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P0C124 (SYI_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BAB2_0194
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length972 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

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
Nucleotide-binding
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 972972Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098362

Regions

Motif63 – 7311"HIGH" region HAMAP-Rule MF_02002
Motif644 – 6485"KMSKS" region HAMAP-Rule MF_02002

Sites

Binding site6031Aminoacyl-adenylate By similarity
Binding site6471ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C124 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 439543DEDCC20013

FASTA972110,042
        10         20         30         40         50         60 
MTDTTKIDYS KTLYLPQTEF PMRAGLPQRE PLFVQRWEEM NLYKKLREQA KDRPLYVLHD 

        70         80         90        100        110        120 
GPPYANGNIH IGHALNKILK DVITRSFQMR GYNSNYVPGW DCHGLPIEWK IEEKYRAAGK 

       130        140        150        160        170        180 
NKDEVPINEF RKECREFASN WIKVQTEEFK RLAILGDFEN PYTTMNFHAE ARIAGELLKF 

       190        200        210        220        230        240 
AASGQLYRGS KPVMWSVVER TALAEAEVEY HDIESDMIWV KFPVAGEVAT ENDLSGSAVV 

       250        260        270        280        290        300 
IWTTTPWTIP GNRAVSYSSR IEYGLFEITE AENDFGPRPG ERLVFADKLV EECCAKAKLQ 

       310        320        330        340        350        360 
FKRLRSVSAE ELGKIVLDHP LKGFGGGYEF VVPMLDGDHV TDDAGTGFVH TAPSHGREDF 

       370        380        390        400        410        420 
EAWMDNARQL EARGIDPNIP FPVGDDGFYT KDAPGFGPDR EGGPARVIDD NGKKGDANKV 

       430        440        450        460        470        480 
VIEQLIAADK LFARGRLKHS YPHSWRSKKP VIFRNTPQWF VYMDKNLGDG TTLRSRALKA 

       490        500        510        520        530        540 
IDETRFVPAA GQTRLRSMIE GRPDWVLSRQ RAWGVPICVF VDEEGNILQD DAVNKRIMDA 

       550        560        570        580        590        600 
FEKEGADAWF ADGARERFLG ARAGEGWTQV RDILDVWFDS GSTHTFTLED RPDLKWPADV 

       610        620        630        640        650        660 
YLEGSDQHRG WFHSSLLESC GTRGRAPYNA VVTHGFTMDE HGKKMSKSLG NTVTPQDVIK 

       670        680        690        700        710        720 
ESGADILRLW VMTTDYWEDQ RLGKSIIQTN IDAYRKLRNT IRWMLGTLAH DEGENVAYAD 

       730        740        750        760        770        780 
LPELERLMLH RLTELDELVR SGYDTFDFKR IARALVDFMN VELSAFYFDI RKDALYCDAP 

       790        800        810        820        830        840 
SSIRRKAALQ TVREIFVRLT TWLAPMLPFT MEEAWLDRYP QSVSIHAEQF RPTPAEWRDD 

       850        860        870        880        890        900 
VLAEKWRKVR AVRRVVTGAL ELERADKRIG SSLEAAPVVY IADKSLSDSL EGLDFAEICI 

       910        920        930        940        950        960 
TSGISVSDAA APEGAFTLGD VKGVAVVPER AKGEKCARSW RYTTDVGADP EFPEVSARDA 

       970 
AALRELQALG KL 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040265 Genomic DNA. Translation: CAJ12360.1.
RefSeqYP_418423.1. NC_007624.1.

3D structure databases

ProteinModelPortalP0C124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB2_0194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ12360; CAJ12360; BAB2_0194.
GeneID3827171.
KEGGbmf:BAB2_0194.
PATRIC17847892. VBIBruMel86222_2479.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycBABO359391:GKDV-2437-MONOMER.
BMEL359391:GJOQ-2437-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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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_BRUA2
AccessionPrimary (citable) accession number: P0C124
Secondary accession number(s): Q579P3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 57 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

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries