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Q5HPZ9 (SYI_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:SERP0758
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length916 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
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 – 916916Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098472

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif595 – 5995"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8851Zinc By similarity
Metal binding8881Zinc By similarity
Metal binding9051Zinc By similarity
Metal binding9081Zinc By similarity
Binding site5541Aminoacyl-adenylate By similarity
Binding site5981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HPZ9 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: E2703272E7420212

FASTA916105,164
        10         20         30         40         50         60 
MNYKDTLLMP KTDFPMRGGL PNKEPQIQEM WDNDDQYRKA LEKNKNNPSF ILHDGPPYAN 

        70         80         90        100        110        120 
GNLHMGHALN KIIKDFIVRY KTMQGFYAPY VPGWDTHGLP IEQALTKKGV DRKKMSVAEF 

       130        140        150        160        170        180 
REKCKEFALK QIDIQKKDFK RLGVRGDFNN PYITLTPEYE AAQIRLFGEM ADKGLIYKGK 

       190        200        210        220        230        240 
KPVYWSPSSE SSLAEAEIEY HDKRSASIYV AFDVKDSKGK VDSDAQFIIW TTTPWTIPSN 

       250        260        270        280        290        300 
VAITVHPELK YGQYNVDGHK YIVAQALSEE VAEALGWDKD SIQLEKEFTG KELEFVEAQH 

       310        320        330        340        350        360 
PFLDRVSLVI NGEHVTTDAG TGCVHTAPGH GEDDYIVGQK YDLPVISPLN DKGVFTEEGG 

       370        380        390        400        410        420 
PFEGMFYDKA NKAVTDLLKE KDALLKLDFI THSYPHDWRT KKPVIFRATP QWFASINKVR 

       430        440        450        460        470        480 
QDILDAIEDT NFKVDWGKTR IYNMIRDRGE WVISRQRVWG VPLPVFYAEN GDIIMTKETV 

       490        500        510        520        530        540 
NHVADLFEKH GSNIWFEKEA KELLPEGFSH PGSPNGEFTK ETDIMDVWFD SGSSHRGVLE 

       550        560        570        580        590        600 
TRPELSFPAD LYFEGSDQYR GWFNSSITTA VATRGQAPYK FLLSHGFVMD GEGKKMSKSL 

       610        620        630        640        650        660 
GNVIVPDQVV KQKGADIARL WVSSTDYLSD VRISDEILKQ TSDVYRKIRN TLRFMLGNIN 

       670        680        690        700        710        720 
DFNPETDSIA ETNLLEVDRY LLNRLREFTA STINNYENFD YLNIYQEVQN FINVELSNFY 

       730        740        750        760        770        780 
LDYGKDILYI EKKDSHKRRS MQTVLYQILV DMTKLLAPIL VHTAEEVWSH TPHVKEESVH 

       790        800        810        820        830        840 
LSDMPKVVDV DEELLEKWNT FMNLRDDVNR ALEQARNEKV IGKSLEAKVV IGSNESFNTA 

       850        860        870        880        890        900 
EFLQQFNDLQ QLFIVSQVEV KDKVNDGVSY QYGDIHIKHA EGEKCERCWN YTEELGSVGE 

       910 
LEHLCPRCQE VVKTLV 

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References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54153.1.
RefSeqYP_188341.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HPZ9.
SMRQ5HPZ9. Positions 1-916.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP0758.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54153; AAW54153; SERP0758.
GeneID3242826.
KEGGser:SERP0758.
PATRIC19612389. VBIStaEpi130894_0737.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-784-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.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 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_STAEQ
AccessionPrimary (citable) accession number: Q5HPZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 76 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