Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q74JX6 (SYI_LACJO) 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:LJ_0980
OrganismLactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) [Complete proteome] [HAMAP]
Taxonomic identifier257314 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length928 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.

Sequence caution

The sequence AAS08801.1 differs from that shown. Reason: Erroneous initiation.

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 – 928928Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098402

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif595 – 5995"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8871Zinc By similarity
Metal binding8901Zinc By similarity
Metal binding9071Zinc By similarity
Metal binding9101Zinc By similarity
Binding site5541Aminoacyl-adenylate By similarity
Binding site5981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q74JX6 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 4A2477DC031533A6

FASTA928105,960
        10         20         30         40         50         60 
MRVKDTLNLG KTKFKMRGNL PVREAEWQKE WEENKLYEQR LKLNEGKPRF DLHDGPPFAN 

        70         80         90        100        110        120 
GNIHMGHSLN KISKDIIVRF KNMNGYYAPY VPGWDTHGLP VEQQLAKKGV DRKTMDRAKY 

       130        140        150        160        170        180 
RELCRQFAEE QVQKQMADFK RLGVMADWDH PYITLQPKFE AEEIRVFGEM FKKGYIYKGK 

       190        200        210        220        230        240 
KPVYWSWSSE STLAEAEVEY HDIKSPRIYV AFPIKDGKGI LDSDTSLVIW TTTPWTIPSN 

       250        260        270        280        290        300 
VGITVNPKFD YSVVEVNGKK YVIGSQRLSA VAEDLGWEDY KVVKTLKGTD FDRMTYQHPL 

       310        320        330        340        350        360 
YDVTGVIMND TYVTADDGTG LVHNATGFGE DDYNVGRRYG LPVFSPMDAQ GRFTKEVPDP 

       370        380        390        400        410        420 
DLVGMFYDDA NKVVADKLEK AGALLKLSFF THSYPHDWRT KKPVIYRATT QWFASIDKFR 

       430        440        450        460        470        480 
DQILAEIEKA NFIPAWGKTR LYNMIKDRGD WVISRQRAWG VPLPIFYAED DTPIVTPETI 

       490        500        510        520        530        540 
EHVAQIFEKE GSNAWYTYTA EELLPEGFKS EHSPNGKFRK ETDILDVWFD SGSSWAGVMQ 

       550        560        570        580        590        600 
ERDGLGFPAD LYLEGSDQYR GWFNSSLITS VAVTGKAPYK QVLSQGFVLD DKGHKMSKSL 

       610        620        630        640        650        660 
GNVISPNDVI KQMGAEIIRL WVAGADTTSD VAVSQDILRQ SAESYRKIRN TMRFMLANTS 

       670        680        690        700        710        720 
DFDPKEDAIA YPDMSGVDQY MEIKLNRLIE EAIEAYNKFD FNSVYKKVFS FISNDLSAFY 

       730        740        750        760        770        780 
LDFAKDILYI DAEDSETRRS MQTVIYDVLV KLTKLMTPIL PHTMEEVWGY LKEPEDYVQL 

       790        800        810        820        830        840 
ANMPEVDHFA NEDEVLADWN AFMKVRSDVL KALEKARNAK VIGKSFEAHV TLYPTEETKA 

       850        860        870        880        890        900 
LLDKLNANIR QILIVSDLTI SDEEAPENAE KLPTASIVVE HAAGEVCPRC RRTTTDVGSD 

       910        920 
PRFPELCARC AAIVAENFPE AEKEGLEK 

« Hide

References

[1]"The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533."
Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.
Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNCM I-1225 / La1 / NCC 533.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017198 Genomic DNA. Translation: AAS08801.1. Different initiation.
RefSeqNP_964835.1. NC_005362.1.

3D structure databases

ProteinModelPortalQ74JX6.
SMRQ74JX6. Positions 1-916.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257314.LJ0980.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS08801; AAS08801; LJ_0980.
GeneID2742127.
KEGGljo:LJ0980.
PATRIC22238322. VBILacJoh1832_0839.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycLJOH257314:GJN3-844-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_LACJO
AccessionPrimary (citable) accession number: Q74JX6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 71 of the entry and version 2 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