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Reviewed, UniProtKB/Swiss-Prot Q39DM8 (SYI_BURS3)

Last modified February 9, 2010. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Isoleucyl-tRNA synthetase
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase
      Short name=IleRS
Gene names
Name: ileS
Ordered Locus Names: Bcep18194_A5844
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

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 MF_02002

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02002

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_02002

Subunit structure

Monomer By similarity. HAMAP MF_02002

Subcellular location

Cytoplasm By similarity HAMAP 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 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 945945Isoleucyl-tRNA synthetase HAMAP MF_02002
PRO_1000022048

Regions

Motif66 – 7611"HIGH" region HAMAP MF_02002
Motif622 – 6265"KMSKS" region HAMAP 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
Q39DM8-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: C6F393E268E23A29

FASTA945105,866
        10         20         30         40         50         60 
MSNKKADSKP QAKYPVNLLD TPFPMRGDLP KREPQWVKEW EERGIYEKIR AASAGRPKFI 

        70         80         90        100        110        120 
LHDGPPYANG DIHLGHAVNK ILKDIVVKSR NMAGFDAPYV PGWDCHGMPI EIQIEKQFGK 

       130        140        150        160        170        180 
SLPAAEVMSK ARAYATEQIE KQKVGFKRLG VLGDWANPYK TMNFVNEAEE LRALGKIIEK 

       190        200        210        220        230        240 
GYVYRGLKPV NWCFDCGSAL AEAEVEYKDR TDPTIDVMFA FAEPEKTAQA FGLPALPRAE 

       250        260        270        280        290        300 
GGIVIWTTTP WTIPANQALN LHPEIVYALV DTERGLLIIA EERVEACMTD FKLTGRVVAT 

       310        320        330        340        350        360 
APGVKLAGLR FHHPLASAHP GYKRTAPVYL GDYVTTDTGT GVVHSSPAYG IEDFVSCKAH 

       370        380        390        400        410        420 
GMTDSDFINP VMGDGRYIES LPLFGGLSIW DANPKIVEAL NAAGSLLRSE KYTHSYMHCW 

       430        440        450        460        470        480 
RHKTPIIYRA TSQWFAGMDV TPRDGGKTLR ETALEGVDAT AFYPSWGKQR LFSMIANRPD 

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

       550        560        570        580        590        600 
NLYEKNRDTL DVWFDSGTTH WHVLRGSHKD QLQFPADLYL EGSDQHRGWF HSSLLTASMI 

       610        620        630        640        650        660 
DGRAPYKGLL THGFTVDGEG RKMSKSLGNG IDPHEVANRL GAEIIRLWIA STDYSGELAI 

       670        680        690        700        710        720 
SEEILKRVTE GYRRIRNTLR FLLANLSDFD FAQHAVPVDE WLEIDRYAVA FSQQLQTELL 

       730        740        750        760        770        780 
GHYEKYEFHP VVAKLQTYCS EDLGGFYLDV LKDRLYTSAA DSRARRSAQT ALYHLTHGLL 

       790        800        810        820        830        840 
RVLAPFLSFT AEEAWKVFQP ASDTIYTETY YAYPEVAGSA ALIEKWALLR DVRGNVTKAL 

       850        860        870        880        890        900 
EEARTANRIG SSLQAEVAVH ASGARYDALT SLGDDLKFVL ITSAATVVKV DDEAQESVDV 

       910        920        930        940 
AASKYQKCER CWHYREDVGA HADHPTLCGR CFSNLFENGE IRSAA 

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References

[1]"Complete sequence of chromosome 1 of Burkholderia sp. 383."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000151 Genomic DNA. Translation: ABB09438.1.
RefSeqYP_370082.1.

3D structure databases

SMRQ39DM8. Positions 13-935.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39DM8.

Genome annotation databases

GeneID3751075.
GenomeReviewsGene locus Bcep18194_A5844 in contig CP000151_GR.
KEGGbur:Bcep18194_A5844.
NMPDRfig|269483.3.peg.6621.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHBG577712.
OMAKQVLTHG.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_A5844-MONOMER.

Family and domain databases

HAMAPMF_02002. Ile_tRNA_synth_type1.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR010663. DNA_glyclase/IsotRNA_synth_Znf.
IPR002301. Ile-tRNA-synt_Ia.
IPR015905. Ile-tRNA-synt_Ia_N.
IPR018353. Isoleucyl-tRNA_synthetase.
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_Ia_edit.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_BURS3
AccessionPrimary (citable) accession number: Q39DM8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: February 9, 2010
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents