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B9MRZ5 (SYI_CALBD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:Athe_1349
OrganismCaldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) (Anaerocellum thermophilum) [Complete proteome] [HAMAP]
Taxonomic identifier521460 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length920 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 – 920920Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189120

Regions

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

Sites

Metal binding8901Zinc By similarity
Metal binding8931Zinc By similarity
Metal binding9101Zinc By similarity
Metal binding9131Zinc By similarity
Binding site5601Aminoacyl-adenylate By similarity
Binding site6041ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B9MRZ5 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 64EB550849406D86

FASTA920107,205
        10         20         30         40         50         60 
MDWSQTLNLP KTDFPMRANL AQREPQFLKF WQENDIFKKM LEKNKNNKKF ILHDGPPYAN 

        70         80         90        100        110        120 
GDIHLGHALN KVLKDIVNKY KSLQGYYTPY IPGWDTHGLP IEQQVIKKLE VNRHEVDPVE 

       130        140        150        160        170        180 
FRKKCKEFAL SYIDIQRQQF KRLGVFGEWE NPYMTLDPKF EARQIRVFGE MAKKGYIYKG 

       190        200        210        220        230        240 
LKPVYWCPSC ETALAEAEIE YQEDRTYSIY VKFEVIDDKG LFSNLPIGDK KVYIVIWTTT 

       250        260        270        280        290        300 
TWTLPGNLAI ALNADFDYSL IDIGNEILVV ASELVERVMK TNKIEQYKEI ARFKGKDLEY 

       310        320        330        340        350        360 
VKCKHPFLDR TSLVILGEHV TLEAGTGCVH TAPGHGEEDF EVCQRYNIHV IVPVDNKGYL 

       370        380        390        400        410        420 
TKEAGKFAGL FYEDSNKEIA KELEASGHLL GVEKITHQYP HCWRCKNPVI FRATEQWFAS 

       430        440        450        460        470        480 
VKGFRDQALK AVDDVKWVPE WGRDRIYNMI VDRQDWCISR QRIWGVPIPI FYCKNCRKEL 

       490        500        510        520        530        540 
ITDETIDYIA KIFEKEGSDA WFSKDVKELL PEGVKCPVCG CSEFEKETDI MDVWFDSGSS 

       550        560        570        580        590        600 
HAYVLESRED LEWPCDMYLE GNDQYRGWFQ SSLLTAVATK GRAPYRIVLT HGFVVDGEGK 

       610        620        630        640        650        660 
KMSKSEGNVI SPFDIINEFG ADILRLWCVS ADYTTDMRIS KDIIKQLTEI YRKIRNTARF 

       670        680        690        700        710        720 
LLGNLYDFNP KTDKVGYENL KEIDKWALQR LYKLIEKVTK AYEEYDYNQV YHLVHNFCVI 

       730        740        750        760        770        780 
DMSNLYLDIN KDRLYASKSE SLDRRSAQTV MYEILIALTI LIAPILSFTA EEIWQNIIFK 

       790        800        810        820        830        840 
EEDAESVFLT RWPSINEDIL RDEALREKWD KIIEIKDIVS KQLEIARNEK LIGSSLDSKV 

       850        860        870        880        890        900 
KIFAKCDIKR FIEENKDIIQ EVLIVSQLDV EESDSDQIKV EVYKADGSKC ERCWKFDTMV 

       910        920 
GKNEESLNVC PRCYEVVKSK 

« Hide

References

[1]"Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Kataeva I., Adams M.W.W.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1888 / DSM 6725 / Z-1320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001393 Genomic DNA. Translation: ACM60449.1.
RefSeqYP_002573222.1. NC_012034.1.

3D structure databases

ProteinModelPortalB9MRZ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING521460.Athe_1349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM60449; ACM60449; Athe_1349.
GeneID7408930.
KEGGate:Athe_1349.
PATRIC20899814. VBIAnaThe135187_1420.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCBES521460:GH8H-1368-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_CALBD
AccessionPrimary (citable) accession number: B9MRZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 41 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