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

B8CWL4 (SYI_HALOH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:Hore_09270
OrganismHalothermothrix orenii (strain H 168 / OCM 544 / DSM 9562) [Complete proteome] [HAMAP]
Taxonomic identifier373903 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaHalanaerobialesHalanaerobiaceaeHalothermothrix

Protein attributes

Sequence length929 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 – 929929Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189169

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif601 – 6055"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8981Zinc By similarity
Metal binding9011Zinc By similarity
Metal binding9181Zinc By similarity
Metal binding9211Zinc By similarity
Binding site5601Aminoacyl-adenylate By similarity
Binding site6041ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B8CWL4 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: CADD37AE9394EAFF

FASTA929106,890
        10         20         30         40         50         60 
MDYKETINLP RTEFPMRANL SKREPGIEKY WEENNVYEKA IKNREGNKQF ILHDGPPYAN 

        70         80         90        100        110        120 
GDIHIGHALN KILKDIVTRY KTLSGYYSPY VPGWDTHGLP IEHKVTKEMG DKAKDLSVSE 

       130        140        150        160        170        180 
LRDKCRDYAL KYVERQKEQF KRLGVWGEWD KPYLTLNPEY EVKQIEVFGE MAKRGLFYKG 

       190        200        210        220        230        240 
KKPVHWCPSC ETALAEAEVE YGEHRSPSIY VKFPLKDKVN VGGVELTPGD SYVVIWTTTP 

       250        260        270        280        290        300 
WTIPANMAIA LHPEFDYVVV KASGEKLVMA RELVDRVMEE AEVENYKVVG QAFKGTELEN 

       310        320        330        340        350        360 
KRCRHPFEDR DSILILGDHV TLEQGTGCVH TAPGHGHDDY LVGLKYDLDI YAPMDNRGVF 

       370        380        390        400        410        420 
TEEAERFAGM YYDDVNKEVT KILDEKGLLM NLSFISHQYP HCWRCKGALI FRATDQWFAS 

       430        440        450        460        470        480 
IEAIKEEALK AIHSVDWYPA WGEERMANMI SERTDWCISR QKKWGVPIPV FYCKDCGHSI 

       490        500        510        520        530        540 
INDETIEAVK KLFAREGSSG WYKYSAEEIL PEGFSCPECG GKSFKKEEDI MDVWFDSGSS 

       550        560        570        580        590        600 
HKAVLETRDH LSWPSQLYLE GTDQYRGWFN SSLLTAVATE GKPPYEAVVT NGFVVDDKGN 

       610        620        630        640        650        660 
KMSKSIGNVV SPQDVIKRYG ADILRLWVAS SNFKDDVRVS DRILKQNSEV YRRIRNTFRF 

       670        680        690        700        710        720 
ILGNINDFNP GQHYVDYNDR AEIDRWIMIK LQDLIKDVTR AYDEYEYHRV YHDVHNFCTI 

       730        740        750        760        770        780 
EMSSLYVDIV KDRLYTDGTN SLSRRSAQST LYDILLVLVK LVAPVLAHTA EEVWQHLDES 

       790        800        810        820        830        840 
SKDAESIFLT DWPEVVNEYY DDRLMSKWDK LLEVRKDVAK ALELSRENKE IGNSLDARVI 

       850        860        870        880        890        900 
LVPVDDKQRQ LLKDNIDILP DLFIVSQVEL QGETGEGFHK GSETGISVSV VKASGEKCAR 

       910        920 
CWKYSEAVGN DEEHPELCER CVEVVRTEV 

« Hide

References

[1]"Genome analysis of the anaerobic thermohalophilic bacterium Halothermothrix orenii."
Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H., Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.
PLoS ONE 4:E4192-E4192(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H 168 / OCM 544 / DSM 9562.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001098 Genomic DNA. Translation: ACL69683.1.
RefSeqYP_002508678.1. NC_011899.1.

3D structure databases

ProteinModelPortalB8CWL4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING373903.Hore_09270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL69683; ACL69683; Hore_09270.
GeneID7313420.
KEGGhor:Hore_09270.
PATRIC22101240. VBIHalOre56292_0986.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMALGRRSCQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycHORE373903:GHB1-972-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_HALOH
AccessionPrimary (citable) accession number: B8CWL4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 39 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