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A4XKR2 (SYI_CALS8) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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:Csac_1912
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [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_1000022052

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
A4XKR2 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: C35E80AF111A9BFF

FASTA920107,030
        10         20         30         40         50         60 
MDWSQTLNLP KTDFPMRANL AQREPQFLRF WEENDIFKKM LKKNRNNKKF ILHDGPPYAN 

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

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

       190        200        210        220        230        240 
LKPVYWCPSC ETALAEAEIE YQEDKTYSIY VKFEVIDDKG LFANLNLSGK KVYIVIWTTT 

       250        260        270        280        290        300 
TWTLPGNLAI ALNTDFDYSL VDVGNEILIV ASELVERVMK TNKIDQYHEI ARFKGKDLEY 

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

       370        380        390        400        410        420 
TQEAGKFAGL FYEDSNKEIA KELEASDHLL GVEKITHQYP HCWRCKNPVI FRATEQWFAS 

       430        440        450        460        470        480 
VKGFREEALK AVDDVKWVPE WGRDRIYNMI ADRQDWCISR QRIWGVPIPI FYCKNCRKEL 

       490        500        510        520        530        540 
ITDETIDHIA KIFEKEGSDA WFSKDVKELL PEGTKCPVCG CMEFEKETDI 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 KTDKVGCENL KEIDKWALQR LYKLIEKVTK AYEEYDYNQV YHLVHNFCVI 

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

       790        800        810        820        830        840 
EEDAESVFLT SWPKVNENIL KDETLEEKWN KIIEIKDIVA KQLEIARNEK LIGSSLDSKV 

       850        860        870        880        890        900 
KIFAKGNIKR FIEENKDIIQ EVLIVSQLEV EEGDSDQIKV EVYKADGLKC ERCWKFDTMV 

       910        920 
GKNEENLNVC PRCYEVVKVK 

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000679 Genomic DNA. Translation: ABP67497.1.
RefSeqYP_001180688.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XKR2.
SMRA4XKR2. Positions 1-918.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351627.Csac_1912.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP67497; ABP67497; Csac_1912.
GeneID5088631.
KEGGcsc:Csac_1912.
PATRIC21253572. VBICalSac56748_2092.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBCLSK2473335.

Enzyme and pathway databases

BioCycCSAC351627:GJ17-1953-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_CALS8
AccessionPrimary (citable) accession number: A4XKR2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: April 16, 2014
This is version 51 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