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A9NBM5 (SYI_COXBR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:COXBURSA331_A0508
OrganismCoxiella burnetii (strain RSA 331 / Henzerling II) [Complete proteome] [HAMAP]
Taxonomic identifier360115 [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_1000088544

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
A9NBM5 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 99D65B215697BC4F

FASTA936106,135
        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 DSAMLRYGVD 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 ARIGKLVADR 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 
LYADERLNAV IATLGEELRF VLITSEASVL PFNEKSKAAF DTALPGLALE INVSEFEKCA 

       910        920        930 
RCWQRRSSVG QIKEHADLCD RCVSNAFEDG EMRQFA 

« Hide

References

[1]"Genome sequencing of phylogenetically and phenotypically diverse Coxiella burnetii isolates."
Seshadri R., Samuel J.E.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RSA 331 / Henzerling II.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000890 Genomic DNA. Translation: ABX77840.1.
RefSeqYP_001596339.1. NC_010117.1.

3D structure databases

ProteinModelPortalA9NBM5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360115.COXBURSA331_A0508.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX77840; ABX77840; COXBURSA331_A0508.
GeneID5792728.
KEGGcbs:COXBURSA331_A0508.
PATRIC17925269. VBICoxBur33747_0527.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCBUR360115:GI0X-513-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_COXBR
AccessionPrimary (citable) accession number: A9NBM5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 48 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