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

A3CLP4 (SYI_STRSV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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:SSA_0661
OrganismStreptococcus sanguinis (strain SK36) [Complete proteome] [HAMAP]
Taxonomic identifier388919 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length930 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 – 930930Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022132

Regions

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

Sites

Metal binding8881Zinc By similarity
Metal binding8911Zinc By similarity
Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Binding site5541Aminoacyl-adenylate By similarity
Binding site5981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A3CLP4 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 8C7E2BCC6478234E

FASTA930105,550
        10         20         30         40         50         60 
MKLKETLNLG KTAFPMRAGL PNKEPIWQKE WDQAKLYQRR QELNEGKPHF ILHDGPPYAN 

        70         80         90        100        110        120 
GNIHVGHAMN KISKDIIVRS KSMAGYYAPY IPGWDTHGLP IEQVLAKQGV KRKELDLVEY 

       130        140        150        160        170        180 
LNMCRDYALS QVEKQKEDFK RLGVSGDWEN PYVTLTPDYE AAQIRVFGEM AKKGYIYRGA 

       190        200        210        220        230        240 
KPVYWSWSSE SALAEAEIEY HDLVSTSLYY ANRVKDGKGV LDTDTYIVVW TTTPFTITAS 

       250        260        270        280        290        300 
RGLTVGADID YVVVQPAGES RKFVVASELL NSLSEKFGWA DVQVLATYRG QELNHIVTVH 

       310        320        330        340        350        360 
PWDTAVDELV ILGDHVTTDS GTGIVHTAPG FGEDDYNVGV ANDLEVFVTV NERGIMMENA 

       370        380        390        400        410        420 
GPDFAGQFYD KVAPTVIEKL GDLLLAQEEI SHSYPFDWRT KKPIIWRAVP QWFASVSKFR 

       430        440        450        460        470        480 
QEILDEIEKV KFHSEWGKVR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTPIMTAETI 

       490        500        510        520        530        540 
EHVAQLFEEH GSIVWWKREA KDLLPEGFTH PGSPNGEFTK ETDIMDVWFD SGSSWNGVVV 

       550        560        570        580        590        600 
NRPELTYPAD LYLEGSDQYR GWFNSSLITS VANHGVAPYK QILSQGFALD GKGEKMSKSL 

       610        620        630        640        650        660 
GNTIAPSDVE KQFGAEILRL WVTSVDSSND VRISMDILSQ VSETYRKIRN TLRFLIANTS 

       670        680        690        700        710        720 
DFNPVEDAVA YEELRSVDKY MTIRFNQLVE TIRKAYADFE FLTIYKAIVN FVTVDLSAFY 

       730        740        750        760        770        780 
LDFAKDIVYI EAAKSLERRQ MQTVFYDVLV KITKLLTPIL PHTAEEIWSY LEHEEEEFVQ 

       790        800        810        820        830        840 
LSELPEAQTF PNQEEILDTW SAFMDFRSQA QKALEEARNE KVIGKSLEAH LTVYPNEVIK 

       850        860        870        880        890        900 
TLLEAVNSDV AQLLIVSQLT IAEGPAPEGA LVFEDVAFVV EHAQGQVCDR CRRIDTTVQE 

       910        920        930 
RSYQALVCDH CAEILEENFA QAVSEGFEAN 

« Hide

References

[1]"Genome of the opportunistic pathogen Streptococcus sanguinis."
Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L., Buck G.A.
J. Bacteriol. 189:3166-3175(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SK36.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000387 Genomic DNA. Translation: ABN44099.1.
RefSeqYP_001034649.1. NC_009009.1.

3D structure databases

ProteinModelPortalA3CLP4.
SMRA3CLP4. Positions 1-917.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING388919.SSA_0661.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN44099; ABN44099; SSA_0661.
GeneID4806788.
KEGGssa:SSA_0661.
PATRIC19768350. VBIStrSan33173_0637.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycSSAN388919:GHEN-670-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_STRSV
AccessionPrimary (citable) accession number: A3CLP4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 61 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