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B2JDY9 (SYI_BURP8) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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:Bphy_0574
OrganismBurkholderia phymatum (strain DSM 17167 / STM815) [Complete proteome] [HAMAP]
Taxonomic identifier391038 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length945 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 – 945945Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189139

Regions

Motif66 – 7611"HIGH" region HAMAP-Rule MF_02002
Motif622 – 6265"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Metal binding9281Zinc By similarity
Metal binding9311Zinc By similarity
Binding site5811Aminoacyl-adenylate By similarity
Binding site6251ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2JDY9 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 0120E0713516D61C

FASTA945105,999
        10         20         30         40         50         60 
MSNKKADSKP QARYPVNLLD TPFPMRGDLP RREPQWVKDW QERKIYEKIR AASKGRKKFI 

        70         80         90        100        110        120 
LHDGPPYANG DIHLGHAVNK ILKDMIVKAR NLAGFDAVYV PGWDCHGMPI EIQIEKQFGK 

       130        140        150        160        170        180 
SLPAAEVMQK ARAYATEQIE KQKAGFRRLG VLGDWDNPYK TMNFANEAGE IRALAKIMEK 

       190        200        210        220        230        240 
GYVFRGLKPV NWCFDCGSAL AEAEVEYKDK TDPTIDVMFT FADPEKTAHA FGLAALPRNE 

       250        260        270        280        290        300 
GGIVIWTTTP WTIPANQALN LHPEIVYALV DTPRGLLILA EERVEACLKS YGIAGTVIAT 

       310        320        330        340        350        360 
APGAKLANLR FNHPLASAHP SYKRTSPVYL GDYVTTETGT GIVHSSPAYG VEDFISCKTH 

       370        380        390        400        410        420 
GMADSDILSP VMGDGRYIES LALFGGLSIW DANPKIVEAL DEAGTLLRTE KYLHSYMHCW 

       430        440        450        460        470        480 
RHKTPIIYRA TSQWFAGMDI KPNDSDKTLR ETALEGIEAT AFYPSWGKQR LFAMIANRPD 

       490        500        510        520        530        540 
WTLSRQRQWG VPMAFFVHKE TGELHPRTLE LLEEVAKRVE VSGIEAWQTL DPRELIGDDA 

       550        560        570        580        590        600 
NMYEKNRDTL DVWFDSGTTH WHVLRGSHKD ELQFPADLYL EGSDQHRGWF HSSLLTASML 

       610        620        630        640        650        660 
DGRPPYNALL THGFTVDGEG RKMSKSLGNG IDPHEVSNRL GAEIIRLWIA STDYSGELAI 

       670        680        690        700        710        720 
SEEILKRVTE SYRRIRNTLR FLLANLSDFD IGKHARPVGE WLEIDRYAVA LTANLQADIL 

       730        740        750        760        770        780 
SHYDRYEFHP VVAKLQTFCS EDLGGFYLDV LKDRLYTTAA DSKARRSAQT ALYHIAHGLL 

       790        800        810        820        830        840 
RLMAPFLSFT AEEAWKVFQP QSETIYTETY HAYPDVPEAS TLLDKWTLLR AVRSDVTKAL 

       850        860        870        880        890        900 
EEARVANQIG SSLQAEVEIR AAGARHDALA SLGADLKFVL ITSGATVVKV DSVDEEGVDV 

       910        920        930        940 
ITSKYLKCER CWHYRKDVGE SAEHPTLCGR CISNLFGNGE TRSAA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phymatum STM815."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D., Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Bacher J., Blanchard J., Cohan F., James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P., Riley M., Souza V., Wertz J., Young P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17167 / STM815.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001043 Genomic DNA. Translation: ACC69765.1.
RefSeqYP_001856811.1. NC_010622.1.

3D structure databases

ProteinModelPortalB2JDY9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391038.Bphy_0574.

Proteomic databases

PRIDEB2JDY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC69765; ACC69765; Bphy_0574.
GeneID6242074.
KEGGbph:Bphy_0574.
PATRIC19187293. VBIBurPhy25146_0602.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBPHY391038:GI4Z-580-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_BURP8
AccessionPrimary (citable) accession number: B2JDY9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 10, 2008
Last modified: April 16, 2014
This is version 46 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