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Q68WC2 (SYI_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. 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:RT0606
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length1086 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 – 10861086Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098561

Regions

Motif53 – 6311"HIGH" region HAMAP-Rule MF_02003
Motif624 – 6285"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6271ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q68WC2 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 02F4A7D6A1934203

FASTA1,086125,447
        10         20         30         40         50         60 
MTNTKYYPDV SANVDFAAIE REILKFWQNN NIFQKSIDHR DGESEFIFYD GPPFANGLPH 

        70         80         90        100        110        120 
YGHLLTGFIK DVYARYQTVK GKKVERRFGW DCHGLPAEMQ SEKELGISGR LAITNFGIEK 

       130        140        150        160        170        180 
FNNHCRASVM QYASEWKQYV TRQARWVAFD NAYKTMDKNF MESVLWAFKE LYNKGLLYES 

       190        200        210        220        230        240 
MRVMPYSWAC ETPLSNFETR LDNSYRERTD KAITVSFMLN DITLFNSMIS QKLGMTGGDN 

       250        260        270        280        290        300 
FKEYRILAWT TTPWTLPANL ALAVGSDIDY ALVNKNDVCY IIAASSVAKY AKELGLSGKE 

       310        320        330        340        350        360 
NFEIIKGLKL QGLSYKPLFN YFENHPNSFK IFASNFVVEG EGTGIVHMAP GFGEDDQILC 

       370        380        390        400        410        420 
ESKGIELVCP VDNSGKFTKE IPDLEGVQVF DANDKIIIKL KEQGNWIKTE QYIHNYPHCW 

       430        440        450        460        470        480 
RTDTPLIYKA VPSWYVRVTQ FKDRMVELNQ QINWIPHNVK DNLFGKWLEN ARDWSISRNR 

       490        500        510        520        530        540 
FWGTPLPVWK SDDPKYPRID VYGSIEEIEQ DFGVKINDLH RPFIDELTRT NPDDPTGKSI 

       550        560        570        580        590        600 
MRRIDDVFDC WFESGSMPYG QAHYPFENKK WFVEHFPADF IVEYSSQTRG WFYTLIVLST 

       610        620        630        640        650        660 
ALFDRPPFLN CICHGVILDA TGQKLSKRLN NYADPLELFD RYGSDALRVT MLSSNVVKGQ 

       670        680        690        700        710        720 
ELLIDKDGKM IFDTLRLFIK PIWNAYHFFT IYANADALKG TLNFTSQNVL DIYILSKLKI 

       730        740        750        760        770        780 
AVNKIEESLD NFDTQTAYHA VSEFFEVLNN WYIRRSRARF WKKEKDTDKQ NAYNTLYSCL 

       790        800        810        820        830        840 
ETMTIAMSAL VPMISEAIYQ GLHNTAITQL NCLLLEGKHV VQNPMSGTQD YNTSVHLCNY 

       850        860        870        880        890        900 
PTLSDFEINH ELVSTMDNVL DICSNSLFIR STKNIRVRQP LACITIISKH NNNLKDFEDL 

       910        920        930        940        950        960 
IKDEINVKTV IYRDDLENYA HKKLSLNFAI LGKRLPHKMK AIIDASKKGE WETSTLGLVI 

       970        980        990       1000       1010       1020 
CGEILNSNEY KLVLEPHSHI KGTANFENNS SLLILDLELT SELIEEGYAR DIIRFIQHAR 

      1030       1040       1050       1060       1070       1080 
KEADFSITDK ILIEIISEFD LSKIIENYGD FIKEQTLGEF AKNFMPDYVS KVALENNLIQ 


LKVKRL 

« Hide

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017197 Genomic DNA. Translation: AAU04070.1.
RefSeqYP_067552.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ68WC2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257363.RT0606.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU04070; AAU04070; RT0606.
GeneID2958495.
KEGGrty:RT0606.
PATRIC17910454. VBIRicTyp34752_0627.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycRTYP257363:GJEQ-637-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. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_RICTY
AccessionPrimary (citable) accession number: Q68WC2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 65 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

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries