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Reviewed, UniProtKB/Swiss-Prot Q62CD5 (SYI2_BURMA)

Last modified November 3, 2009. Version 41. 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

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Names and origin

Protein namesRecommended name:
    Isoleucyl-tRNA synthetase 2
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase 2
      Short name=IleRS 2
Gene names
Name: ileS2
Synonyms: ileS-2
Ordered Locus Names: BMAA0963
OrganismBurkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]
Taxonomic identifier13373 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

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Protein attributes

Sequence length967 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 967967Isoleucyl-tRNA synthetase 2 HAMAP MF_02002
PRO_0000098369

Regions

Motif58 – 6811"HIGH" region HAMAP MF_02002
Motif639 – 6435"KMSKS" region HAMAP MF_02002

Sites

Metal binding9221Zinc By similarity
Metal binding9251Zinc By similarity
Metal binding9421Zinc By similarity
Metal binding9451Zinc By similarity
Binding site5981Aminoacyl-adenylate By similarity
Binding site6421ATP By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q62CD5-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 5C51960417CE8A58

FASTA967106,372
        10         20         30         40         50         60 
MSEYKETLNL LQTPFPMKGD LPRREPALVE RWAAQRVYAR MRAAAAGRPP FVLHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHAV NKVLKDIVLK SRFAAGYDAQ WIPGWDCHGM PIEHRIEQLH GRGLPPAAVQ 

       130        140        150        160        170        180 
RLCREYAFEQ TERQRRDFLR LGLLGDWPHA FRTMDFRTEA NELRFLERIR ARGLLYRGQK 

       190        200        210        220        230        240 
PVNWCVDCQS ALAEAELEYA RKTSVAIHAG LRVRDPVDFA SRFRRRPVLD KPAMLVVWTT 

       250        260        270        280        290        300 
TPWTIPGNAA AGVRADAPYG LYDTPGALIV VAQPLADALF ASLGVDHALC ALARGRELVG 

       310        320        330        340        350        360 
LALGQPFFAG RDVPVVEAEF VTLDAGTGIV HLAPAHGAED AELCRRLGIA GENVVDGAGR 

       370        380        390        400        410        420 
FAADLPEIGG LPLADGIARI VAKLRADGTL VREAAFEHAY PHCWRHKTPI LFRSTPQWFI 

       430        440        450        460        470        480 
GMDIECEQGE ADPGRAAVTE EAGATGEARK VGKAEEAEEA GPAKTLRASA RDAIADVPFY 

       490        500        510        520        530        540 
PPSARQRMEA MIDGRPDWCV SRQRTWGVPL PYFVRRDDRS LHPRSARLVE AVAARVERDG 

       550        560        570        580        590        600 
IAAWSRLRPA ELGVDENAYE KLSDTLDVWF DSGSIHATVY RDAARADTGG YPADLYLEGA 

       610        620        630        640        650        660 
DQHRGWFGAS LMTGCAADGR APFRAILTHG FVVDGAGRKM SKSLGNTVSP QRIADTRGAD 

       670        680        690        700        710        720 
ILRLWIASTD YAAEMSISDE ILERVVETYR RMRNTLRFLL QNVADFDPRD DAVPAGQLLD 

       730        740        750        760        770        780 
VDRYALARCR EFVDACRSAY ARYDFVAVTR LAHGYCAEEL GGFYLDALKD RLYASVADGV 

       790        800        810        820        830        840 
ERRAAQTALH SVLANLLISI APILSFTAEE AWTVFAGDER DSVFLHTWDE HAPPPDDAAL 

       850        860        870        880        890        900 
ARWAHVRALR PHVTKALEEA RGAALIGRSS EAELVVRAPR DVLDALAPLH GELAAVFIVA 

       910        920        930        940        950        960 
GVTLETADQI AVAVARTPLA RCERCWRHEP SVAAHASGDA LCARCRHALS RRARAERSEP 


RAAVGSR

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Cross-references

Sequence databases

CP000011 Genomic DNA. Translation: AAU46160.1.
RefSeqYP_105643.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3086173.
GenomeReviewsGene locus BMAA0963 in contig CP000011_GR.
KEGGbma:BMAA0963.
TIGRBMAA0963.

Phylogenomic databases

HOGENOMQ62CD5.
OMAARYDFLA.

Enzyme and pathway databases

BioCycBMAL243160:BMA_A0963-MON.
BRENDA6.1.1.5. 260531.

Family and domain databases

HAMAPMF_02002.
[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.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
[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...

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Entry information

Entry nameSYI2_BURMA
AccessionPrimary (citable) accession number: Q62CD5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 25, 2004
Last modified: November 3, 2009
This is version 41 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)

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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