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Q67Q27 (SYI_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:STH1231
OrganismSymbiobacterium thermophilum (strain T / IAM 14863) [Complete proteome] [HAMAP]
Taxonomic identifier292459 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium

Protein attributes

Sequence length938 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 – 938938Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098488

Regions

Motif61 – 7111"HIGH" region HAMAP-Rule MF_02002
Motif601 – 6055"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9041Zinc By similarity
Metal binding9071Zinc By similarity
Metal binding9231Zinc By similarity
Metal binding9261Zinc By similarity
Binding site5591Aminoacyl-adenylate By similarity
Binding site6041ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q67Q27 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: A21A5E420CA8C381

FASTA938106,189
        10         20         30         40         50         60 
MAEKTDYKAT LNMPRTDFPM RANLPTREPE QLKKWEEMDL YNLVQRATAG RPKFVLHDGP 

        70         80         90        100        110        120 
PYANGDIHLG TALNKILKDI IVKHATMAGY DAPYVPGWDM HGLPIELRAL KDMNIDRRKI 

       130        140        150        160        170        180 
DPLELRAKCY EYAHHWLNVQ REQFKRLGVR GDWENPYRTV APEFEAKEVE VFGAMAAKGY 

       190        200        210        220        230        240 
IYRGLKPVYW CPYCETALAE AEIEYNEKTS YSIYVRFPVV DPRGKLPEGS YLVIWTTTPW 

       250        260        270        280        290        300 
TIPANLAVAV HPEVEYGVYA TEKGNLVVAT ALAEKFFQAV NLPAAEPVAT LKGADLEGIT 

       310        320        330        340        350        360 
YRHLLYDRVS PVILGDHVTT EDGTGLVHTA PGHGHEDFEV GQKYGLPVLN PVNDQGVFTA 

       370        380        390        400        410        420 
EAGPFAGMFI EKANPEIIKA LDEAGMLLGQ GKIRHQYAHC WRCKNPVIYR ATVQWFVKVE 

       430        440        450        460        470        480 
GFMDIAKEAM NHVRWIPDWG YNRMYAMIDG LADWCISRQR AWGLPIPILT CSACDEPSFE 

       490        500        510        520        530        540 
PKMFEKIAEI FRAEGSDAWW RRPAEDFMPE GGLTCKKCGG RTFHKEKDIL DVWFDSGSSH 

       550        560        570        580        590        600 
VGVLETRPEL TWPADLYLEG SDQHRGWFKS SLLTAVVARD GKPPYKAVLT HGFTVDEQGR 

       610        620        630        640        650        660 
KMSKSLGNVV DPADVIKRYG ADILRLWVAS TDYRHDMALS ENILKQVADA YRKIRNTLRY 

       670        680        690        700        710        720 
LLGNLYDFNP DTDMVERDDL LEIDRWQMHR LQEVIRKVTE AYREYEYHIV YHTLNNYCAV 

       730        740        750        760        770        780 
DLSAVYLDIL KDRLYTSAPA SRERRSAQTV LYHVADALIR MLTPILTFTA EEAYSHLPKP 

       790        800        810        820        830        840 
AGSPPTSQLL MMPQPDPAYL DENLAAEWDR LMELRDAVQV VLERARVDKL IGSSQEAAVN 

       850        860        870        880        890        900 
LYASGGEGSW AELLDRHLPD LPSIFIVSDV KLFVGGQSAP SGTYFGEGPG DLSVEVVRAE 

       910        920        930 
GEKCERCWNY RKVGAIEQHP TLCERCAGVV LSLNLDNA 

« Hide

References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006840 Genomic DNA. Translation: BAD40216.1.
RefSeqYP_075060.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ67Q27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292459.STH1231.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD40216; BAD40216; STH1231.
GeneID2979836.
KEGGsth:STH1231.
PATRIC23780624. VBISymThe116959_1233.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycSTHE292459:GJMM-1300-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_SYMTH
AccessionPrimary (citable) accession number: Q67Q27
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 76 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