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Q92H19 (SYI_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:RC0953
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [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.

Sequence caution

The sequence AAL03491.1 differs from that shown. Reason: Erroneous initiation.

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_0000098558

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
Q92H19 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 97E4CE3E51AB91DD

FASTA1,092125,342
        10         20         30         40         50         60 
MTNTKYYPEV SSNADFAGLE REILKFWQDN NIFQKSIDDR NGESEFIFYD GPPFANGLPH 

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

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

       190        200        210        220        230        240 
MRVMPYSWAC ETPLSNFETR LDNSYRERAD KAVTVSFVLS HPVTTTTGSF 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 
ICHGVILDST GQKLSKRLNN YADPLELFDK YGSDALRVTM LSSNVVKGQE LLIDKDGKMV 

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

       730        740        750        760        770        780 
FDTQTAYHAV SAFFEVLNNW YIRRSRARFW KSAKDTDKQN AYNTLYSCLD TMAIAMSALV 

       790        800        810        820        830        840 
PMISEAIYKG LRHCEERNDT ALSGKSNIIA RKDTSLDKAI SGVSHKIATA LSVPRNDAIS 

       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 
TGGLAICGET LNSDEYKLVL EPYSHIKGAA SFENNSSLLI LDLELTPELI EEGYARDIVR 

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

      1090 
ENHQIQLKVK KS 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL03491.1. Different initiation.
PIRA97819.
RefSeqNP_360590.2. NC_003103.1.

3D structure databases

ProteinModelPortalQ92H19.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0953.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL03491; AAL03491; RC0953.
GeneID927861.
KEGGrco:RC0953.
PATRIC17889296. VBIRicCon45613_1086.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARVEHMVE.
OrthoDBEOG644ZM1.

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_RICCN
AccessionPrimary (citable) accession number: Q92H19
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 74 of the entry and version 2 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 conorii

(strain Malish 7): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries