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C3N5S5 (SYI_SULIA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 37. 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:M1627_1468
OrganismSulfolobus islandicus (strain M.16.27) [Complete proteome] [HAMAP]
Taxonomic identifier427318 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length1049 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.

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 – 10491049Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000216258

Regions

Motif48 – 5912"HIGH" region HAMAP-Rule MF_02003
Motif597 – 6015"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6001ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C3N5S5 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 6E9C7F840E1C9E40

FASTA1,049121,984
        10         20         30         40         50         60 
MKPLTGNYDP KKIEDEIISF WEENKIYNKL RDIVSKRREK FLFIDGPPYP SSPTPHIGTI 

        70         80         90        100        110        120 
WNKVIKDCIL RYERLLGKKV HDQPGYDTHG LPIEVATERL LGILNKQEII DKIGVENFIN 

       130        140        150        160        170        180 
KCKEFALSNA TKMTQNFKDV GVFMDWERPY YTLDPSYISS SWSVIKKAYE KGMLDKGTAV 

       190        200        210        220        230        240 
LHWCPRCETT LSDYEVSEYR DLEDPSIYVK FKIKGEENRY LLIWTTTPWT IPSNVFVMVN 

       250        260        270        280        290        300 
KDYDYADVEV NGEVLVLAKD RIEAVMKEAS ITNYKVLRTY KGSELIGVKY KHPLRDFVSA 

       310        320        330        340        350        360 
QTKLDDFHQV VDAGNVVTLT DGTGLVHAAT GHGEEDFLIG QKYGFPVVMF VNDRGEFTEE 

       370        380        390        400        410        420 
GGKYKGLKVR DASKVIINDL KSKNALFFEG KIVHRYPVCW RCKTPLVLRA IDQWFIRVTK 

       430        440        450        460        470        480 
IKDEMLKEIE NVNWIPDWGK SRISNMVKEL RDWVISRQRF WGTPLPIWIC EKCNNVIVVG 

       490        500        510        520        530        540 
SREDLESIAI DSVPNDLHRP WIDNVRVKCN KCGGVAKRIA DVADVWFDSG VAFFASLGKD 

       550        560        570        580        590        600 
WQEKWKELGP VDLVLEGHDQ LRGWFFSLLR SGLILLDKAP YVSVLVHGFM LDEQGREMHK 

       610        620        630        640        650        660 
SLGNYVEPSV VIQRYGRDIL RLWLLRNTTW EDARFSWRAL ELTKRDLQII WNTYVFASMY 

       670        680        690        700        710        720 
MNLDNFEPVK YTLDDVIKYA KIEDLWILSR FNSMLKKVNE SMKNYKVHEM ANYLINFLVE 

       730        740        750        760        770        780 
DVSRFYIRLI RKRAWIEANT QDKIAMYYIL YFILKQWIIL ASTIIPFISE KIYKSFVVNP 

       790        800        810        820        830        840 
KESVSMESSI NYDERFIDNE LERAFEVARE INEASLNARA KAGIKLRWPL AKVYIFVEDE 

       850        860        870        880        890        900 
DTLAKVNRIK DVLLSLLNAK DIEISKIEGF KSFSKYKVEP NRSIIGKEYK SMSPKILDYI 

       910        920        930        940        950        960 
RNNSDIIAID ILNKKQHVAR IDNVDVILNT SHVIISEETI EGYVSSKFAQ GIVVISKEIS 

       970        980        990       1000       1010       1020 
ESEEEEGLVR DIIRRIQFMR KQLKLNVVDY IEISIKAPEE RVKTIQKWEE FIKSETRGNK 

      1030       1040 
VILGDPKGDI VMDWDIEGES YIIGIKKST 

« Hide

References

[1]"Biogeography of the Sulfolobus islandicus pan-genome."
Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.
Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M.16.27.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001401 Genomic DNA. Translation: ACP55350.1.
RefSeqYP_002843395.1. NC_012632.1.

3D structure databases

ProteinModelPortalC3N5S5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING427318.M1627_1468.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP55350; ACP55350; M1627_1468.
GeneID7814234.
KEGGsim:M1627_1468.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAKPVHWCL.

Enzyme and pathway databases

BioCycSISL427318:GH3D-1523-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
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.
IPR023585. Ile-tRNA-ligase_type1.
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]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
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_SULIA
AccessionPrimary (citable) accession number: C3N5S5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: May 14, 2014
This is version 37 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