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

Q8EUN9 (SYI_MYCPE) 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:MYPE8820
OrganismMycoplasma penetrans (strain HF-2) [Complete proteome] [HAMAP]
Taxonomic identifier272633 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length900 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 – 900900Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098423

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif591 – 5955"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8711Zinc By similarity
Metal binding8741Zinc By similarity
Metal binding8881Zinc By similarity
Metal binding8911Zinc By similarity
Binding site5501Aminoacyl-adenylate By similarity
Binding site5941ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8EUN9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E7710FE7B619458C

FASTA900104,162
        10         20         30         40         50         60 
MSDYKKTLSM PNTNFEMKAN LSVKETKIQE NWVLEKIEKK ILAKNKSNTP FIIADGPPYA 

        70         80         90        100        110        120 
NGDLHTGHAL NKILKDIILR FKASVGFYTK YIPGWDTHGL PIEQEMAKRG LNKNANQTIT 

       130        140        150        160        170        180 
EKRKNCKNFA IENVYKQRDQ FRRLGILSEM DEIYVTCDLD YVIRQIKIFN KMLSKGLIYQ 

       190        200        210        220        230        240 
DLKPVYWSWS SQTALADAEI IYQDVESDSI YVSLEILDKN EFVSKGDKVI IWTTTPWTLP 

       250        260        270        280        290        300 
SNLAIAANPK VTYCRVQVEN SVYVISKNLV EKLAETLEWT NYEILSEFSG KKLENLPYKS 

       310        320        330        340        350        360 
PISDKKCKII VDGYVSDSDG TGLVHNAPGF GHEDYLACKK YNIKPYCPID NLGKFTGEVN 

       370        380        390        400        410        420 
DKELAGLFYK DANPIIIERL AKKKLLLKAS KFTHSAAHDW RTKKPVIYRA TKQWFVNIDK 

       430        440        450        460        470        480 
ISKEIVAALN KVKSIDNTII KKIKEMVLNR QEWCISRQRI WGVPICIIYD KDYNPILDPK 

       490        500        510        520        530        540 
LLNNIVDILN DEGINAWYNE DAKYFLTDSY NTSKKYIKET DIMDVWFDSG TSYSVLQADK 

       550        560        570        580        590        600 
LGYPADLYFE GKDQFRGWFN SSLITSVAAF KKSPYKELLT HGFVLDENGN KMSKSLGNII 

       610        620        630        640        650        660 
DPLQVCKEYG ADVLRLWVAS VDFSKDVSIS KDIIAQNAEL YRRIRNTLFR FILGNLNGFN 

       670        680        690        700        710        720 
LKKLRGAKYS EADLYVLSCL SNDIKTIKAC YDKYDFKQIV KIVSKNVADL SSWYFDYIKD 

       730        740        750        760        770        780 
PLYCEKEDNE QRIAIQATLY QLLDSYLRIL APIIPHTCEE AYEFFDKKDK QKSVHLEGFT 

       790        800        810        820        830        840 
NFKIDSKYKV DFKKWEEFFD LKDKVYSEIE KTRNEKVINS KGQAHITIHS KSLPFDEQTL 

       850        860        870        880        890        900 
ERYLGVAKVE FKVKEKDGTT IKVKNSKYAR CERCWNYYPT NLIANELCER CKKVIGNKKI 

« Hide

References

[1]"The complete genomic sequence of Mycoplasma penetrans, an intracellular bacterial pathogen in humans."
Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K., Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.
Nucleic Acids Res. 30:5293-5300(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HF-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000026 Genomic DNA. Translation: BAC44673.1.
RefSeqNP_758269.1. NC_004432.1.

3D structure databases

ProteinModelPortalQ8EUN9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272633.MYPE8820.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC44673; BAC44673; BAC44673.
GeneID1041417.
KEGGmpe:MYPE8820.
PATRIC20020952. VBIMycPen56664_0908.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycMPEN272633:GJBP-912-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.
InterProIPR002300. 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.
ProtoNetSearch...

Entry information

Entry nameSYI_MYCPE
AccessionPrimary (citable) accession number: Q8EUN9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
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