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Q5LNR7 (SYI_RUEPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:SPO3136
OrganismRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) [Complete proteome] [HAMAP]
Taxonomic identifier246200 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length970 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 – 970970Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098462

Regions

Motif65 – 7511"HIGH" region HAMAP-Rule MF_02002
Motif649 – 6535"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9431Zinc By similarity
Metal binding9461Zinc By similarity
Metal binding9621Zinc By similarity
Metal binding9651Zinc By similarity
Binding site6081Aminoacyl-adenylate By similarity
Binding site6521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LNR7 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 6A84B8DB96390B75

FASTA970109,796
        10         20         30         40         50         60 
MCADTTAETP EYKDTLNLPK TDFPMRAGLP AREPQWLERW EKIGVYDRLR EKQGRAPFTL 

        70         80         90        100        110        120 
HDGPPYANGH LHIGHALNKT IKDMIVRSHQ MMGFDARYVP GWDCHGLPIE WKIEEQYRKK 

       130        140        150        160        170        180 
GKSKDDVNVV EFRQECRRFA EGWIDIQREE FKRLGITGNW ADPYVTMDYH AEAVIADEFM 

       190        200        210        220        230        240 
KFLMNGTLYQ GSKPVMWSPI EQTALAEAEV EYHDKESFTI WVKFRAVNSG DLDGAQVVIW 

       250        260        270        280        290        300 
TTTPWTIPSN KAVVYGKDIA YGLYEITGTP EECWASVGDK YILADKLADD VMRRARLDPD 

       310        320        330        340        350        360 
MYRRVGDVDP SQIGGLTHPL HGAEGGNGEW DDIRDFRAAE FVTDTEGTGF VHCAPSHGME 

       370        380        390        400        410        420 
EFELYRDLGM LEQVITYNVM DDGSFRADLP FFGGKYILSR KGGEGDANKT VIDKLVEVGG 

       430        440        450        460        470        480 
LLARGKIKHS YPHSWRSKAP IIYRNTPQWF ASVDRPVNDG QDSYGKTIRE RALTSIDQLV 

       490        500        510        520        530        540 
KFTPQTGRNR LYSMIEARPD WVLSRQRAWG VPLTCFTRKG ALPTDADFLL RDPAVNARIF 

       550        560        570        580        590        600 
AAFEAEGADC WYAEGAKERF LGNDYKADEW DQVFDVLDVW FDSGSTHAFV LRDREDGTAD 

       610        620        630        640        650        660 
GIADVYMEGT DQHRGWFHSS LLQACGTLGR APYRNVVTHG FTLDEKGMKM SKSLGNTIVP 

       670        680        690        700        710        720 
DEVVKQYGAD ILRLWVAQTD YTADQRIGPE ILKGVADSYR RLRNTMRFML GSLSDFTEAD 

       730        740        750        760        770        780 
RIEDPAEMPP LERWVLSRMA ELDEQVRKGY AGFDFQGVYS AVFNFATVDL SAFYFDIRKD 

       790        800        810        820        830        840 
VLYCDGDTTR RRAARTVLDL LFHRLTTWLA PILVFTMEEV WLERYPGEGS SVHLVDFPET 

       850        860        870        880        890        900 
PASWRNPQNE SNVARVRRVR RVVTAALEIQ RRDKVIGSSL EAAPVVHVED AETRALLAQI 

       910        920        930        940        950        960 
DIDDLCITSG LTVSADPAPA EAFRLPEIEG VGVVFEMAEG EKCQRCWKIL PDVGRHAHAG 

       970 
VCGRCDAALG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000031 Genomic DNA. Translation: AAV96371.1.
RefSeqYP_168339.1. NC_003911.12.

3D structure databases

ProteinModelPortalQ5LNR7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246200.SPO3136.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV96371; AAV96371; SPO3136.
GeneID3193197.
KEGGsil:SPO3136.
PATRIC23379717. VBIRuePom114501_3202.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAERLMLHQ.
OrthoDBEOG644ZM1.

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.
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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_RUEPO
AccessionPrimary (citable) accession number: Q5LNR7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 72 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