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Q4UMD8 (SYI_RICFE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:RF_0423
OrganismRickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi) [Complete proteome] [HAMAP]
Taxonomic identifier315456 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length1094 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 – 10941094Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098559

Regions

Motif53 – 6311"HIGH" region HAMAP-Rule MF_02003
Motif624 – 6285"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6271ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4UMD8 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 8C4804C46D115EB6

FASTA1,094125,428
        10         20         30         40         50         60 
MTNTKYYPEV SSNADFAAIE REILKFWQDN NIFQKSIDDR NGESEFIFYD GPPFANGLPH 

        70         80         90        100        110        120 
YGHLLTGFIK DVYARYQTVK GKKVERRFGW DCHGLPAEMQ SEKELGISGR LAITNFGIEK 

       130        140        150        160        170        180 
FNSHCRASVM KYASDWEEYV TRQARWVDFK NSYKTMDKNF MESVIWAFKE LYNKGLLYES 

       190        200        210        220        230        240 
MRVMPYSWAC ETPLSNFETR LDNSYRERAD KAVTVSFVLN EIPAINGMTS RESGTTSSGD 

       250        260        270        280        290        300 
YKEYRILAWT TTPWTLPSNL ALAVGSDIDY ASIPKEDICY IIAASSVSKY AKELGLSGEE 

       310        320        330        340        350        360 
NFEIIKGSAL QGLSYKPLFD YFANHPNSFK IFAGDFVVEG DGTGIVHMAP GFGEDDQILC 

       370        380        390        400        410        420 
ESKGISLVCP VDNSGKFTKE IPDLEGVQVF DANDKIIIKL KEQGNWLKTE QYIHNYPHCW 

       430        440        450        460        470        480 
RTDTPLIYKA VPSWYVKVTQ FKDRMVELNQ QINWIPFHVK DNLFGKWLEN ARDWSISRNR 

       490        500        510        520        530        540 
FWGTPLPVWK SDDPKYPRID VYGSIEELEK DFGVKVTDLH RPFIDELARP NPNDPTGKST 

       550        560        570        580        590        600 
MRRIEDVFDC WFESGSMPYG QAHYPFENKK WFEDHFPADF IVEYSAQTRG WFYTLMVLST 

       610        620        630        640        650        660 
ALFDRPPFLN CICHGVILDA TGQKLSKRLN NYADPLELFD KYGSDALRVT MLSSNVVKGQ 

       670        680        690        700        710        720 
ELLIDKDGKM VFDTLRLFIK PIWNAYHFFT MYANADSLKG ELNFASQNVL DIYILSKLKI 

       730        740        750        760        770        780 
AVNKIEESLD NFDTQTAYHA VSEFFEVLNN WYIRRSRARF WKSEKDADKQ NAYNTLYSCL 

       790        800        810        820        830        840 
ETMAIAMSAL VPMISEAIYL GLCHKRPDVI ARKDLSLDEA ISGNSHEIAT ALSVPRNDGS 

       850        860        870        880        890        900 
ISVHLCNYPN LSSFEINHEL VATMDNVLDI CSNSLFIRST ENIRVRQPLA TITIISKHND 

       910        920        930        940        950        960 
KLKSFEDLIK DEINVKSVIY RDDLENYASK KLSINFPMLG KRLPAKMKEI IAASKKGEWE 

       970        980        990       1000       1010       1020 
AIGGGLAICD ETLNSDEYKL VLEPHVHIKG AASFENNSSL LILDLELTAE LIEEGYARDI 

      1030       1040       1050       1060       1070       1080 
VRFIQQARKD ADFSITDRIL IEIISEFDLS KIIDNYGDFI KEQTLGEFSK NFTPDYVSKV 

      1090 
ELENHQIQLK VKRS 

« Hide

References

[1]"The genome sequence of Rickettsia felis identifies the first putative conjugative plasmid in an obligate intracellular parasite."
Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., Parinello H., Claverie J.-M., Raoult D.
PLoS Biol. 3:1-12(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-1525 / URRWXCal2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000053 Genomic DNA. Translation: AAY61274.1.
RefSeqYP_246439.1. NC_007109.1.

3D structure databases

ProteinModelPortalQ4UMD8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315456.RF_0423.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY61274; AAY61274; RF_0423.
GeneID3400708.
KEGGrfe:RF_0423.
PATRIC17891332. VBIRicFel64634_0500.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycRFEL315456:GKEK-436-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_RICFE
AccessionPrimary (citable) accession number: Q4UMD8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2005
Last modified: April 16, 2014
This is version 62 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

Rickettsia felis (Rickettsia azadi)

Rickettsia felis (strain URRWXCal2): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries