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O27428 (SYI_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. 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:MTH_1375
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length1044 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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

Initiator methionine11Removed By similarity
Chain2 – 10441043Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098578

Regions

Motif49 – 5911"HIGH" region HAMAP-Rule MF_02003
Motif591 – 5955"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5941ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O27428 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BDE882817791051B

FASTA1,044120,980
        10         20         30         40         50         60 
MPIQEAEKSY RPHRIEEKVQ SFWEERDIYE RVKELREDRP RYSFLDGPPY CSGRIHLGTA 

        70         80         90        100        110        120 
WNKIMKDTYL RFKSMKGFNV RRQPGWDTHG LPIEHKVEGL LGVRSKKDIE DKIGIEEFVN 

       130        140        150        160        170        180 
KCREFAVENK AVMTGQFQRL GVWMDWDDPY VTFDPAYMES CWWTLKRAHE KDLLVRDLRV 

       190        200        210        220        230        240 
ITWCPRCETA LALAEIDYHD KEDPSIYVKF PVSGDTHILV WTTTPWTLPA NMAVAVHPDF 

       250        260        270        280        290        300 
EYAYARLDGE TYIMAEALVE KVLGEEAEIL KRVKGTELEG LTYRHPLDDE VPLHREIEHR 

       310        320        330        340        350        360 
VILGDHVTLT EGTGCVHTAP GHGPEDFEIG KKYGLEVICP VDEAGIFTEE AGKYSGRFVK 

       370        380        390        400        410        420 
DADEDIIADL RSKGLLLKAG TISHRYGFCW RCKTPIIYLA TEQWFLKITE IKDKMLRELD 

       430        440        450        460        470        480 
RVQWVPSWAG ESRFRNWIEN ARDWTISRQR YWGIPIPIWI CEECDSIHVV GSIDELRELA 

       490        500        510        520        530        540 
VEGELEGDFI HRPHVDRIVL ECGECGGRMK RTPDVLDVWI DSGVAGWAAL HYPSETELFR 

       550        560        570        580        590        600 
EWFPYDFITE GHDQTRGWFY SQLGCGVIAL DEVPYRRVLM HGFTLDEEGR KMSKSLGNVV 

       610        620        630        640        650        660 
EPEDVIEKYG ADVLRFYLLW ENKPWEDLKF VWDELRNVNK MFNILWNVYV FATTYMSLDR 

       670        680        690        700        710        720 
FQPGDHSAED LSFRDEDRWI LSRINSVALK VTEAIENLHF HRATREIHDF IVEDLSRWYI 

       730        740        750        760        770        780 
RLIRSRTWIE RDDPDKLAAY HTLYTVLKTL IVTLSPMAPH VCEDIYQNLV RGAEPDSPES 

       790        800        810        820        830        840 
IHMLDWILDE GAVDSQLEAD MDIVREIIEA CARARDTARY KLRWPVREMV VVSEDEGVLK 

       850        860        870        880        890        900 
AAESLKNVIA EQANAKSIKT STEFPDMKII ARPNPATLGP RLRQDIPLVM RELEGADGSA 

       910        920        930        940        950        960 
VKAALDSDGE FTVETDGKKF KLTSEDIVFE TELPENIVSA QFDGGSVFID TELTPEIMSE 

       970        980        990       1000       1010       1020 
AMARELVRRI QDMRKDLDLD VEASIEVSVK CSEEFRELTE PQREFIENEV RASTLSFDYS 

      1030       1040 
ELEYTKEWKI SDENLIISIK PAKV 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB85852.1.
PIRH69049.
RefSeqNP_276491.1. NC_000916.1.

3D structure databases

ProteinModelPortalO27428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187420.MTH1375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB85852; AAB85852; MTH_1375.
GeneID1471092.
KEGGmth:MTH1375.

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKPVHWCL.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-1377-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR023586. Ile-tRNA-ligase_type2.
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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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_METTH
AccessionPrimary (citable) accession number: O27428
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 95 of the entry and version 3 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