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Q5P221 (SYI_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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:AZOSEA25180
ORF Names:ebA4448
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length939 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 – 939939Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098343

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif615 – 6195"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9021Zinc By similarity
Metal binding9051Zinc By similarity
Metal binding9221Zinc By similarity
Metal binding9251Zinc By similarity
Binding site5741Aminoacyl-adenylate By similarity
Binding site6181ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P221 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 42837213399F6856

FASTA939105,391
        10         20         30         40         50         60 
MADYRKTLNM PDTPFPMRGD LAKREPGWVA DWQAKKLYQK VRKAAAGRPK FVLHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHAV NKILKDIIVR SKTLAGFDAP YVPGWDCHGL PIEHQIEKQH GKHLPADRAR 

       130        140        150        160        170        180 
ELCREYAAEQ IERQKKDFIR LGVLGDWDNP YRTMNFSNEA DEIRALGELF RKGFLFKGLK 

       190        200        210        220        230        240 
PVNWCFDCGS ALAEAEVEYQ DKKSPAIDVG FPLVDNERDK LAHAFGLDTL PEQPVYIVIW 

       250        260        270        280        290        300 
TTTPWTIPSN QALNVHPELI YELVETPKGL LILAAELRAS ALERYQLEGR VLAAARGVAL 

       310        320        330        340        350        360 
DRINFRHPFY DRLSPVFLGD YVAADAGTGI VHSAPAYGLD DFVSCTRYGM RNDEILNPVQ 

       370        380        390        400        410        420 
ADGTFAGSLP FFGGLSVWDA NPKIVDKLAE VGSLFASGTL THSYMHCWRH KTPVIYRATT 

       430        440        450        460        470        480 
QWFVGMDRLP GREAVEPGSA TLRELALKAV DETQFYPAWG KARLHSMIAN RPDWCVSRQR 

       490        500        510        520        530        540 
NWGVPIPLFL HKETGEPHPR SLELLEQVAQ RVEQHGIDAW FKLDAAELLG SDVAQYDKMR 

       550        560        570        580        590        600 
DTLDVWFDSG TTHWTVLRGS HAADSQWPAA LYLEGSDQHR GWFHSSLLTG CAIDGRAPYD 

       610        620        630        640        650        660 
ALLTHGFVVD GQGKKMSKSK GNVVAPQEVS DKLGAEILRL WVAATDYSGE LTISKEILDR 

       670        680        690        700        710        720 
VVEVYRRLRN TLRFLLANTG DFDIARDGVP VEEWLDIDHY ALALTRRLQE QVTGDYARFE 

       730        740        750        760        770        780 
FHKIVQALQN FAAEDLGAFY VDILKDRLYT TKADSRARRA AQTALWHITQ AITRMMAPIL 

       790        800        810        820        830        840 
TFTAEEIWRV TGNDAEDSVM LHTWHELPEL GASDEILARW ELIRSARAEV QKVLESLRSD 

       850        860        870        880        890        900 
GRIGASLQAE VRVRASGARF DALASVGADL HFVLITSRAE LVRVETEADE GVDAAPSSHQ 

       910        920        930 
KCGRCWHFRE DIGVDADHPE LCGRCCTNLH GDGESRTHA 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI08643.1.
RefSeqYP_159544.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5P221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76114.ebA4448.

Proteomic databases

PRIDEQ5P221.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI08643; CAI08643; ebA4448.
GeneID3182804.
KEGGeba:ebA4448.
PATRIC20971222. VBIAroAro98752_2549.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAERLMLHQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycAARO76114:GJTA-2549-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_AROAE
AccessionPrimary (citable) accession number: Q5P221
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 75 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