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A9IRC2 (SYI_BORPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:Bpet2814
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length953 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 – 953953Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189130

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif623 – 6275"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9161Zinc By similarity
Metal binding9191Zinc By similarity
Metal binding9361Zinc By similarity
Metal binding9391Zinc By similarity
Binding site5821Aminoacyl-adenylate By similarity
Binding site6261ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9IRC2 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: A994E669957A6EF7

FASTA953105,198
        10         20         30         40         50         60 
MDYKKTLNLP DTPFPMRGDL AKREPAWVAQ WEENHVYQAI RAASRGRPRF VLHDGPPYAN 

        70         80         90        100        110        120 
GDIHIGHAVN KVLKDIIVKS RNMAGYDAHY VPGWDCHGMP IEIQIEKKFG KHLPVTEVQA 

       130        140        150        160        170        180 
KARAYALEQI DRQRKDFKRL GVLGEWDRPY LTMNFSNEAN EIRALGGILQ KGYVFRGLKP 

       190        200        210        220        230        240 
VNWCFDCGSA LAEAEVEYAD RVDPAVDVAF PFADKPGLAA AFGLDSVDDG AVVIWTTTPW 

       250        260        270        280        290        300 
TIPANQALNM HPELEYALVR ATPAPAHGPL LLLARERVEA CLKAWGLQGE VIATAPGAAL 

       310        320        330        340        350        360 
SGLRFHHPLA SADAGYARTS PVYLGDYVTL DAGTGVVHSA PAYGIEDFVS CKAHGLSDDD 

       370        380        390        400        410        420 
ILNPVLGDGK YADSLPLFGG LSIWDANPRI IEALKAAGSL MDVQKLSHSY MHCWRHKTPI 

       430        440        450        460        470        480 
IYRATSQWFA GMDVKPADGG PTLRESALAG IDATAFYPSW GRARLHAMIA NRPDWTLSRQ 

       490        500        510        520        530        540 
RQWGVPMAFF VHKETGALHP RTAELLEQVA QRVEQHGIEA WQSLDPRELL GDEADQYEKN 

       550        560        570        580        590        600 
RDTLDVWFDS GTTHATVLGG KDQALGGSHG AELAWPADLY LEGSDQHRGW FHSSLLTGCM 

       610        620        630        640        650        660 
LYGQPPYKAL LTHGFVVDGQ GRKMSKSVGN VIAPQKVSDS LGAEILRLWV ASTDYSGELS 

       670        680        690        700        710        720 
ISDEILKRVV EGYRRIRNTL RFLLANVADF DAVSQAVPYG ELFEIDRYAL TMTAQMQAEV 

       730        740        750        760        770        780 
LAHYERYDFH PAVSRLQTFC SEDLGAFYLD ILKDRLYTTA AGSLARRSAQ TALLDITQAL 

       790        800        810        820        830        840 
LKLMAPILSF TAEEAWQVLA QSALQHQADV SRTTIFTEVY HALPPFADAD ALAAKWARLR 

       850        860        870        880        890        900 
AIRAEVQRKL EDVRTAGGIG SSLQAEVDLY AGGDDRALLA SLGDDLRFVL IVSRATVHEA 

       910        920        930        940        950 
QGELRVEITP SAHKKCERCW HWRLDVGSDA DHPEICGRCV TNLFGAGEPR DKA 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM902716 Genomic DNA. Translation: CAP43156.1.
RefSeqYP_001631424.1. NC_010170.1.

3D structure databases

ProteinModelPortalA9IRC2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340100.Bpet2814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP43156; CAP43156; Bpet2814.
GeneID5817009.
KEGGbpt:Bpet2814.
PATRIC21167146. VBIBorPet31633_2829.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycBPET340100:GJBO-2847-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_BORPD
AccessionPrimary (citable) accession number: A9IRC2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 55 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