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

Q899C3 (SYI_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. 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:CTC_00261
OrganismClostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]
Taxonomic identifier212717 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length1036 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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 – 10361036Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098535

Regions

Motif48 – 5811"HIGH" region HAMAP-Rule MF_02003
Motif590 – 5945"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5931ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q899C3 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 53261B634ADDD476

FASTA1,036120,322
        10         20         30         40         50         60 
MYKKIDGSKS FVQMEREVLD FWNKNNIVDK SFALNEEGEY FTFYDGPPTA NGKPHVGHVL 

        70         80         90        100        110        120 
TRVIKDLIPR YKVMKGYKVL RKAGWDTHGL PVELEIEKKL GISGKEEIEK FGVEEFIKEC 

       130        140        150        160        170        180 
KDSVFTYSSM WKDMSEKLAF WVDMENPYVT YHNDYIESVW WALKQLWNKE LLYKGHKVIP 

       190        200        210        220        230        240 
YCPRCGTALS SHEVAQGYKD VKEATAFVKF KVKGEENKYI LAWTTTPWTL PSNVALAINK 

       250        260        270        280        290        300 
NFDYVEVKNN DEVLILAKEL VDSVIDGEYE IIKEFKGEDI LGLQYEQLLP FYTPEEEAFR 

       310        320        330        340        350        360 
VIHGDFVTLS DGTGIVHTAP AYGEDDNIVC KKHGLPMINL VDKEGKFIDC VEPWKGMPVK 

       370        380        390        400        410        420 
KADSKIIEYM DEKGILYKSE KFTHSYPHCW RCDTALLYYP TDSWFVRMTS LRDKLLENNN 

       430        440        450        460        470        480 
KVNWYPDNIR TGRFGKFLEN VIDWGISRDR YWGTPLPIWE CECGHRECIG SISELKEKGI 

       490        500        510        520        530        540 
DVPEDIELHK PYIDKVKLKC SKCGKEMKRT REVIDCWFDS GSMPFAQHHY PFENKEVFEK 

       550        560        570        580        590        600 
TFPAQFISEA VDQTRGWFYT LTAISTAIFD TNPFENCIVL GHVLDKHGLK MSKSKGNVVD 

       610        620        630        640        650        660 
PFDVLDSAGA DASRWHFYTA SAPWLPTRFS PEDVEETQRK FLSTLWNVYS FYVLYADIDK 

       670        680        690        700        710        720 
FNPLEYKDFV SENVMDKWIV SKLNSLIKDV EDHMDSYRIT QAALAIEDFV DELSNWYVRR 

       730        740        750        760        770        780 
NRSRFWSEEL REDKIGAYVT LYKVLTTVSL IAAPFVPFIT EEIYNNLVRG LDKNALESIH 

       790        800        810        820        830        840 
LCNWPKYDEN LIQKELEREM DEAYKIVKLG RSARNSVNIK NRQPLSSMLV SIKTLPEYYG 

       850        860        870        880        890        900 
RIIKDELNIK DIIFGADLSS YVEFNIKPNL PVLGKAYGRY IPQIRKEITS MDQMKLAQKI 

       910        920        930        940        950        960 
KQGEKVIINI DGNEIELNEE NLLVTMKGLE GFAFAGEGNI GVVLNTTITD ELKEEGQLRE 

       970        980        990       1000       1010       1020 
ILSKIQNMRK EKEFEVADRI KLYVSGNRML ESVVEKFEDI IRKETIAEEV IYNEEREYVD 

      1030 
CKINGEDFKI EVEAIK 

« Hide

References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015927 Genomic DNA. Translation: AAO34906.1.
RefSeqNP_780969.1. NC_004557.1.

3D structure databases

ProteinModelPortalQ899C3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING212717.CTC00261.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO34906; AAO34906; CTC_00261.
GeneID1059829.
KEGGctc:CTC00261.
PATRIC19508330. VBICloTet101274_0226.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycCTET212717:GJAM-221-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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.
[Graphical view]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_CLOTE
AccessionPrimary (citable) accession number: Q899C3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 70 of the entry and version 2 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