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A5IFX5 (SYI_LEGPC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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:LPC_2353
OrganismLegionella pneumophila (strain Corby) [Complete proteome] [HAMAP]
Taxonomic identifier400673 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length931 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 – 931931Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022087

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif600 – 6045"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8941Zinc By similarity
Metal binding8971Zinc By similarity
Metal binding9141Zinc By similarity
Metal binding9171Zinc By similarity
Binding site5591Aminoacyl-adenylate By similarity
Binding site6031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5IFX5 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: E02C6D9F6C2A3DFA

FASTA931105,933
        10         20         30         40         50         60 
MAEYKDTLNL PNTSFPMKAS LSVREPEMLA DWQAKGIYQK IRKARVGSKR FILHDGPPYA 

        70         80         90        100        110        120 
NGHLHCGHAL NKILKDIIIK SKTFSGFDAP FVPGWDCHGL PIELNVEKKV GKAGSKISPR 

       130        140        150        160        170        180 
EFRAKCREYA ASQIDIQRDE FQRLGVLGDW YNPYVTMDYH YEANIVRALG LMIKNGHLQQ 

       190        200        210        220        230        240 
GFKPVHWCID CGSALAEAEV DYEDKTSPSI DVAFSAVNPS EFLNCFETQP AVKPLILPIW 

       250        260        270        280        290        300 
TTTPWTLPAN EAVCLHPEID YALIDAGNSY YIVATDLVES VMARYGISHY KTSGFAKGRV 

       310        320        330        340        350        360 
FEHFKLQHPF YKRQVPVVLA EHVTTESGTG CVHTAPAHGP DDYLVGQSYQ LPLINPVMAN 

       370        380        390        400        410        420 
GCFAENVELF AGISVLKANE TILAVLSERN VLLASESIRH SYPHCWRHKS PMIFLATPQW 

       430        440        450        460        470        480 
FISMDKSNLR QAIINEIDKV NWVPDWGKAR ISNMVENRPD WCISRQRSWG TPMPLFVHKT 

       490        500        510        520        530        540 
TRELHPDTLE LIERVAVMIE KSGIDAWFDL DSSELLGDDA KHYDKITDTM DVWLDSGISH 

       550        560        570        580        590        600 
YSVLKHNNDL DFPADVYFEG SDQHRGWFNS SLTTAVAMYG VAPYKTVLTH GYTVDAEGKK 

       610        620        630        640        650        660 
LSKSKGNYVA LDKLVNQHGA DILRLWVAST DYRHEVSISE EIIKRNADAY RRIRNTARFL 

       670        680        690        700        710        720 
LANLFDFNPA SDCIDAKELL ELDRWALKRC QLLQEEIITA YENYHFHLIY QKIHNFCAVD 

       730        740        750        760        770        780 
MGSFYLDLIK DRQYTTAKDS IARRSCQTAM YHMVKAFTIW LAPILSFTAE EIWQTIPGNN 

       790        800        810        820        830        840 
SESIFIEHWY NAWPTIDAVN MEDWEQLHIV RDEVNKALEE TRQRGEIGSA LAAEVTVYAD 

       850        860        870        880        890        900 
AKVLPKLTRL GEELRFLFIT SEAKACPISQ SPKGLAVTDC GVSIQVTASV HEKCARCWHR 

       910        920        930 
REDVGQNQEH PELCLRCVGN ISRYHEERLY I 

« Hide

References

[1]"Identification and characterization of a new conjugation/ type IVA secretion system (trb/tra) of L. pneumophila Corby localized on a mobile genomic island."
Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Corby.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000675 Genomic DNA. Translation: ABQ56275.1.
RefSeqYP_001251621.1. NC_009494.2.

3D structure databases

ProteinModelPortalA5IFX5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING400673.LPC_2353.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ56275; ABQ56275; LPC_2353.
GeneID5180184.
KEGGlpc:LPC_2353.
PATRIC22311275. VBILegPne45588_2450.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycLPNE400673:GCIT-1047-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.
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_LEGPC
AccessionPrimary (citable) accession number: A5IFX5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 51 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