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A9VTD5 (SYI_BACWK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. 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:BcerKBAB4_3722
OrganismBacillus weihenstephanensis (strain KBAB4) [Complete proteome] [HAMAP]
Taxonomic identifier315730 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length921 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 – 921921Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189129

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif593 – 5975"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8881Zinc By similarity
Metal binding8911Zinc By similarity
Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Binding site5521Aminoacyl-adenylate By similarity
Binding site5961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9VTD5 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 60E6FB75EAF633D3

FASTA921104,479
        10         20         30         40         50         60 
MEYKNTLLMP KTEFPMRGNL PKREPAMQEK WAEMNIYEKV QEHTKGRPLF VLHDGPPYAN 

        70         80         90        100        110        120 
GDIHMGHALN KVLKDFIVRF KSMTGYCAPY VPGWDTHGLP IEQALTNKGV KRKEMTVAEF 

       130        140        150        160        170        180 
RKLCAEYAYE QVERQREQFK RLGVRADWDN PYITLEPAYE AQQIKVFGDM AKKGYIYKGQ 

       190        200        210        220        230        240 
KPVYWSPTSE SALAEAEIEY QDKKSASIYV AFPVKDGKNV LEGDEKYIIW TTTPWTLPAN 

       250        260        270        280        290        300 
LGISVHPELE YAIVKVNDEK YIIASELFET VAKTLEWENA EVVKTVKGSE LEYTVAKHPF 

       310        320        330        340        350        360 
YDRDSLVMLG EHVTTDAGTG CVHTAPGHGE DDFVVGKKYG LEVLCPVDDK GVLTNEAPGF 

       370        380        390        400        410        420 
EGLFYDKANK PITEKLEEVG ALLKLTFITH SYPHDWRTKK PIIFRATAQW FASIEAFRKE 

       430        440        450        460        470        480 
LLEAVAETKW VPAWGETRLH NMVRDRGDWC ISRQRAWGVP IPVFYAENGD PIITDETINH 

       490        500        510        520        530        540 
VADLFREHGS NVWFEREAKD LLPEGFTHTG SPNGEFRKET DIMDVWFDSG SSHQAVLEER 

       550        560        570        580        590        600 
EDLQRPADLY LEGSDQYRGW FNSSLSTAVA VTGKAPYKGV LSHGFVLDGE GRKMSKSIGN 

       610        620        630        640        650        660 
IVVPKKIMDQ LGGDILRLWV SSVDYQSDVR ISDDILKQVA EVYRKIRNTF RFLLGNLDDF 

       670        680        690        700        710        720 
NPSENTVAVA ELREVDRYML VKLNDLITKV KDAYETYDFA AVYHAIHNFC TIDLSSFYLD 

       730        740        750        760        770        780 
FAKDILYIEG ADHADRRAIQ TVLYDVLVAL TKLVTPILPH TADEVWPYVP GAEEESVQLT 

       790        800        810        820        830        840 
NMPEATEVEG SEALRAKWDA FMTLRDDVLK ALEVARNEKV IGKSLNASIT LYPTAEMKAM 

       850        860        870        880        890        900 
LESISEDLKQ LFIVSEYKLG GTIEEAPTEA PKYEHTAVVV AQATGETCER CWVVSETIGK 

       910        920 
DAEHETLCER CATVVKENYV K 

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References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KBAB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000903 Genomic DNA. Translation: ABY44891.1.
RefSeqYP_001646519.1. NC_010184.1.

3D structure databases

ProteinModelPortalA9VTD5.
SMRA9VTD5. Positions 2-883.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315730.BcerKBAB4_3722.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY44891; ABY44891; BcerKBAB4_3722.
GeneID5843934.
KEGGbwe:BcerKBAB4_3722.
PATRIC19012079. VBIBacWei55973_4356.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBWEI315730:GHRU-3837-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_BACWK
AccessionPrimary (citable) accession number: A9VTD5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 54 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