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Q30SH2 (SYI_SULDN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. 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:Suden_0780
OrganismSulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)) [Complete proteome] [HAMAP]
Taxonomic identifier326298 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeSulfurimonas

Protein attributes

Sequence length919 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 – 919919Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022139

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif610 – 6145"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8951Zinc By similarity
Metal binding8981Zinc By similarity
Metal binding9101Zinc By similarity
Metal binding9131Zinc By similarity
Binding site5691Aminoacyl-adenylate By similarity
Binding site6131ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30SH2 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 10250E6BCF51E029

FASTA919104,455
        10         20         30         40         50         60 
MDYKDTLLLP TTKFEMRGNL INNEPIRYAS WDEKKIYEKM KKNRKNAQSF TLHDGPPYAN 

        70         80         90        100        110        120 
GHTHIGHALN KILKDIIVKH NYFSGKSVRF TPGWDCHGLP IEQQVEKKLG GKQKKELLEK 

       130        140        150        160        170        180 
AKIRELCRAH AAEFVDIQRE EFKKLGVIAD WENPYVTMDF KFEANIYRTL CNVAKKGLLI 

       190        200        210        220        230        240 
ERSKPVFWSW AERTALAEAE VEYEDKEDYS IFIAFELSDE AKAKLSINSK AALVIWTTTP 

       250        260        270        280        290        300 
WTIPANTGIS LNPEEEYILT TTGYIVAKKL LSSLNESKIL SGDIAQTFKA KEFENLLALN 

       310        320        330        340        350        360 
PLNGRTSRIV LGEHVLVENG TGCVHTAPGH GEDDYRIGLV YDLEVVMPVD ETGCYDETIV 

       370        380        390        400        410        420 
RDGLIPNAED FLGRHIFKSN EDLITLMGES VVHVSKFKHS YPHCWRSHTP LIFRATKQWF 

       430        440        450        460        470        480 
ISVDEKPSGS DKTLRDIALS EVEKTLFFPE TGRNRLKSMV ANRPDWCISR QRDWGVPIAF 

       490        500        510        520        530        540 
FRVKATGEVL LDEKVLNFTA MVFEMHGSDA WYSMPTEQLL YPGAGYSADE LEKVTDILDV 

       550        560        570        580        590        600 
WFDSGSTWYS VLKSRNYDAG EFQADLYVEG SDQHRGWFQS SMFLSAAVEH KAPYKGVLTH 

       610        620        630        640        650        660 
GFTVDEKGEK MSKSKGNVVA PETVLKEYGS EILRLWVASS DYQGDLKISQ SILKQSAENY 

       670        680        690        700        710        720 
RKLRNTFRIM LANINDLHAL TPYEKMGELD KWILNEAKSV FDGVHKSFSN YNFVNGMSLL 

       730        740        750        760        770        780 
NNFIVNELSG IYIDITKDSL YCDAKDDARR TSSQSAMALI VKSLLTLIAP ILTYTADEIV 

       790        800        810        820        830        840 
EYLPEVIRES KEDIFDFVHK NIDVAESGFN TDYMYAAREK FYEIVDGLKK EKIIKNTLEL 

       850        860        870        880        890        900 
VIVTESKKIA EMDKTAAEDW FVVSGISHSE VIAELGKFEV DGSIFVIQKA TAAKCPRCWK 

       910 
YQAKDETATC TRCSKVLNA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000153 Genomic DNA. Translation: ABB44059.1.
RefSeqYP_393294.1. NC_007575.1.

3D structure databases

ProteinModelPortalQ30SH2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326298.Suden_0780.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB44059; ABB44059; Suden_0780.
GeneID3764306.
KEGGtdn:Suden_0780.
PATRIC23770118. VBISulDen68967_0807.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSDEN326298:GH9P-814-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.
InterProIPR002300. 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.
ProtoNetSearch...

Entry information

Entry nameSYI_SULDN
AccessionPrimary (citable) accession number: Q30SH2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 65 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