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C5D8P2 (SYI_GEOSW) 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:GWCH70_1039
OrganismGeobacillus sp. (strain WCH70) [Complete proteome] [HAMAP]
Taxonomic identifier471223 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length923 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 – 923923Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000216236

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif593 – 5975"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8901Zinc By similarity
Metal binding8931Zinc By similarity
Metal binding9101Zinc By similarity
Metal binding9131Zinc By similarity
Binding site5521Aminoacyl-adenylate By similarity
Binding site5961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C5D8P2 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 631E16D4758054CC

FASTA923104,948
        10         20         30         40         50         60 
MDYKETLLMP QTEFPMRGNL PKREPEIQKK WEEMDIYRKV QERTKGRPLF VLHDGPPYAN 

        70         80         90        100        110        120 
GDIHMGHALN KILKDIIVRY KSMSGYCAPY VPGWDTHGLP IETALTKKGV DRKSMSVAEF 

       130        140        150        160        170        180 
RKLCEQYAYE QINNQREQFK RLGVRGDWEN PYITLKPEYE AQQIKVFGEM AKKGLIYKGL 

       190        200        210        220        230        240 
KPVYWSPSSE SALAEAEIEY KDKRSPSIYV AFPVKDGKGV LDGDEKIVIW TTTPWTIPAN 

       250        260        270        280        290        300 
LAIAVHPDLD YQVVETNGAK YVVAAALLES VAKEIGWDEV TVVKTIKGKD LEYVVAKHPF 

       310        320        330        340        350        360 
YDRDSLVICG EHVTTDAGTG CVHTAPGHGE DDFIVGQKYG LDVLCPVDER GYMTSEAPGF 

       370        380        390        400        410        420 
EGLFYDEANK AITQKLEEVG ALLKLSFITH SYPHDWRTKK PTIFRATTQW FASIDKIRGE 

       430        440        450        460        470        480 
LLQAIKETKW IPEWGEIRIH NMIRDRGDWC ISRQRAWGVP IPVFYGENGE PIITDETIEH 

       490        500        510        520        530        540 
VSNLFRQYGS NVWFEREAKD LLPEGFTHPS SPNGIFTKEI DIMDVWFDSG SSHQAVLVER 

       550        560        570        580        590        600 
DDLQRPADLY LEGSDQYRGW FNSSLSTAVA VTGKAPYKAV LSHGFVLDGE GRKMSKSLGN 

       610        620        630        640        650        660 
VVVPAKVMEQ LGADILRLWV ASVDYQADVR ISDSILKQVA EVYRKIRNTF RFMLGNLFDF 

       670        680        690        700        710        720 
NPETDAVPVN ELREVDRYMI VKLNHLIENV KHAYETYDFA SIYHDVNNFC TVDLSAFYLD 

       730        740        750        760        770        780 
FAKDILYIEA PNDRARRSIQ TVLYETVVAL TKLVAPILPH TAEEVWEHIP NRKEKEESVQ 

       790        800        810        820        830        840 
LVDMPETINI DEEDAIVAKW DAFMNLRDDV LKALEVARNE KVIGKSLTAS VTVYPTKEAR 

       850        860        870        880        890        900 
QLLGSIEEDL KQLFIVSEFT IADDYEHAPE DAQKLANVAV IVKPAEGETC ERCWVVTPEV 

       910        920 
GKDADHPTLC PRCAHIVKEH YSA 

« Hide

References

[1]"Complete sequence of chromosome of Geopacillus sp. WCH70."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Brumm P., Mead D.A., Richardson P.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WCH70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001638 Genomic DNA. Translation: ACS23899.1.
RefSeqYP_002949165.1. NC_012793.1.

3D structure databases

ProteinModelPortalC5D8P2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471223.GWCH70_1039.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS23899; ACS23899; GWCH70_1039.
GeneID7976822.
KEGGgwc:GWCH70_1039.
PATRIC21971004. VBIGeoSp101709_1117.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycGSP471223:GH2C-1123-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_GEOSW
AccessionPrimary (citable) accession number: C5D8P2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 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