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B1KIT5 (SYI_SHEWM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. 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:Swoo_1291
OrganismShewanella woodyi (strain ATCC 51908 / MS32) [Complete proteome] [HAMAP]
Taxonomic identifier392500 [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_1000189196

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
B1KIT5 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 9D57D8E96617ACED

FASTA940105,573
        10         20         30         40         50         60 
MSDYKSTLNL PETEFPMRGN LANREPVMLK SWAEDDLYQQ IRDSRIGRKP FILHDGPPYA 

        70         80         90        100        110        120 
NGSIHIGHSV NKILKDIIVK SKTMSGFDAP YIPGWDCHGL PIELKVEQKV GKPGHKVTAA 

       130        140        150        160        170        180 
EFRVKCREYA AKQVDGQRDD FMRLGVFGDW HNPYLTMDYS TEANIVRSLS KVIDSGHLHK 

       190        200        210        220        230        240 
GVKPVHWCTE CGSALAEAEV EYEDKKSPAI DVAFAAADKV TLLAKFGVEE CSGSVSMVIW 

       250        260        270        280        290        300 
TTTPWTLPAN RALSVAGDIE YALVEFVKGD KTSSVILAET LVESCMERYG VDSHNVLGKT 

       310        320        330        340        350        360 
SGQSLELLRF NHPFYDFDVP VILGEHVTVD SGTGVVHTAP GHGQDDFVVG QKYGLEVANP 

       370        380        390        400        410        420 
VGDNGVYKSD TEIFAGQHVF KANDNVVALL EEKGALIKLE NILHSYPHCW RHKTPIIFRA 

       430        440        450        460        470        480 
TPQWFISMEQ KGLRKQALNE IEQTQWIPDW GQSRIEKMVE NRPDWCISRQ RTWGVPIALF 

       490        500        510        520        530        540 
VHRETEELHP DSSSLMERVA NKIEQEGIQA WWDLDAAELL GEEADQYRKV TDTLDVWYDS 

       550        560        570        580        590        600 
GSSFSSVVAS RPEFQGHDID LYLEGSDQHR GWFMSSLMIS TAMNGKAPYK QVLTHGFTVD 

       610        620        630        640        650        660 
GNGRKMSKSV GNVIAPQTVT NKLGADILRL WVAATDYSGE MTVSDEILKR SADAYRRIRN 

       670        680        690        700        710        720 
TARFLLANIN GFNPETDLVA VEEMVALDRW AVRRAAALQE ELLEAYEQYN FHVVTQKLMQ 

       730        740        750        760        770        780 
FCSVELGSFY LDIIKDRQYT AKGDSHARRS CQSALYLISE AMVRWIAPIL SFTADEVWQL 

       790        800        810        820        830        840 
LPGQRDKYVF TQEWFQGLKS VTLESDLSDD FWSELLTVRG EVNKVIEQAR REKQVGGSLE 

       850        860        870        880        890        900 
AEITLYADDA LSTALATLGD ELRFVLLTSK TQILDLSAAP ADAIETELSS LKLGLKKAET 

       910        920        930        940 
EKCERCWHHR EDVGQVATHP TLCTRCVTNI EGDGEVRQFA 

« Hide

References

[1]"Complete sequence of Shewanella woodyi ATCC 51908."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Zhao J.-S., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51908 / MS32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000961 Genomic DNA. Translation: ACA85583.1.
RefSeqYP_001759678.1. NC_010506.1.

3D structure databases

ProteinModelPortalB1KIT5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING392500.Swoo_1291.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA85583; ACA85583; Swoo_1291.
GeneID6115526.
KEGGswd:Swoo_1291.
PATRIC23604891. VBISheWoo126588_1341.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSWOO392500:GI2C-1309-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_SHEWM
AccessionPrimary (citable) accession number: B1KIT5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: April 16, 2014
This is version 49 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