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

A5EWT0 (SYI_DICNV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 52. 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:DNO_0083
OrganismDichelobacter nodosus (strain VCS1703A) [Complete proteome] [HAMAP]
Taxonomic identifier246195 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCardiobacterialesCardiobacteriaceaeDichelobacter

Protein attributes

Sequence length924 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 – 924924Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022060

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif602 – 6065"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8871Zinc By similarity
Metal binding8901Zinc By similarity
Metal binding9071Zinc By similarity
Metal binding9101Zinc By similarity
Binding site5611Aminoacyl-adenylate By similarity
Binding site6051ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5EWT0 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: BB6A36F6ED0BBF2C

FASTA924105,346
        10         20         30         40         50         60 
MADYKHTLNL PQTDFPMRGN LAQREPEQLR WWQEHEIYRK QREAFADCPT FMLHDGPPYA 

        70         80         90        100        110        120 
NGQIHVGHAL NKTLKDIIIK SRHLLGYNSP YVPGWDCHGL PIEQKVEQKI GKPNQKVSAT 

       130        140        150        160        170        180 
EFRAACRRYA AEQVALQKDG FMRLGIFGFW DQPYLTMNFE TEAQIVRALR DIVAAGHVTQ 

       190        200        210        220        230        240 
GFKPINWCFD CASSLAEAEV EYQDKTSYSI DVAFAVKDVA ALAKIMHADV VPAAVDVVIW 

       250        260        270        280        290        300 
TTTPWTLPAN VAVSIHPEFY YVLVEIEGWY CVVAEELIPA LKSRWKKSAD WRICGRALGK 

       310        320        330        340        350        360 
DLDRLTLRHP FIDRDVLLIN GTHVTLDAGT GCVHTAPAHG VEDYDVCQQY GIDLIHCVLG 

       370        380        390        400        410        420 
NGLYNDDTPH FAGQHIFAAE PQIIELLQTQ NRLIAVEKIT HSYPHCWRHK TPTIYRATTQ 

       430        440        450        460        470        480 
WFISMDKAGL RQKALDGLNE VAFTPDWGKP RLLNMIAHRP DWCISRQRYW GVPLCFVVDK 

       490        500        510        520        530        540 
QTGQLHPDIV NIMDKAASAI EQKGVEAWYE LSLDTLLSGK EVDRYEKLND VLDVWFDSGT 

       550        560        570        580        590        600 
THYSVLKKRA ELSYPADLYL EGSDQHRGWF HSSLLTASAI TGKPPYKALL THGFTVDEDG 

       610        620        630        640        650        660 
RKMSKSLGNV VDPNQVIKTL GADILRLWVA SADYTAEVSL SPNILNQRAD AYRRMRNTCR 

       670        680        690        700        710        720 
FLLANLHDFD PEKNSVAYEK LLPLDRYVIA VAHDLQEKIK KLYVSYDFHL IYQEIFNFCS 

       730        740        750        760        770        780 
VMLGGFYLDV IKDRQYTVAQ NALARRSAQT AIFHIIEAMV RWLAPILSFT AEEIWRYLPG 

       790        800        810        820        830        840 
KREESVFLTK FYEGLQPLND DFLSMHDWEL LLQLREKVNA ALEKARNQGI IGGSLEAMVV 

       850        860        870        880        890        900 
LHLPPQEYEI AARFEQELRF ILIVSAVNVQ PSAALSIEVQ HAIGEKCERC WHYLPDVGTD 

       910        920 
HQHPTLCKRC IENVDGGGEL RRFA 

« Hide

References

[1]"Genome sequence and identification of candidate vaccine antigens from the animal pathogen Dichelobacter nodosus."
Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T., Fedorova N. expand/collapse author list , Khouri H., Bottomley S.P., Whittington R.J., Adler B., Songer J.G., Rood J.I., Paulsen I.T.
Nat. Biotechnol. 25:569-575(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCS1703A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000513 Genomic DNA. Translation: ABQ13975.1.
RefSeqYP_001209014.1. NC_009446.1.

3D structure databases

ProteinModelPortalA5EWT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246195.DNO_0083.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ13975; ABQ13975; DNO_0083.
GeneID5123129.
KEGGdno:DNO_0083.
PATRIC21784452. VBIDicNod48475_0078.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycDNOD246195:GHHS-83-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_DICNV
AccessionPrimary (citable) accession number: A5EWT0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 52 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