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Q6G4S5 (SYI_BARHE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:BH02580
OrganismBartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier283166 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length971 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_02002

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002.

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_02002

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 971971Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098353

Regions

Motif64 – 7411"HIGH" region HAMAP-Rule MF_02002
Motif643 – 6475"KMSKS" region HAMAP-Rule MF_02002

Sites

Binding site6021Aminoacyl-adenylate By similarity
Binding site6461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G4S5 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: D404145683BF5EDA

FASTA971110,734
        10         20         30         40         50         60 
MTVKNETVDY SKTLYLPQTN FPMRAGLPQK ELELMERWEK RGLYAQLRQQ AKDRPLYTLH 

        70         80         90        100        110        120 
DGPPYANGHI HIGHALNKVL KDVIIRSFQM RGFNANYVPG WDCHGLPIEW KIEEKYRAQG 

       130        140        150        160        170        180 
KNKDDVPLNE FRQECRQFAQ HWITVQSEEF KRLGVVGDFN RPYTTMAFHA EARIASELMK 

       190        200        210        220        230        240 
FALSDQIYRG SKPVMWSVVE RTALAEAEIE YHDHESDVIW VKFPVLQADS KDLYDAYVVI 

       250        260        270        280        290        300 
WTTTPWTIPA NRAVSYSSQI SYSIYEVKSA ENDFGPQVGE KLLFADALVM SCAEKAKLVL 

       310        320        330        340        350        360 
KRLRVISAKE FKTLVLSHPL KGLAGGYNNK IAMLDGSHVT ESAGTGFVHT APSHGREDFE 

       370        380        390        400        410        420 
IWNAYKPLLE QSGIDSSIPF PVDDAGFYTK DAPGFGPDRK GGAIRVIDDN GKMGDANKEV 

       430        440        450        460        470        480 
INALIKADRL FARGRLKHSY PHSWRSKKPI IFRNTPQWFI SMDKDLGDGS TLRSRALKAI 

       490        500        510        520        530        540 
SMTRFVPSSG QNRLASMIAD RPDWVLSRQR AWGVPICIFA NEDGVILKDE RVNERILRAF 

       550        560        570        580        590        600 
EAEGADAWFA EGARERFLGE RAHESWIQVV DILDVWFDSG ASHSFVLEDR DDLNWPADVY 

       610        620        630        640        650        660 
FEGSDQHRGW FQSSLLESCG TRACSPYKAV ITHGFTLDEN GKKMSKSLGN TVVPQEIIKT 

       670        680        690        700        710        720 
FGADIFRLWV MTTDYWEDQR LGKQILQTNV DSYRKLRNAI RWMLGTLAHD EGEEISYCAL 

       730        740        750        760        770        780 
PDLEKLILHR LSELDQLVNR AYDDFDFKKI MRALLDFSIT ELSAFYFDIR KDSLYCDPPS 

       790        800        810        820        830        840 
SKKRKASLQV VREIFERMVI WLAPMLPFTM EEAWLERYPE STSVHLEQFR PVPMEWQNES 

       850        860        870        880        890        900 
LAERWKKIRQ VRKVVTGALE LERADKRIGS SLEAAPIVFI SNPVLREALE NLDMAEICIT 

       910        920        930        940        950        960 
SALTITQGVP PSDAFILSDV EGVGVYPRKA LGTKCARSWR YTQDVGSDPT YPDVSARDAA 

       970 
ALRELQVLGK I 

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References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897699 Genomic DNA. Translation: CAF27070.1.
RefSeqYP_033110.1. NC_005956.1.

3D structure databases

ProteinModelPortalQ6G4S5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283166.BH02580.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF27070; CAF27070; BH02580.
GeneID2865553.
KEGGbhe:BH02580.
PATRIC20544261. VBIBarHen29080_0287.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycBHEN283166:GIVZ-258-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
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]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_BARHE
AccessionPrimary (citable) accession number: Q6G4S5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 66 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