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Q822L8 (SYI_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. 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:CCA_00664
OrganismChlamydophila caviae (strain GPIC) [Complete proteome] [HAMAP]
Taxonomic identifier227941 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length1043 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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 – 10431043Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098531

Regions

Motif49 – 5911"HIGH" region HAMAP-Rule MF_02003
Motif592 – 5965"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5951ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q822L8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 39606F73FF6A6635

FASTA1,043119,911
        10         20         30         40         50         60 
MNTEGESSKE SLANREERIL DFWKTHDIFQ KSLKNREGKT LYSFYDGPPF ATGLPHYGHL 

        70         80         90        100        110        120 
LAGTIKDVVG RFATMDGYYV PRRFGWDCHG VPVEYEVEKS LDLTTPGAIE DFGVAKFNEE 

       130        140        150        160        170        180 
CRKIVFRYVD EWERYVHRLG RWVDFSVTWK TMDASFMESV WWVFRSLYDQ GLVYEGVKVV 

       190        200        210        220        230        240 
PFSTKLGTPL SNFEAGQNYK EVDDPSVVIK FALHGDPASL LVWTTTPWTL VSNMAAAVGP 

       250        260        270        280        290        300 
EITYVRVADK VSGEQWILGQ GCLSRWFSDP DSYEILESFL GTALVGKSYE PPFSFFEHKR 

       310        320        330        340        350        360 
AEGAYKILSG SFVEESEGTG VVHMAPAFGE ADFFVCKEHH VPIVCPVDNH GCFTEEIPEY 

       370        380        390        400        410        420 
QGQYIKSCDK GIIKSLKNLG KVFYHGTVMH RYPFCWRTDT PLIYKTVNSW FVSVEKIKDK 

       430        440        450        460        470        480 
MLRANQKIHW VPEHIKEGRF GKWLDGARDW AISRNRYWGT PIPIWKSKEG EILVIGSVKE 

       490        500        510        520        530        540 
LEELTGEKIS DLHCHFIDQL KVEKEGKTFQ RVPYVFDCWF DSGAMPYAQN HYPFENQKET 

       550        560        570        580        590        600 
EAGFPADFIA EGLDQTRGWF YTLTVISSAL FDQTAFKNAI VNGIVLAEDG NKMSKRLNNY 

       610        620        630        640        650        660 
PSPMGIMNTY GADALRLYLL DSVVVKAEDL RFSDKGVESI LKQILLPLTN VLSFFKTYTD 

       670        680        690        700        710        720 
LYGFDADNYD KEEITYSEID RWILSNLYTV VGKVRESMSS YNLNTAVNPF VTFIDDLTNW 

       730        740        750        760        770        780 
YIRRCRRRFW ESEDTPDRRA AFATLYEVLT VFCRVIAPFI PFISEDIYQQ IKTEHSAESV 

       790        800        810        820        830        840 
HLCDFPHIDL AKVFPDLEQR MSDAREIVGL GHSLRKEHKL KVRQPLANFY IVGPKDRLDE 

       850        860        870        880        890        900 
LTSFEQLIAE ELNVKNIVFY KETPSFVKTT VKPNFRSLGR KVGEKIKDVQ RALSNLSQDQ 

       910        920        930        940        950        960 
IQQLLKQQYL LLNLGFEEIT LGIDDVVISW ETDPGYVARS SSLFTVVLDC QLTEDLIVEA 

       970        980        990       1000       1010       1020 
ISRELVNKIN TMRRNHKLHV SDRILLQIHS SEDVEKAFLH YEDYICEETL TVQFEFKDSV 

      1030       1040 
EGEEWDINGH PTVIALTVAS KAN 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015925 Genomic DNA. Translation: AAP05406.1.
RefSeqNP_829528.1. NC_003361.3.

3D structure databases

ProteinModelPortalQ822L8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227941.CCA00664.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP05406; AAP05406; CCA_00664.
GeneID1218349.
KEGGcca:CCA00664.
PATRIC20270441. VBIChlCav107360_0707.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycCCAV227941:GH8L-690-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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]
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_CHLCV
AccessionPrimary (citable) accession number: Q822L8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 71 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