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

C3PP60 (SYI_RICAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:RAF_ORF0859
OrganismRickettsia africae (strain ESF-5) [Complete proteome] [HAMAP]
Taxonomic identifier347255 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length1092 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 – 10921092Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000216256

Regions

Motif53 – 6311"HIGH" region HAMAP-Rule MF_02003
Motif613 – 6175"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6161ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C3PP60 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 15ACF54252DACEDC

FASTA1,092125,494
        10         20         30         40         50         60 
MTNTKYYPEV NSNADFAGLE REILKFWQDN NIFQKSIDDR NGELEFIFYD GPPFANGLPH 

        70         80         90        100        110        120 
YGHLLTGFIK DVYARYQTIK GKKVERRFGW DCHGLPAEMQ SEKELGISGR LAIANFGIEK 

       130        140        150        160        170        180 
FNAHCRASVM KYANDWEEYV TRQARWVNFK NSYKTMDKNF MESVLWAFKE LYNKGLLYES 

       190        200        210        220        230        240 
MRVMPYSWAC ETPLSNFETR LDNSYRERAD KAVTVSFVLS HPVATTTGSF KEYRILAWTT 

       250        260        270        280        290        300 
TPWTLPSNLA LAVGSDIDYA LVPKNDVCYI IAAYSVSKYA KELGLSGEEN FEIIKGSALQ 

       310        320        330        340        350        360 
GLNYKSLFDY FENHPNSFKI FAGDFVVEGD GTGVVHMAPG FGEDDQILCE SKGIELVCPV 

       370        380        390        400        410        420 
DNSGKFTKEI PDLEGLQVFD ANDKIIIKLK EQGNWLKTEQ YIHNYPHCWR TDTPLIYKAV 

       430        440        450        460        470        480 
PSWYVKVTQF KDRMVELNQQ INWIPFHVKD NLFGKWLENA RDWSISRNRF WGTPLPVWKS 

       490        500        510        520        530        540 
DDPKYPRIDV YGSIEELEKD FGVKVTDLHR PFIDELTRPN PDDPTGKSTM RRIEDVFDCW 

       550        560        570        580        590        600 
FESGSMPYGQ AHYPFENKEW FEDHFPADFI VEYSAQTRGW FYTLMVLSTA LFDRPPFLNC 

       610        620        630        640        650        660 
ICHGIILDST GQKLSKRLNN YADPLELFDK YGSDALRVTM LSSNVVKGQE LLIDKDGKMV 

       670        680        690        700        710        720 
FDTLRLFIKP IWNAYHFFTM YANTDSLKGK LNFSSKNVLD VYILSKLKIA VQKIEESLDN 

       730        740        750        760        770        780 
FDTQTAYHAV SEFFEVLNNW YIRRSRARFW KSEKDTDKQN AYNTLYSCLD TMAIAMSALV 

       790        800        810        820        830        840 
PMISEAIYKG LHHCEERNDT ALSGKSNVIV RKDTSLDKAI SGVSHKIATA LSVPCNDAIS 

       850        860        870        880        890        900 
VHLCNYPTLS DFEINHELVA TMDNVLDICS NSLFIRSTEN IRVRQPLASI AIISKHNNNL 

       910        920        930        940        950        960 
KDFEDLIKDE INVKAVIYRD DLENYASKKL SINFPMLGKR LPHKMKEIIA ASKKGEWEAI 

       970        980        990       1000       1010       1020 
AGGLAICGET LNSDEYKLVL EPYSHIKGAA SFENNSSLLI LDLELTPELI EEGYARDIVR 

      1030       1040       1050       1060       1070       1080 
FIQQARKDAD FSITDRILIE IISEFNLSKI IDNYGDFIKE QTLGEFAKNF TPDYVSKVEL 

      1090 
ENHQIQLKVK KS 

« Hide

References

[1]"Analysis of the Rickettsia africae genome reveals that virulence acquisition in Rickettsia species may be explained by genome reduction."
Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B., Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.
BMC Genomics 10:166-166(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ESF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001612 Genomic DNA. Translation: ACP53720.1.
RefSeqYP_002845463.1. NC_012633.1.

3D structure databases

ProteinModelPortalC3PP60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347255.RAF_ORF0859.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP53720; ACP53720; RAF_ORF0859.
GeneID7814858.
KEGGraf:RAF_ORF0859.
PATRIC17873887. VBIRicAfr6986_1065.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARVEHMVE.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycRAFR347255:GJCT-807-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 2 hits.
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_RICAE
AccessionPrimary (citable) accession number: C3PP60
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: May 14, 2014
This is version 39 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