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B6J1S2 (SYI_COXB2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:CbuG_1612
OrganismCoxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)) [Complete proteome] [HAMAP]
Taxonomic identifier434923 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length936 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 – 936936Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189143

Regions

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

Sites

Metal binding8991Zinc By similarity
Metal binding9021Zinc By similarity
Metal binding9191Zinc By similarity
Metal binding9221Zinc By similarity
Binding site5611Aminoacyl-adenylate By similarity
Binding site6051ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B6J1S2 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 11B778F5F7F9C450

FASTA936106,126
        10         20         30         40         50         60 
MTDYKDTLNL PQTDFPMRAN LPEREPQTLA RWQTLDLYRK IRKDREGQPK FILHDGPPYA 

        70         80         90        100        110        120 
NGRAHLGTAF NKTLKDIVVK SKTLSGFDAP FVPGWDCHGL PIELNVEKKL GKDKLSANAF 

       130        140        150        160        170        180 
RQACRDYAFS QIELQRDDFQ RLGVLGDWQH PYLTMDFGYE ADTVRALAKI VANGHLLRGQ 

       190        200        210        220        230        240 
KPVHWCAACG SALAEAEVEY RDKASPAVDV GFEAVDAEAV RQRFGVKNAT TRVLVPIWTT 

       250        260        270        280        290        300 
TPWTLPANEA VSVHPELHYA LVKSELQNQP VYLILAKDLV DSAMQRYGVD DYEVHGNLKG 

       310        320        330        340        350        360 
DALEGMQLQH PFLDRIVPII LGEHVTTEAG TGNVHTAPAH GLEDYFVAEK YNLPINNPVD 

       370        380        390        400        410        420 
ARGRFIPDTF LVGGQPVFKA NEPIIVLLAD SGHLLHSETI QHSYPHCWRH KTPLIFRATP 

       430        440        450        460        470        480 
QWFIGMNKNG LRERALAEIE KVTWLPAWGE ARIGKMVADR PDWCISRQRL WGIPIPLFIH 

       490        500        510        520        530        540 
KKSGELHPKS PALMEKVAQL IEKESVDAWF DLDPKVLLGD DADHYEKVTD VLDVWFDSGV 

       550        560        570        580        590        600 
THFCVLEKRR ELKVPADIYL EGSDQHRGWF QSSLLTSLAI RDKAPYKSVL TYGFVVDSQG 

       610        620        630        640        650        660 
RKMSKSLGNV ILPADVVKNL GADVLRLWAA SMDYTVEVNV SDEILKRASD AYRRIRNTAR 

       670        680        690        700        710        720 
FLLSNLYDFD PKKDKVAVDQ LVALDRWAIF TTQKLQEKII TAYDRYRFPA IYQAIHNFCT 

       730        740        750        760        770        780 
VEMGSFYLDI IKDRLYTSKE SGLPRRSAQT ALYYIAEAFV RWIAPIISFT ADEIWQFMPG 

       790        800        810        820        830        840 
DREPSVFLTQ WFSDFPNAAL SGEEEQRWQL LLQIRDEVNK ALETYRNEGK IGSALTAEVV 

       850        860        870        880        890        900 
LYADERLNAA IATLGEELRF VLITSEASVL PFNEKSKAAF DTALPGLALE INVSEFEKCA 

       910        920        930 
RCWQRRSSVG QIKEHADLCD RCVSNAFEDG DMRQFA 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CbuG_Q212.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001019 Genomic DNA. Translation: ACJ18900.1.
RefSeqYP_002304045.1. NC_011527.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434923.CbuG_1612.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ18900; ACJ18900; CbuG_1612.
GeneID7014028.
KEGGcbg:CbuG_1612.
PATRIC17914305. VBICoxBur10955_1611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCBUR434923:GC8S-1609-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.
InterProIPR002300. 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.
ProtoNetSearch...

Entry information

Entry nameSYI_COXB2
AccessionPrimary (citable) accession number: B6J1S2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 39 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