.H., Yu J., Hu S., Xiao X.
PLoS ONE 3:E1937-E1937(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WP3 / JCM 13877.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000472 Genomic DNA. Translation: ACJ30411.1.
RefSeqYP_002312998.1. NC_011566.1.

3D structure databases

ProteinModelPortalB8CSC1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING225849.swp_3728.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ30411; ACJ30411; swp_3728.
GeneID7034696.
KEGGswp:swp_3728.
PATRIC23545829. VBIShePie65056_3425.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycSPIE225849:GH6V-3628-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_SHEPW
AccessionPrimary (citable) accession number: B8CSC1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 43 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