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

C0QP76 (SYI_PERMH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:PERMA_0684
OrganismPersephonella marina (strain DSM 14350 / EX-H1) [Complete proteome] [HAMAP]
Taxonomic identifier123214 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesHydrogenothermaceaePersephonella

Protein attributes

Sequence length947 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 – 947947Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000216243

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif609 – 6135"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Metal binding9261Zinc By similarity
Metal binding9291Zinc By similarity
Binding site5681Aminoacyl-adenylate By similarity
Binding site6121ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C0QP76 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: DE47D4F7B6D5933A

FASTA947110,771
        10         20         30         40         50         60 
MEWKDTLNLP KTAFPMKGNL PNKEPEIIKK WEEIDLYKRL REERKGKEKY ILHDGPPYAN 

        70         80         90        100        110        120 
GNIHLGHALN KILKDILVKY ESMKGKDAPF VPGWDCHGLP IEQQVEKLLK KEKKRKEDLS 

       130        140        150        160        170        180 
KSEFRKLCRE YALKYVNIQR EEFKRLGIIG NWEKPYLTMR PSYQAQEIRE LGKIFRKGIA 

       190        200        210        220        230        240 
YRGKKPVYWC IYDKTAEAEA EVEYKEKKDP SIYVAFELVE SPFDIKEKVY AVIWTTTPWT 

       250        260        270        280        290        300 
LPANLGIMVN PDFDYLFLRS EDKVYIVAKD LLESFSEKTG IEGEVIKEVK GRELEFLEYR 

       310        320        330        340        350        360 
HPFIDRVSKI YLSEFVELGT GTGLVHMAPG HGQEDYIIGQ RYGVEAFAPV DDEGRFTDEA 

       370        380        390        400        410        420 
PEFIQGLRVF EANERIVEKL RENGVLLHHE TVKHSYPHCW RCKNPVIFRA TPQWFISMDG 

       430        440        450        460        470        480 
ITEKGETLRG EALKEIERVK WIPHWGENRI KSMIENRPDW CISRQRSWGV PIAVFYCKRC 

       490        500        510        520        530        540 
GNIIDDEKVF EHIADLVEKD EFGADIWFER EAEELLPEGY RCPKCDGEEF KKEEDILDVW 

       550        560        570        580        590        600 
FDSGVSHASV LKSGFWDELK WPADMYLEGS DQHRGWFQSS LLEGVASYGR APYDAVLTHG 

       610        620        630        640        650        660 
FILDEKGNKM SKSLGNVIPP EKIIKMYGAD ILRLWVVSED YTEDIKIGMN LLKSIADDYR 

       670        680        690        700        710        720 
KIRNTFRYFL GNLYDFDANK DRVPYENLLE IDRWMLSKLQ RLIDRSHSAY SNYRFHKIYH 

       730        740        750        760        770        780 
EIKRFVIVDL SAVYLDILKD RLYVYAPDSL ERRSAQTVLY ELLDSLTKLL APILSFTTEE 

       790        800        810        820        830        840 
IWGYVREINP SVKESIHLEE MPVVNQDYID PELEETYEKL MKVRDDILKA LEEARRSDII 

       850        860        870        880        890        900 
RHPYEAKVVL SLPDEYRSVV EKRIDWIKFF FTVSQVELSD QAEGDVIIGG EKVEGGKIAV 

       910        920        930        940 
KKASGEKCPR CWIYDESVGK DGQPVCDRCM EQLERMEIKI SDIEEAK 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14350 / EX-H1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001230 Genomic DNA. Translation: ACO03207.1.
RefSeqYP_002730472.1. NC_012440.1.

3D structure databases

ProteinModelPortalC0QP76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING123214.PERMA_0684.

Proteomic databases

PRIDEC0QP76.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO03207; ACO03207; PERMA_0684.
GeneID7674544.
KEGGpmx:PERMA_0684.
PATRIC22914835. VBIPerMar119911_0726.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycPMAR123214:GIZP-683-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_PERMH
AccessionPrimary (citable) accession number: C0QP76
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 5, 2009
Last modified: May 14, 2014
This is version 40 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