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

B2V9T1 (SYI_SULSY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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:SYO3AOP1_1087
OrganismSulfurihydrogenibium sp. (strain YO3AOP1) [Complete proteome] [HAMAP]
Taxonomic identifier436114 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesHydrogenothermaceaeSulfurihydrogenibium

Protein attributes

Sequence length939 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 – 939939Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000216246

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif604 – 6085"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9031Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9211Zinc By similarity
Metal binding9241Zinc By similarity
Binding site5631Aminoacyl-adenylate By similarity
Binding site6071ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2V9T1 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 321C86AB3AFA3007

FASTA939109,922
        10         20         30         40         50         60 
MEFKDTLNLP QTEFPMKGNL PNKEPEILSF WEKINLYQKL REDRKGKDKY ILHDGPPYAN 

        70         80         90        100        110        120 
GHIHIGHALN KILKDILVKY QSMKGKDAPF VPGWDCHGLP IEQQVEKELK EKKIKKEDLS 

       130        140        150        160        170        180 
KSEFRKLCRE YALKFVNIQK EEFKRLGIIG NWEKPYLTMR PSYQAQEVLE LGRVFNKGVA 

       190        200        210        220        230        240 
YRGKKPVYWC IYDKTAEAEA EIEYYDKKDP SIYVKFKMKD SDDTYLVIWT TTPWTLPANL 

       250        260        270        280        290        300 
GVMVHPEFDY VYFKTGKGTL IVAKELLENF KEKTGLNGEV IKQVKGKDLE FKEYYHPFID 

       310        320        330        340        350        360 
RVSKVYLSEF VELGTGTGLV HMAPGHGQED YIIGQRYGVD AFAPVDDEGR FIQEAPDWLK 

       370        380        390        400        410        420 
GIRVFDANDL IIEKLQEVDA LIYKEVISHS YPHCWRCKNP VIFRATPQWF ISMEAKVNEN 

       430        440        450        460        470        480 
QTLREAALKE IERVKWIPYY GQNRIKSMVE NRPDWCISRQ RSWGVPITVF YCENCGEIVK 

       490        500        510        520        530        540 
DMEVFEHVAN LIKNDEFGAD IWFEKLVKEL LPEGYKCKKC GGQEFKKEED ILDVWFDSGV 

       550        560        570        580        590        600 
SHAAVLKYGE WEELRWPADM YLEGSDQHRG WFQSSLLESV ASYNRAPYDT VLTHGFTLDE 

       610        620        630        640        650        660 
KGRKMSKSAG NVVAPEKVIK EYGADILRLW VVTEDYTEDI KIGFNLIKRI AEDYRKIRNT 

       670        680        690        700        710        720 
FRYFLGNLYD FNPNQDYVPY ENLLEIDRWM LSKLQNIIQI ADKSYEEGKF HKIYHTIKNF 

       730        740        750        760        770        780 
VIVDLSAIYL DILKDRLYVY APKSLERKSA QTVLWELLLS LNKILAPIIS FTAEEVWQYV 

       790        800        810        820        830        840 
RKIDSNIKES IHLEIMPVVN EKFIDKNLEE TYEKLLEVRD DILKAIEEAR KQDLVRHPYE 

       850        860        870        880        890        900 
ARVILKLPKE YKEIVEKRLD WIKFFFTVSQ VELSDNPEGD VVINGESVKD SVIAVSKAKG 

       910        920        930 
EKCPRCWIYD ESVGRNGQPV CDRCKIQLEI MNIKLEELA 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YO3AOP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001080 Genomic DNA. Translation: ACD66704.1.
RefSeqYP_001931258.1. NC_010730.1.

3D structure databases

ProteinModelPortalB2V9T1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436114.SYO3AOP1_1087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD66704; ACD66704; SYO3AOP1_1087.
GeneID6332096.
KEGGsul:SYO3AOP1_1087.
PATRIC23767009. VBISulSp94719_1135.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSP436114:GI6I-1131-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_SULSY
AccessionPrimary (citable) accession number: B2V9T1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 1, 2008
Last modified: April 16, 2014
This is version 50 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