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P26499 (SYI_METTM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 94. 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:MTBMA_c17620
OrganismMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) [Complete proteome] [HAMAP]
Taxonomic identifier79929 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length1045 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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
Direct protein sequencing
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 HAMAP-Rule MF_02003
Chain2 – 10451044Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098579

Regions

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

Sites

Binding site5941ATP By similarity

Experimental info

Mutagenesis5891G → D: Resistance to mupirocin (pseudomonic acid A).

Sequences

Sequence LengthMass (Da)Tools
P26499 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5A935B0FE300077E

FASTA1,045121,362
        10         20         30         40         50         60 
MPIQEAEKSY KPHVIEEKVQ SFWEERDIYE RVKELREEGP RYSFLDGPPY CSGRIHLGTA 

        70         80         90        100        110        120 
WNKIMKDSYL RFKSMRGFNV RRQPGWDTHG LPIEHKVEGI LGVRSKKDIE DKIGIEEFVR 

       130        140        150        160        170        180 
KCREFAMENK AVMTSQFQRL GVWMDWDDPY VTFDPAYMES CWWTLKRAHE KDLLLRDLRV 

       190        200        210        220        230        240 
ITWCPRCETA LALAEIDYHE KEDPSIYVKF PVSGDTYILV WTTTPWTLPA NMAVAVHPDF 

       250        260        270        280        290        300 
DYAHTRLDGE TYIMAEALVE KVLGEEAEII KTVRGSELEG LTYRHPLDEE VPCHRDMEHR 

       310        320        330        340        350        360 
VILGDHVTLT EGTGCVHTAP GHGPEDFEIG KEYGLPVFCP VDEAGVFTED AGKYRGLFVK 

       370        380        390        400        410        420 
DADSDIIDDL RSKNLLLRAE TISHRYGFCW RCKTPIIYLA TEQWFLKITE IKDKMLSELD 

       430        440        450        460        470        480 
RVQWIPSWAG ESRFRNWIEN ARDWTISRQR YWGIPIPIWV CEDCDSIHVV GSIGELRELA 

       490        500        510        520        530        540 
VEGQLEGDFI HRPHVDRIIL ECGRCGGRMK RTPDVLDVWI DSGVAGWAAL HYPREKELFS 

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

       610        620        630        640        650        660 
EPEDVIEKYG ADVLRFYLLW ANKPWEDLKF VWDELKNVNK MFNILWNVYV FATTYMSLDR 

       670        680        690        700        710        720 
FQPGDHELED LHFRDEDRWI ISRVNSVALK VTEALDNLHF HRATREIHDF IVEDLSRWYI 

       730        740        750        760        770        780 
RLIRSRTWIE RDDPDKLAAY HSLYTALKTL IVTLSPIAPH VCEDIYQNLV RGAEPDSPES 

       790        800        810        820        830        840 
IHMLDWMVSE DAVDGKLEAE MDIVREIIEA CARARDTARY KLRWPVREIV VVSEDDKVLE 

       850        860        870        880        890        900 
AAESLKGVIA EQANAKSIRT STEFPDMRII AKPNPATLGP KLRQDMPPVM RKLEEADGAE 

       910        920        930        940        950        960 
VKAALESEGS FRVDLDGRII VLEPDDIIFE TELPENIVNA QFEGGSVFVD TELTPEIMSE 

       970        980        990       1000       1010       1020 
AMARELVRRI QDMRKDLDLD VEARIEVSVK CSPEFRELTE PQREFVENEV RASHLSFDYT 

      1030       1040 
ELEYTKEWKI SDENLIISIK PSDKV 

« Hide

References

« Hide 'large scale' references
[1]"Isoleucyl-tRNA synthetase of Methanobacterium thermoautotrophicum Marburg. Cloning of the gene, nucleotide sequence, and localization of a base change conferring resistance to pseudomonic acid."
Jenal U., Rechsteiner T., Tan P.-Y., Buehlmann E., Meile L., Leisinger T.
J. Biol. Chem. 266:10570-10577(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[2]"Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59245 Genomic DNA. Translation: AAA72950.1.
CP001710 Genomic DNA. Translation: ADL59330.1.
RefSeqYP_003850643.1. NC_014408.1.

3D structure databases

ProteinModelPortalP26499.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL59330; ADL59330; MTBMA_c17620.
GeneID9705473.
KEGGmmg:MTBMA_c17620.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000246403.
KOK01870.
OMAKPVHWCL.

Enzyme and pathway databases

BioCycMMAR79929:GH5J-1768-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_METTM
AccessionPrimary (citable) accession number: P26499
Secondary accession number(s): D9PYN2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 94 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