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

B7VJ87 (SYI_VIBSL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:VS_0536
OrganismVibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32)) [Complete proteome] [HAMAP]
Taxonomic identifier575788 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length952 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 – 952952Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189215

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif617 – 6215"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9151Zinc By similarity
Metal binding9181Zinc By similarity
Metal binding9351Zinc By similarity
Metal binding9381Zinc By similarity
Binding site5761Aminoacyl-adenylate By similarity
Binding site6201ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B7VJ87 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 845A0CA06B4F3C80

FASTA952106,624
        10         20         30         40         50         60 
MSDYKDTLNL PETGFPMRGN LANREPEMLK RWYKEDLYGE IRKAKKGKKS FVLHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHAL NKILKDIIIK SKTLSGFDAP YIPGWDCHGL PIELMVEKKK GKPGQKISAA 

       130        140        150        160        170        180 
EFREECRKYA AGQVEGQKES FKRLGIMGEW DKPYRTMDFG TEANIIRSLG KIADKGHLLK 

       190        200        210        220        230        240 
GFKPVHWCTD CGSALAEAEV EYKDKVSPSI DVKFTAADEA ALLEKFTLAE GHAGQGEISI 

       250        260        270        280        290        300 
VIWTTTPWTL PANRAVCLRD DLEYVLIQVE ANGDQPAQRI VVASELAKDV MDRAGIEHFH 

       310        320        330        340        350        360 
NLGFATGADL ELSQFNHPFY NFTVPAVLGD HVTTDSGTGV VHTAPGHGQE DFVVGKKYNL 

       370        380        390        400        410        420 
EIANPVGSNG VYLPDTELFA GQHVFKANDS VLEVLKEKGA LLHHHAYEHS YPHCWRHKTP 

       430        440        450        460        470        480 
IIFRATPQWF ISMDQAGLRA KALESTKSVE WMPEWGQSRI EGMIEGRPEW CISRQRTWGV 

       490        500        510        520        530        540 
PIALFVHKET SELHPDSPAL IEKVAKLVEE KGIQAWWDVD AAELMGAEDA DKYEKVLDTL 

       550        560        570        580        590        600 
DVWFDSGVTH FSVVDSREEY NFPNEERTHS ADLYLEGSDQ HRGWFQSSLI SSIAMKDEAP 

       610        620        630        640        650        660 
YKQVLTHGFV VDGNGRKMSK SIGNVVAPKD VTNKLGADIL RLWVASTDYT NEVAVSDEIL 

       670        680        690        700        710        720 
KRSADAYRRI RNTARFFLAN LNGFNPETDL VPAEEMVALD RWAVGRAQAA QEEIVKAYGE 

       730        740        750        760        770        780 
YNTHGVTQRL MQFCSIEMGS FYLDVIKDRQ YTAKQGSHAQ RSCQTALYYI VEALVRWMAP 

       790        800        810        820        830        840 
IMSFTADEIW NEMPGERDTF VFTGEWFEGL FGLADDEELS NEFWTEIQSV RGAVNKLLED 

       850        860        870        880        890        900 
ARKEKTIGGA LQAEVTLYAD DALAAKINKL EDELRFVLIT SAAVVKPLSD KSDTAQATDV 

       910        920        930        940        950 
EGLYVEVAAT EAEKCDRCWH HTPDVGTIEG HEKICGRCVS NIDGEGEVRK FA 

« Hide

References

[1]"Vibrio splendidus str. LGP32 complete genome."
Mazel D., Le Roux F.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LGP32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM954972 Genomic DNA. Translation: CAV17541.1.
RefSeqYP_002416191.1. NC_011753.2.

3D structure databases

ProteinModelPortalB7VJ87.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING575788.VS_0536.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAV17541; CAV17541; VS_0536.
GeneID7160168.
KEGGvsp:VS_0536.
PATRIC20151772. VBIVibSpl48387_1900.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycVSPL575788:GH64-517-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_VIBSL
AccessionPrimary (citable) accession number: B7VJ87
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 42 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