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Q65JV7 (SYI_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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:BLi01762, BL02267
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length922 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 – 922922Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098350

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif594 – 5985"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8891Zinc By similarity
Metal binding8921Zinc By similarity
Metal binding9091Zinc By similarity
Metal binding9121Zinc By similarity
Binding site5531Aminoacyl-adenylate By similarity
Binding site5971ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65JV7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: DFCB33B0F71906B6

FASTA922104,356
        10         20         30         40         50         60 
MDYKDTLLMP KTDFPMRGNL PNREPEIQGK WEDMDIYSLV QKRTEGRPMF VLHDGPPYAN 

        70         80         90        100        110        120 
GDIHMGHALN KVLKDFIVRS RSMSGYHAPY VPGWDTHGLP IETALTKNKK VKRKEMTVAE 

       130        140        150        160        170        180 
FRKLCEEYAW QQIEGQKAQF KRLGVRGDWE NPYVTLKPEF EAQQIKVFGE MAKKGYIYKG 

       190        200        210        220        230        240 
KKPVYWSPSS ESALAEAEIE YHDKRSPSIY VAFDVKDGKG VLTNGEKIVI WTTTPWTIPA 

       250        260        270        280        290        300 
NLGIAVHPEL EYSVVAAGGA RYVMASALIE SVAKAIGFED HEVVQTVKGK DLEHIVAVHP 

       310        320        330        340        350        360 
LYGRDSLVML GEHVTTDAGT GCVHTAPGHG EDDFIIGQKY GLDVLCPVDE KGHMTSEAPG 

       370        380        390        400        410        420 
FEGLFYDQAN KPITEQLEEK GALLKLDFIT HSYPHDWRTK KPTIFRATAQ WFASIKDFRD 

       430        440        450        460        470        480 
ELLEAVKKTK WVPEWGETRL YNMIRDRGDW CISRQRAWGV PIPVFYAENG EPIITDETIN 

       490        500        510        520        530        540 
HVSELFREHG SNIWFEKEAN ELLPEGFTHP GSPNGKFTKE QDIMDVWFDS GSSHQAVLEE 

       550        560        570        580        590        600 
REDLVRPADL YLEGSDQYRG WFNSSISTAV AVTGKAPYKG VLSHGFALDG EGRKMSKSLG 

       610        620        630        640        650        660 
NVVVPAKIMN QFGADILRLW VASVDYQADV RVSDAILKQV AEVYRKIRNT FRFLHGNIAD 

       670        680        690        700        710        720 
FDPAKDAIAV EDLREVDQYI LIKLNSLIEK VKKAYEEYDF AVIYHAVHNF CAIELSSFYM 

       730        740        750        760        770        780 
DFAKDVVYIE HADHKDRRSM QTVFYETLLA LVKLIAPILP HTADEMWSHF TFVSEKSVQL 

       790        800        810        820        830        840 
TDMPETRDIP NAKETEEKFD SFMKLRDDVL KALETARNEK IIGKSSVASL TLYPNEEAKA 

       850        860        870        880        890        900 
LLSSIKEDVK QLFIVSELAI GGTEADAPED AQSFETGKIV VAQAEGETCE RCRMVSKEIG 

       910        920 
EDPDHPELCP RCAGIVKTYY QN 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU40657.1.
CP000002 Genomic DNA. Translation: AAU23298.1.
RefSeqYP_006713139.1. NC_006322.1.
YP_078936.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65JV7.
SMRQ65JV7. Positions 1-918.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL02267.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU23298; AAU23298; BL02267.
AAU40657; AAU40657; BLi01762.
GeneID3030915.
3100552.
KEGGbld:BLi01762.
bli:BL02267.
PATRIC18949125. VBIBacLic203714_1766.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-1747-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_BACLD
AccessionPrimary (citable) accession number: Q65JV7
Secondary accession number(s): Q62VB1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 82 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