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Q8RH47 (SYI_FUSNN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. 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:FN0067
OrganismFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131) [Reference proteome] [HAMAP]
Taxonomic identifier190304 [NCBI]
Taxonomic lineageBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium

Protein attributes

Sequence length933 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
Reference 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 – 933933Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098389

Regions

Motif60 – 7011"HIGH" region HAMAP-Rule MF_02002
Motif606 – 6105"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9061Zinc By similarity
Metal binding9091Zinc By similarity
Metal binding9251Zinc By similarity
Metal binding9281Zinc By similarity
Binding site5651Aminoacyl-adenylate By similarity
Binding site6091ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8RH47 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 10058192B01AEECA

FASTA933107,496
        10         20         30         40         50         60 
MSDKEYTSTL HLPKTDFQMK ANLPNKEPKY IKKWTEEKIY EKGLEKNKNG ETFILHDGPP 

        70         80         90        100        110        120 
YANGNTHIGH ALNKILKDII LKYKTFRGFR SPYVPGWDTH GLPIELQVVK EVGVGKAREM 

       130        140        150        160        170        180 
SALEIRKLCE KYAKKWVGIQ KEQFIRLGVL GDWDNPYLTL DPRFEAKQLE LFGEIYVNGY 

       190        200        210        220        230        240 
IFKGLKPVYW SPATETALAE AEIEYYDHVS PSIYVRMQAN KDLLDKIGFN EDVYVLIWTT 

       250        260        270        280        290        300 
TPWTLPANVA ICLNENFDYG LYKTEKGNLI LAKDLAESAF KDIGIENFEL IKEFKGKDLE 

       310        320        330        340        350        360 
YTTYKHPFLE RTGLIILGDH VTADAGTGAV HTAPGHGQDD YVVGLAYKLP VISPIDHRGC 

       370        380        390        400        410        420 
LTEEAGDLFK GLVYSEANKA IIKHLTETGH ILKMQEISHS YPHDWRSKTP VIFRATEQWF 

       430        440        450        460        470        480 
IRMEGGDLRE KTLKVIDKIN FIPSWGKNRI GSMMETRPDW CISRQRVWGV PIPIFYNDET 

       490        500        510        520        530        540 
NEEIFHKEIL DRICDLVREH GSNIWVEKSP EELIGEELLV KYNLKGLKLR KETNIMDVWF 

       550        560        570        580        590        600 
DSGSSHRGVL EVWEGLHRPC DLYLEGSDQH RGWFHTSLLT SVASTGDSPY KSVLTHGFVN 

       610        620        630        640        650        660 
DGEGKKMSKS LGNTVSPEDV IKVYGADILR LWCGSVDYRD DVRISDNIVK QMSEAYRRIR 

       670        680        690        700        710        720 
NTARYILGNS YDFNPKTDKV AYKDMLEIDK WALNKLEVLK RSVTESYDKY EFYNLFQGIH 

       730        740        750        760        770        780 
YFAAIDMSAF YLDIIKDRLY TEKKDSVARR AAQTVMYEVL MTLTKMVAPI LSFTAEEIWE 

       790        800        810        820        830        840 
SLPAETRESE SIFLADWYVN NDEYLKPELD EKWQQIIKLR KEVNKKLEKA RQGENKIIGN 

       850        860        870        880        890        900 
SLDAKVSLYT EDNTLKEFIK ENLELLKIVF IVSDLEVVDS ADGNYTDAEE IEKLKIKIAH 

       910        920        930 
ADGEKCERCW KYDELGTDSE HPTLCPRCAA VLK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009951 Genomic DNA. Translation: AAL94280.1.
RefSeqNP_602981.1. NC_003454.1.

3D structure databases

ProteinModelPortalQ8RH47.
SMRQ8RH47. Positions 5-933.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190304.FN0067.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL94280; AAL94280; FN0067.
GeneID992969.
KEGGfnu:FN0067.
PATRIC21949919. VBIFusNuc122357_0659.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

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.
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.
ProtoNetSearch...

Entry information

Entry nameSYI_FUSNN
AccessionPrimary (citable) accession number: Q8RH47
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 81 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