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Q605M7 (SYI_METCA) 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:MCA2253
OrganismMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]
Taxonomic identifier243233 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus

Protein attributes

Sequence length939 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 – 939939Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098415

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif604 – 6085"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9021Zinc By similarity
Metal binding9051Zinc By similarity
Metal binding9221Zinc By similarity
Metal binding9251Zinc By similarity
Binding site5631Aminoacyl-adenylate By similarity
Binding site6071ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q605M7 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 2A212FE9025A9D6C

FASTA939105,504
        10         20         30         40         50         60 
MDYKSTLNLP QTPFPMKANL AQREPEQIER WRTLDLYRKV RSRRAGRDKF ILHDGPPYAN 

        70         80         90        100        110        120 
GEIHIGHAVN KILKDFIVKS RTLSGFDAPY VPGWDCHGLP IELMVEKKIG KAGHKVSPAE 

       130        140        150        160        170        180 
FRKACREYAA AQVDLQRREF IRLGVLGDWE NPYLTMDFRF EADIVRALGR IAARGHLAKG 

       190        200        210        220        230        240 
AKPVHWCLDC GSALAEAEVE YENKHSPAID VRFAVVDEFG LMARFHTADG ALGEGPLSVV 

       250        260        270        280        290        300 
IWTTTPWTLP ANQAVALNPE LDYVVVQRTD IKERLVLADA LMKDVMLRCG AEGYRVIGYC 

       310        320        330        340        350        360 
KGAALEGVQL RHPFYDRIVP VILGDHVTLD AGTGAVHTAP GHGQEDYAVG QRYGLAVDNP 

       370        380        390        400        410        420 
VGGDGRFLPN TELFAGEHVL SANDHVIEVL KERGALLHEA RIEHSYPHCW RHKTPVIFRA 

       430        440        450        460        470        480 
TPQWFIAMDK GELRRQALEA IGQVQWIPDW GQARIEAMVG NRPDWCISRQ RTWGVPIPLF 

       490        500        510        520        530        540 
VHKETGALHP DTDRLIEEIA KKIETAGIDA WFELDPAELL GAEADRYGKI GDTLDVWFDS 

       550        560        570        580        590        600 
GVTHHAVLAQ NPDLAFPADL YLEGSDQHRG WFQSSLMTSV AMSGQAPYKA VLTHGFTVDA 

       610        620        630        640        650        660 
EGKKMSKSRG NVVAPQKVMQ TLGADVLRLW VAATDYRGEM TVSDEILKRI SDVYRRIRNT 

       670        680        690        700        710        720 
ARYLLANLDG FDPALHLVKP EDMLALDRWV VDRALAIQQE VIEAYETYQF NTIFQKTHHF 

       730        740        750        760        770        780 
CSVDLGSFYL DVLKDRQYTC KTDSLPRRSG QTAMYHIAEA MVRWLAPVLS FTAEEIWQYL 

       790        800        810        820        830        840 
PGQREESVFL SEWYDGLFGL DENSRCDRAF WDQMLKIREA VSKELEILRV RGEIGASLDA 

       850        860        870        880        890        900 
EVELFCDPPL FRKLSEAGDE LRFVLLTSYA TVKPAAEAGT DALPTEIPGL ELKLAASGKP 

       910        920        930 
KCVRCWHHRH DVGTHPDHPE LCGRCVDNVA GTGELRTFG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017282 Genomic DNA. Translation: AAU91752.1.
RefSeqYP_114671.1. NC_002977.6.

3D structure databases

ProteinModelPortalQ605M7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243233.MCA2253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU91752; AAU91752; MCA2253.
GeneID3103165.
KEGGmca:MCA2253.
PATRIC22608354. VBIMetCap22254_2281.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

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_METCA
AccessionPrimary (citable) accession number: Q605M7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 23, 2004
Last modified: April 16, 2014
This is version 70 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