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P46213 (SYI_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. 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:TM_1361
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length919 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
Reference 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 – 919919Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098494

Regions

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

Sites

Metal binding8871Zinc By similarity
Metal binding8901Zinc By similarity
Metal binding9071Zinc By similarity
Metal binding9101Zinc By similarity
Binding site5531Aminoacyl-adenylate By similarity
Binding site5971ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P46213 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 40E4D0876010C385

FASTA919107,156
        10         20         30         40         50         60 
MEYKNTLNLP KTSFPMKANL VNKEKVFLEE WEKMDLYNYV LEQRKGKPLF VLHDGPPYAN 

        70         80         90        100        110        120 
GHIHIGTALN KILKDIVVKY KTMRGYRAPY VPGWDTHGLP IEHRVSQELG EKIKEMSPAE 

       130        140        150        160        170        180 
IRKKCEEFAL RFVDIQREEF KRLGVRGDWE NPYITLKPDY EVKILDVFKT LVEQGNVYRS 

       190        200        210        220        230        240 
LKPIYWCPRC RTALAEAEIE YHDHKSPSIY VKFRSKEDPN FFIVIWTTTP WTLPANVGIA 

       250        260        270        280        290        300 
LHPDYEYSVV KVGEEKWVIA TDLLDAFSKE TGIDCSNVVE KIKGKDLEGK EFVHPIFDDR 

       310        320        330        340        350        360 
TSRVILADYV SLETGTGCVH IAPGHGEEDY IYGHVQYGLP IVSPVDEEGR FTEEAGKYKG 

       370        380        390        400        410        420 
MFIEDANEVI IEDLKRKGIL VHASSITHSY PHCWRCKGPV IFRATEQWFI SVDHNNLRQK 

       430        440        450        460        470        480 
VLEEIDKVKW IPEWGRNRIR SMVEERPDWC ISRQRVWGTP IPAVKCKECG EVVLDPKVIE 

       490        500        510        520        530        540 
HFMKIVEKEG TNAWFEKEVE ELIPEDFVCP KCGKRSFEKM LDTLDVWIDS GASFEYITTK 

       550        560        570        580        590        600 
REDHPFPLDM YLEGSDQHRG WFHSSIFLAV AKRGSAPYKE VLTHGFIKDE QGRKMSKSLG 

       610        620        630        640        650        660 
NVVDPMEVVE KYGAEILRLW LASSDYFNDI KISMRIVEQQ TEVYRKIRNT FRFLLGNLED 

       670        680        690        700        710        720 
FDPELDRVPH EKLLTIDRWA LGRLQEIIKR ATEYYDSYEF SKVYNLVVKY CTTELSSLYL 

       730        740        750        760        770        780 
DVVKDRLYVE AKDSIYRRSA QTVMHEILIS LMKILAPIMT FTMEEVYSHL HEKDRKYKTV 

       790        800        810        820        830        840 
QAEYWPEYRE EFIDRKLMED FEKLLSIRED VLKALEEKRQ QDVIGHSLDA EVVLVPKNDT 

       850        860        870        880        890        900 
IKALLEKYRD ILEELFIVSK VSLSDASGEL KGELVEVTVK HAEGEKCQRC WKYTTEISAS 

       910 
EDFPGVCPRC LAVLKGERK 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications."
Brown J.R., Doolittle W.F.
Proc. Natl. Acad. Sci. U.S.A. 92:2441-2445(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-599.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36431.1.
L37104 Genomic DNA. Translation: AAC41448.1.
PIRB72263.
RefSeqNP_229162.1. NC_000853.1.
YP_007977717.1. NC_021214.1.
YP_008991548.1. NC_023151.1.

3D structure databases

ProteinModelPortalP46213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1361.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36431; AAD36431; TM_1361.
GeneID898119.
KEGGtma:TM1361.
tmi:THEMA_07535.
tmm:Tmari_1368.
PATRIC23937660. VBITheMar51294_1373.

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

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_THEMA
AccessionPrimary (citable) accession number: P46213
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 108 of the entry and version 2 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