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Q49WX5 (SYI_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:SSP1578
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [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_0000098474

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
Q49WX5 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 74E0CF2322EA81CC

FASTA916104,782
        10         20         30         40         50         60 
MDYKDTLLMP KTDFPMRGGL PNKEPKIQEE WDAKNIYQKV LDKNEGNPSF ILHDGPPYAN 

        70         80         90        100        110        120 
GNLHMGHALN KILKDIITRY KSMLGYYAPY VPGWDTHGLP IEQALTKKGV KRKELSIAEF 

       130        140        150        160        170        180 
RKKCEAFALE QIDNQKKDFK RLGVKGDFNN PYITLKPEYE AAQIRLFGEM ADKGLIYKGK 

       190        200        210        220        230        240 
KPVYWSPSSE SSLAEAEIEY QDKRSPSIYV AFDVIDGKGI VDDDAQFIIW TTTPWTLPSN 

       250        260        270        280        290        300 
VAITVHPDLT YGQYNVNGKK YIIGKDLASD VAEALDWDED TLELEKEFKG KDLEYIKAQH 

       310        320        330        340        350        360 
PFFDRESLVI NGLHVTTDAG TGCVHTAPGH GEDDYIVGQK YNLPVISPVD DKGVFTDEAG 

       370        380        390        400        410        420 
QFEGMFYDKA NKEITDLLKE DGSLLKLEFI THSYPHDWRT KKPVIFRATP QWFASIDKVR 

       430        440        450        460        470        480 
EDILSAIDDT QFKVDWGKTR IYNMIRDRGE WVISRQRVWG VPLPVFYAEN GDIIMTSETV 

       490        500        510        520        530        540 
NHVADLFEAN GSNIWFEREA KDLLPEGFTH PGSPNGEFTK ETDIMDVWFD SGSSHRGVLE 

       550        560        570        580        590        600 
ARPELSYPAD LYLEGSDQYR GWFNSSITTS VATRGQSPYK MLLSHGFVMD GEGKKMSKSL 

       610        620        630        640        650        660 
GNVIVPDQIV KQKGADIARL WVSSVDYLAD VRISDEILKQ SSDVYRKIRN TLRFMLGNVS 

       670        680        690        700        710        720 
DYNPATDAIA EKDLLEVDKY LLNRLREFTA NTLDHYDNYD YLDIYQEVQN FINVELSNFY 

       730        740        750        760        770        780 
LDYGKDILYI EERDSHKRRS MQTVLYQIVV DMTKLLAPIL VHTAEEVWSH IPHVEEESVH 

       790        800        810        820        830        840 
LTNMPERVEI DQAFVDRWNT FMKLRDDVNR ALEVARNEKV IGKSLEAKVV IGSNENFDAT 

       850        860        870        880        890        900 
TFLQQFKDLQ QLFITSQAEV VDKVDDGVAY QHGDIRIEHA HGEKCERCWN YSEELGSVGE 

       910 
LDNLCPRCQA VVKTLV 

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References

[1]"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15305 / DSM 20229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008934 Genomic DNA. Translation: BAE18723.1.
RefSeqYP_301668.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ49WX5.
SMRQ49WX5. Positions 1-916.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342451.SSP1578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE18723; BAE18723; SSP1578.
GeneID3615322.
KEGGssp:SSP1578.
PATRIC19624746. VBIStaSap90642_1580.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMALGRRSCQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycSSAP342451:GKFA-1637-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_STAS1
AccessionPrimary (citable) accession number: Q49WX5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 71 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