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

B4U8K1 (SYI_HYDS0) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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:HY04AAS1_0775
OrganismHydrogenobaculum sp. (strain Y04AAS1) [Complete proteome] [HAMAP]
Taxonomic identifier380749 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeHydrogenobaculum

Protein attributes

Sequence length937 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 – 937937Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000216237

Regions

Motif55 – 6511"HIGH" region HAMAP-Rule MF_02002
Motif624 – 6285"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9151Zinc By similarity
Metal binding9181Zinc By similarity
Metal binding9301Zinc By similarity
Metal binding9331Zinc By similarity
Binding site5831Aminoacyl-adenylate By similarity
Binding site6271ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B4U8K1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 833B423E2424492E

FASTA937109,507
        10         20         30         40         50         60 
MDYKDTINLP KTDFPMKANL SEKELEILKK WEGLYEKLRA QRKGKQLFVL HDGPPYANGN 

        70         80         90        100        110        120 
IHIGHALNKI LKDIICKVAL IEGFDVDYKP GWDCHGLPIE QQVEKELKAK KINKESMPKD 

       130        140        150        160        170        180 
EFRRLCREYA SKFVSIQKEE FLRLGVLGDW ENPYLTMDPK YEAQEVREIG RCLQNGVLYK 

       190        200        210        220        230        240 
GNKPVYWCIY DKTAEAEAEV EYKEKKDISI YVRFELLKQS ENVLRQKLDL PDKPISIVIW 

       250        260        270        280        290        300 
TTTPWTLPAN LGVMSSEDIE YVVVEEDNYL LLLEKQSQYV KNKEFIASLK GKELTGLEYQ 

       310        320        330        340        350        360 
HPFIERTGKI YPSEFVEAGT GTGFVHMAPG HGMEDYIVGL RYGLEPFSPV DESGRFTEEA 

       370        380        390        400        410        420 
PEFIRGLNVF EANTVIIEHL KQTGFLLKEE EILHSYPHCW RCKNPVIYRA TPQWFIGVDR 

       430        440        450        460        470        480 
AITSHFASCE DEKIDTSDVK KLQNKSIREK AIEETYNVKW VPKTGQNRML SMLQNRPDWC 

       490        500        510        520        530        540 
ISRQRFWGVP ITIFYCKRCG EPLLESHIFE HVAKIFESSP YGADEWFKKD EKELLPPDTV 

       550        560        570        580        590        600 
CKKCGSKDFV KETDILDVWF DSGSSHASVL RPRGIEKADV YLEGSDQHRG WFQASLLESI 

       610        620        630        640        650        660 
ASYGEAPFKS VVTHGFTVDE KGHKMSKSQG NVISPLEIIK EYGADILRLW VISEDYTEDI 

       670        680        690        700        710        720 
KLGKSILKRL AEDYKKIRNT LRYCLGNLYD FKYEFSIAPD KLHHFDRYMY AYASKVFEEL 

       730        740        750        760        770        780 
FSFYKNYQYH RFYHRLMEFV SIDLSALYFD VLKDRLYMYK SGSFERLSAQ TVLYFLLKNL 

       790        800        810        820        830        840 
TILLSPVLSF TAEETYSYMK SIENHLPESI FMNEYKASDF TDEELLKDYQ KLLLLRKDVL 

       850        860        870        880        890        900 
KAIEIERKND IIKHPYEARV VIKPNEEFYK LLEKYKDYLH SFFTVSQVEI AENDGEEGEY 

       910        920        930 
TKLRIKVEKA KGEKCPRCWL YVETMINGVC PRCSQNI 

« 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: Y04AAS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001130 Genomic DNA. Translation: ACG57462.1.
RefSeqYP_002121440.1. NC_011126.1.

3D structure databases

ProteinModelPortalB4U8K1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING380749.HY04AAS1_0775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACG57462; ACG57462; HY04AAS1_0775.
GeneID6743580.
KEGGhya:HY04AAS1_0775.
PATRIC22136222. VBIHydSp64203_0780.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycHSP380749:GH30-802-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_HYDS0
AccessionPrimary (citable) accession number: B4U8K1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 46 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