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Q6KHN7 (SYI_MYCMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:MMOB4070
OrganismMycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) [Complete proteome] [HAMAP]
Taxonomic identifier267748 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length885 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 – 885885Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098421

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif591 – 5955"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8611Zinc By similarity
Metal binding8641Zinc By similarity
Metal binding8771Zinc By similarity
Metal binding8801Zinc By similarity
Binding site5501Aminoacyl-adenylate By similarity
Binding site5941ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6KHN7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A0C5A0DAB008E2AF

FASTA885103,616
        10         20         30         40         50         60 
MKNKYKETLN IPQDVLPMRA NLIEKELKFK TFWDQNKIYQ KALEKNKTNK PFILHDGPPY 

        70         80         90        100        110        120 
ANGDLHIGHA LNKILKDIVV RYKSLSGFYA PFVPGWDTHG LPIENKILKE LKIDDHKNIS 

       130        140        150        160        170        180 
TLELRKQARE YALSQIKNQK KQFLTMQLFS DFKDYYQTLD PKFEAEQLKV FKKMALDGLI 

       190        200        210        220        230        240 
YKSLQPVFWS PSSQSALAEA EVEYHEHKSH SIYTAFKIVK GNKFVEKNDF LVIWTTTPWT 

       250        260        270        280        290        300 
LIANSGVSVK EEFSYSKINY ENKNYIFATD LVQKVTEIFG WKNFKIISSF QGKDLVGIEY 

       310        320        330        340        350        360 
QRPIKQEKTA PIVLGHHVTL ESGSGLVHMA PLFGLDDFII GRVEKLEEIM HINDDGSINE 

       370        380        390        400        410        420 
FGNQFANKFY WDANPEINEF LKQNNLLLHH SFLYHSYPHD WRTNKPVIYR GSNQWFVSID 

       430        440        450        460        470        480 
PIKEKITKSI EHVESYPTWG ISRLKTMIDN RTSWTISRQR AWGVPIPIFY NEKNEPVFEE 

       490        500        510        520        530        540 
ELFDHIIDLV SKYGTDIWFE KSTDELLPEK YKNKNWTKEK DIMDVWFDSG TTSMGVKIEG 

       550        560        570        580        590        600 
APVPWDVYLE GSDQYRGWFN SSLINSVVYY NQAPFKKLVS HGFVLDEKGN KMSKSKGNVV 

       610        620        630        640        650        660 
LPQEIISKFG ADILRLWVAN SEYTSDVTIG ENIINQNVEI YRKFRNTFRF LIANLVDFDY 

       670        680        690        700        710        720 
KKDLKELTGI HLLIKEQLET LKFNTKIAYE NFQFTNVIKL TNNFVYNLSS FYLDFSKDIL 

       730        740        750        760        770        780 
YANKIEDLQR KMIQTNFYNI TKTLLLILAP ILPTTIEEVY QIFDQANKKE SVHLENFFGI 

       790        800        810        820        830        840 
SSIETIQEEK WNSFFELKNK VYALIEIAIK DKLIKSANQA LVYIKETDEF LKTLDLKNLL 

       850        860        870        880 
MVGKVIFSKE NKIENYEGHL CERCRIYFDF IDKDNLCVRC SKVIL 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017308 Genomic DNA. Translation: AAT27893.1.
RefSeqYP_016104.1. NC_006908.1.

3D structure databases

ProteinModelPortalQ6KHN7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267748.MMOB4070.

Proteomic databases

PRIDEQ6KHN7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT27893; AAT27893; MMOB4070.
GeneID2807754.
KEGGmmo:MMOB4070.
PATRIC20016173. VBIMycMob32482_0429.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKKRIELM.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycMMOB267748:GH6Y-430-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.
[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_MYCMO
AccessionPrimary (citable) accession number: Q6KHN7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 74 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