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A8GW18 (SYI_RICB8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:A1I_03430
OrganismRickettsia bellii (strain OSU 85-389) [Complete proteome] [HAMAP]
Taxonomic identifier391896 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length1108 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 – 11081108Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000022159

Regions

Motif53 – 6311"HIGH" region HAMAP-Rule MF_02003
Motif654 – 6585"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6571ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8GW18 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 641A2AE9DC46BAB4

FASTA1,108127,564
        10         20         30         40         50         60 
MTNTKYYPEV SSNADFATIE KEILKFWQDN NIFQKSIDIR EGDAEFIFYD GPPFANGLPH 

        70         80         90        100        110        120 
YGHLLTGFIK DVYARYQTVR GKKVERRFGW DCHGLPAEMQ SEKELGISGH LAITNFGIEK 

       130        140        150        160        170        180 
FNAHCRDSVM KYAGEWEQYV TRQARWVDFK NSYKTMDKNF MESVLWAFKE LYNKGLLYES 

       190        200        210        220        230        240 
MRVMPYSWAC ETPLSNFETR LDNSYRERAD KAVTVSFVLC HPVSKSTLDV IPWLDHGIQK 

       250        260        270        280        290        300 
TINNDSANCS MDPVDKPRYD TENFLGITAN YKEYRILAWT TTTWTLPSNL ALAVGSDIDY 

       310        320        330        340        350        360 
ALVPKGDVCY IIAASSVSKY AKELELKGDE QFTIIKGSEL QGLSYKPLFD YFKNHPNSFK 

       370        380        390        400        410        420 
IFAGDFVVEG DGTGVVHMAP GFGEDDQILC ESKGIKLVCP VDNSGKFTKE IPDLEGLQVF 

       430        440        450        460        470        480 
DANDKIIIKL KEQGNWLKTE QYIHNYPHCW RTDTPLIYKA VPSWYVKVTE FKDRMVELNQ 

       490        500        510        520        530        540 
QINWIPTHVK DNLFGKWLEN ARDWSISRNR FWGTPLPVWK SDDPKYPRID VYGSIEELEK 

       550        560        570        580        590        600 
DFGVKITDLH RPFIDELTRA NPDDPTGKST MRRIEDVFDC WFESGSMPYG QAHYPFENKQ 

       610        620        630        640        650        660 
WFEEHFPADF IVEYSAQTRG WFYTLMVLST ALFDRPPFLN CICHGVILDA TGQKLSKRLN 

       670        680        690        700        710        720 
NYADPLELFD KYGSDALRVT MLSSNVVKGQ ELLIDKDGKM VFDTLRLFIK PIWNAYHFFT 

       730        740        750        760        770        780 
MYANADHIKG ELNFTSENVL DVYILSKLKI AVEKIKESLD SFDTGTAYHA VSEFFEVLNN 

       790        800        810        820        830        840 
WYIRRSRARF WKSEKDADKQ SAYNTLYTCL ETMAIAMSSL VPLISEAIYL GLYCHPRKSG 

       850        860        870        880        890        900 
DPEKPECLDS RLCGNDNLSV HLCDYPDLSK FKINSELVDT MDTVLDICNH SLFIRSSENA 

       910        920        930        940        950        960 
RVRQPLSSIT IISKNNDKLK SFEDLIKDEI NVKSVIYRDD LENYAVKKLS INFPLLGKRL 

       970        980        990       1000       1010       1020 
PAKMKDIIAA SKKNEWEVTS GSLIICNETL NSDEYKLILE PHSHIKGASS FAHNSSLLIL 

      1030       1040       1050       1060       1070       1080 
DLELTPELID EGIARDIVRF IQQARKNADF AITDRILIDI NLPKITDIYG EFIKEQTLGK 

      1090       1100 
FAKDFIPDHI SEIELDNHKL QLKIKKVN 

« Hide

References

[1]"Complete genome sequencing of Rickettsia bellii."
Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OSU 85-389.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000849 Genomic DNA. Translation: ABV79045.1.
RefSeqYP_001496082.1. NC_009883.1.

3D structure databases

ProteinModelPortalA8GW18.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391896.A1I_03430.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV79045; ABV79045; A1I_03430.
GeneID5646403.
KEGGrbo:A1I_03430.
PATRIC17879292. VBIRicBel35792_0716.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAYETLYEC.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycRBEL391896:GH75-644-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.
IPR022439. RPE4.
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. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
TIGR03777. RPE4. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_RICB8
AccessionPrimary (citable) accession number: A8GW18
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 46 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