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A4IM25 (SYI_GEOTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:GTNG_1001
OrganismGeobacillus thermodenitrificans (strain NG80-2) [Complete proteome] [HAMAP]
Taxonomic identifier420246 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length924 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 – 924924Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022071

Regions

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

Sites

Metal binding8911Zinc By similarity
Metal binding8941Zinc By similarity
Metal binding9111Zinc By similarity
Metal binding9141Zinc By similarity
Binding site5521Aminoacyl-adenylate By similarity
Binding site5961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4IM25 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 1E5311B4A319A8AB

FASTA924104,675
        10         20         30         40         50         60 
MDYKETLLMP QTEFPMRGNL PKREPEMQKK WEEMDIYRKV QERTKGRPLF VLHDGPPYAN 

        70         80         90        100        110        120 
GDIHMGHALN KILKDIIVRY KSMSGFCAPY VPGWDTHGLP IETALTKQGV DRKSMSVAEF 

       130        140        150        160        170        180 
RKLCEQYAYE QIDNQRQQFK RLGVRGDWDN PYITLKPEYE AQQIKVFGEM AKKGLIYKGL 

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

       250        260        270        280        290        300 
LAIAVHPDLD YYIVEANGQK YVVAAALAES VAKEVGWEAW SVVKTVKGKE LEYVVAKHPF 

       310        320        330        340        350        360 
YERDSLVVCG EHVTTDAGTG CVHTAPGHGE DDFIVGQKYG LPVLCPVDER GYMTEEAPGF 

       370        380        390        400        410        420 
AGMFYDEANK AITQKLEEVG ALLKLSFITH SYPHDWRTKQ PTIFRATTQW FASIDKIRDQ 

       430        440        450        460        470        480 
LLDAIKETKW VPEWGEIRIH NMVRDRGDWC ISRQRAWGVP IPVFYGENGE PIITDETIEH 

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

       550        560        570        580        590        600 
DDLERPADLY LEGSDQYRGW FNSSLSTAVA VTGKAPYKGV LSHGFVLDGE GRKMSKSLGN 

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

       670        680        690        700        710        720 
DPNQNAVPVG ELGELDRYML AKLNKLIAKV KKAYDSYDFA AVYHEMNHFC TVELSAFYLD 

       730        740        750        760        770        780 
MAKDILYIEA ADCRARRAVQ TVLYETVVAL AKLIAPILPH TADEVWEHIP NRKEQVESVQ 

       790        800        810        820        830        840 
LTDMPEPMAI DGEEALLAKW DAFMDVRDDI LKALENARNE KVIGKSLTAS VTVYPKDEVR 

       850        860        870        880        890        900 
ALLASINEDL RQLLIVSAFS VADESYDAAP AEAERLNHVA VIVRPAEGET CERCWTVTPD 

       910        920 
VGRDESHPTL CPRCAHIVNE HYSA 

« Hide

References

[1]"Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NG80-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000557 Genomic DNA. Translation: ABO66379.1.
RefSeqYP_001125124.1. NC_009328.1.

3D structure databases

ProteinModelPortalA4IM25.
SMRA4IM25. Positions 2-871.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420246.GTNG_1001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO66379; ABO66379; GTNG_1001.
GeneID4965944.
KEGGgtn:GTNG_1001.
PATRIC21978339. VBIGeoThe136879_1053.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycGTHE420246:GIXT-1073-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_GEOTN
AccessionPrimary (citable) accession number: A4IM25
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2007
Last modified: May 14, 2014
This is version 56 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