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

B2A2I8 (SYI_NATTJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 48. 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:Nther_1320
OrganismNatranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF) [Complete proteome] [HAMAP]
Taxonomic identifier457570 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaNatranaerobialesNatranaerobiaceaeNatranaerobius

Protein attributes

Sequence length926 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 – 926926Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189182

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif596 – 6005"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8971Zinc By similarity
Metal binding9001Zinc By similarity
Metal binding9141Zinc By similarity
Metal binding9171Zinc By similarity
Binding site5551Aminoacyl-adenylate By similarity
Binding site5991ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2A2I8 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 5D98C9332F25718F

FASTA926106,964
        10         20         30         40         50         60 
MNYKDTLNLP KTDFPMKAKL PSREPEFLQE WESNNLYQRV QQKRSGKPKY ILHDGPPYAN 

        70         80         90        100        110        120 
GNIHMGHALN KVLKDIVVKF KTMQGYDSPY VPGWDTHGLP IEHQITKTEK VDRKSMSDVE 

       130        140        150        160        170        180 
FRKKCHDYAM KYVEIQKEEF KRLGVRGDWD NPYLTLSPEF EAEQVKLFGE MAQKGYIYKG 

       190        200        210        220        230        240 
LKPVYWCTDC ETALAEAEVE YHDKRSPSIY VGFHVKDSKG EFNEEGVEFI IWTTTPWTIP 

       250        260        270        280        290        300 
ANMAIALHPE FQYSLIKSGE KHYIVATDLL ETVAEEAKLG EYQIIREYTG RELEGIVCQH 

       310        320        330        340        350        360 
PLFDSRESLV ILGDHVTLEQ GTGCVHTAPG HGHEDYEVAQ KYDLEVLSPL NDSGVFTEEA 

       370        380        390        400        410        420 
GQFQGLYYDK ANKEITQALD KRGALLSLSF ITHQYPCCWR CKESVIFRAT EQWFASVDGF 

       430        440        450        460        470        480 
RQDALKAIED VDWIPAWGEE RIKAMVMNRG DWCISRQRVW GVPLPIFYCQ ECGHELITEE 

       490        500        510        520        530        540 
SISAVAELFR QEGSDAWFEK EAPEILPQGI QCSCGAKKFS KETDIMDVWF DSGSTHRGVC 

       550        560        570        580        590        600 
AQRQELAWPV DLYLEGSDQY RGWFQSSLLT AVATKGESPY RECLTNGWVV DGEGKKMSKS 

       610        620        630        640        650        660 
QGNVIAPQDI TNQYGADILR LWVASSEFKQ DVRVSQKILK QTAEAYRKIR NTARFILGNL 

       670        680        690        700        710        720 
YDFTPEKDYV SFDQLEEIDS YILCRLQKVI DQATRAYDEF EFHEFYHLIH NFCVVELSQF 

       730        740        750        760        770        780 
YLDVIKDRIY TMPTESRERR AAQTTMYYLL DSLVKMLAPV LTFTSEEIWQ YLPGDREESI 

       790        800        810        820        830        840 
QLTDWPEVNE ELVDNELEQK WANFLEFRKE VAKALENARK DKKIGSSLES KILIYADEDL 

       850        860        870        880        890        900 
FKKLQSFEDN LEELFIVSQV ELKKAEQLTE TVKNQALSSE DVEQASIIIE AAQGEKCPRC 

       910        920 
WNYHPEVTKA EELCPRCSHV LETSNK 

« Hide

References

[1]"Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-LF."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001034 Genomic DNA. Translation: ACB84903.1.
RefSeqYP_001917491.1. NC_010718.1.

3D structure databases

ProteinModelPortalB2A2I8.
SMRB2A2I8. Positions 1-923.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING457570.Nther_1320.

Proteomic databases

PRIDEB2A2I8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB84903; ACB84903; Nther_1320.
GeneID6315558.
KEGGnth:Nther_1320.
PATRIC22671306. VBINatThe92436_1355.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycNTHE457570:GHRL-1356-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_NATTJ
AccessionPrimary (citable) accession number: B2A2I8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 20, 2008
Last modified: April 16, 2014
This is version 48 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