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Q9ZCU4 (SYI_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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:RP617
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length1086 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
Reference 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 – 10861086Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098560

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
Q9ZCU4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: DEC857A0D81E5963

FASTA1,086125,637
        10         20         30         40         50         60 
MTNTKYYPDV SANVDFAAIE QEILKFWQNN NIFQKSIDYR NGESEFIFYD GPPFANGLPH 

        70         80         90        100        110        120 
YGHLLTGFIK DVYARYKTIK GKKVERRFGW DCHGLPAEMQ SEKELGISGR IAITNFGIEK 

       130        140        150        160        170        180 
FNNHCRASVM QYASEWEQYV TRQARWVAFK NAYKTMDKNF MESVLWAFKE LYNKDLLYES 

       190        200        210        220        230        240 
MRVMPYSWAC ETPLSNFETR LDNAYRERTD KAITVSFVLN EVTLINGIIS QKSDMKEGDN 

       250        260        270        280        290        300 
FKEYRILAWT TTPWTLPANL ALAVGSDIDY AFVDKNEVCY IIAASSVAKY AKELGLSGKE 

       310        320        330        340        350        360 
NFEIIKGLKL QGLSYKPLFN YFENHPNSFK IFASDFVVEG DGTGIVHMAP GFGEDDQILC 

       370        380        390        400        410        420 
ESKGIELVCP VDNSGKFTKE IPDLEGVQVF DANDKIIIKL KEQGNWIKTE QYIHNYPHCW 

       430        440        450        460        470        480 
RTDTPLIYKA VPSWYVRVTK FKDRMVELNQ QINWIPHNVK DNLFGKWLEN ARDWSISRNR 

       490        500        510        520        530        540 
FWGTPLPVWK SDDPKYPRID VYGSIEEIEK DFGVKINDLH RPFIDELTRT NPDDPTGKST 

       550        560        570        580        590        600 
MRRIDDVFDC WFESGSMPYG QVHYPFENKK WFVEHFPADF IVEYSSQTRG WFYTLMVLST 

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

       670        680        690        700        710        720 
ELLIDKDGKM VFDTLRLFIK PIWNAYHFFT IYANADSLKG TLNFASQNVL DVYILSKLKI 

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

       790        800        810        820        830        840 
KIMTIAMSAL IPMISETIYQ GLHNTAITQL NCLLSEGKHI VQNPMSDTQD YNTSVHLCNY 

       850        860        870        880        890        900 
PTLSDFEINY ELVSTMDNVL DICSNSLFIR STENIRVRQP LACITIISKH NNNLKDFEDL 

       910        920        930        940        950        960 
IKDEINVKTV IYRDDLENYA RKKLSLNFAI LGKRLPHKMK AIIDAAKKGE WEATTLGLAI 

       970        980        990       1000       1010       1020 
CGEILNSDEY TLILEPYSHI KGTANFDNNS SLLILNLELT SELIEEGYAR DIVRFIQYAR 

      1030       1040       1050       1060       1070       1080 
KEADFSITDR ILIEIISEFD LSKIIDHYGD FIKEQTLGEF AKNFTPDYVS KVALENNQIQ 


LKVKRL 

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235272 Genomic DNA. Translation: CAA15060.1.
PIRB71667.
RefSeqNP_220984.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZCU4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272947.RP617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA15060; CAA15060; CAA15060.
GeneID883643.
KEGGrpr:RP617.
PATRIC17902053. VBIRicPro72556_0636.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARVEHMVE.
OrthoDBEOG644ZM1.

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_RICPR
AccessionPrimary (citable) accession number: Q9ZCU4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 84 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 prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries