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A6QB84 (SYI_SULNB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:SUN_1796
OrganismSulfurovum sp. (strain NBC37-1) [Complete proteome] [HAMAP]
Taxonomic identifier387093 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaSulfurovum

Protein attributes

Sequence length918 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 – 918918Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022134

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif609 – 6135"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8941Zinc By similarity
Metal binding8971Zinc By similarity
Metal binding9091Zinc By similarity
Metal binding9121Zinc By similarity
Binding site5681Aminoacyl-adenylate By similarity
Binding site6121ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6QB84 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: C36014E919AD2338

FASTA918103,033
        10         20         30         40         50         60 
MDFKETLLLP KTDFPMRGNL PANEPKKYKT WFDTNIYEQM KAKREGAELF TLHDGPPYAN 

        70         80         90        100        110        120 
GDIHIGHALN KILKDIILKY NYFQGKAVRM TPGWDCHGLP IEQKVEEKLG KSKKEAMPTE 

       130        140        150        160        170        180 
KFRELCRAHA GKFVDIQRDE FKSLGVVADW ENPYVTMDFK FEANIYRTLC EVAKRGLLVE 

       190        200        210        220        230        240 
RHKPIFWSWA ARTALADAEV EYEDKEDYSI YVHFELSDAA KEKLGLEGKA GLVIWTTTPW 

       250        260        270        280        290        300 
TLPANTGISI NPDEMYVLTD DGHIVADARY DAMIEEGVVA GHASRKIAAT ELDGLLAINP 

       310        320        330        340        350        360 
LNERPSKVVL GEHVMMDGGT GCVHTAPGHG EDDYKVGLEN GLEVVMPVDE RGCYDESVVG 

       370        380        390        400        410        420 
LDLLPDAEKF VGMHIFKANE PILELLGDNL LKVSKFTHSY PHCWRTKKPL IYRATNQWFI 

       430        440        450        460        470        480 
SIDDAAKGSD KTLREAAVDA IDSVDFYPAS SKNRLKPMVE GRPDWCISRQ RSWGVPIAFF 

       490        500        510        520        530        540 
RVKSTKAVIF DEDVLEHVAS LFDEHGADAW YSMSIAELLP AGSKYDPADL EKIEDILDVW 

       550        560        570        580        590        600 
FDSGSTWNSV LSSGNYDAGN YPASLYLEGS DQHRGWFQSS LLLSSAINGI APYETIITHG 

       610        620        630        640        650        660 
FTMDAKGEKM SKSKGNVVAP EKVVKQFGSE ILRLWVALSD YQNDQKISDD ILKQTAEQYR 

       670        680        690        700        710        720 
KIRNTFRFLL ANVNDLDALV SADAYGELDR WILNKADDVF ASVKESFETY DFLKGFATLN 

       730        740        750        760        770        780 
HFITNELSGI YMDVTKDRLY CEAKDSDVRR ATQSAMALIS KAMLGLIAPV LTYTADEILA 

       790        800        810        820        830        840 
YAPAIFKGDI ENVFDLVYEA VPETAASFDD AILLEAREKF SEAIDSLKKE KVIKATLELE 

       850        860        870        880        890        900 
IAGDRDLLPI SDDKDLEDWF VVSAVKESSK GEQVASFKVE GRTFTVHKAM MAKCPRCWRF 

       910 
TSTSEDCLCE RCAKVVGA 

« Hide

References

[1]"Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBC37-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009179 Genomic DNA. Translation: BAF72743.1.
RefSeqYP_001359100.1. NC_009663.1.

3D structure databases

ProteinModelPortalA6QB84.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387093.SUN_1796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF72743; BAF72743; SUN_1796.
GeneID5363362.
KEGGsun:SUN_1796.
PATRIC23776607. VBISulSp49917_1824.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycSSP387093:GH25-1819-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_SULNB
AccessionPrimary (citable) accession number: A6QB84
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 53 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