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Q64U07 (SYI_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:BF2275
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length1141 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 – 11411141Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098520

Regions

Motif50 – 6011"HIGH" region HAMAP-Rule MF_02003
Motif689 – 6935"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6921ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64U07 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: B5BAF18AEA5AF9C4

FASTA1,141130,126
        10         20         30         40         50         60 
MSKKFAEYSQ FDLSKVNKDV LKKWDENQVF AKSMTEREGC PSFVFFEGPP SANGMPGIHH 

        70         80         90        100        110        120 
VMARSIKDIF CRYKTMKGYQ VKRKAGWDTH GLPVELGVEK SLGITKEDIG KTISVAEYNA 

       130        140        150        160        170        180 
HCRQDVMKFT KEWEDLTHKM GYWVDMKHPY ITYDNRYIET LWWLLKQLYK KGLLYKGYTI 

       190        200        210        220        230        240 
QPYSPAAGTG LSSHELNQPG CYRDVKDTTV VAQFKMKNPK PEMAQWGTPY FLAWTTTPWT 

       250        260        270        280        290        300 
LPSNTALCVG PKIDYVAVQS YNAYTGQPIT VVLAKALLNA HFNPKAAELK LEDYKAGDKL 

       310        320        330        340        350        360 
VPFKVIAEYK GPDLVGMEYE QLIPWVNPGE GAFRVILGDY VTTEDGTGIV HIAPTFGADD 

       370        380        390        400        410        420 
AQVAKAAGIP PLQLVNKKGE LRPMVDLTGK FYTLDELDED FIKQRVNIDL YKEYAGRFVK 

       430        440        450        460        470        480 
NAYDPNLSDQ DESLDVSICM MMKVNNQAFK IEKHVHNYPH CWRTDKPVLY YPLDSWFIRS 

       490        500        510        520        530        540 
TACKERMIEL NKTINWKPES TGTGRFGKWL ENLNDWNLSR SRYWGTPLPI WRTEDNSDEK 

       550        560        570        580        590        600 
CIESVEELYN EIEKSVAAGY MQSNPYKDKG FVPGEYNEEN YNKIDLHRPY VDDIILVSKD 

       610        620        630        640        650        660 
GKPMKREADL IDVWFDSGAM PYAQIHYPFE NKELLDSHQV YPADFIAEGV DQTRGWFFTL 

       670        680        690        700        710        720 
HAIATMVFDS VSYKAVISNG LVLDKNGNKM SKRLGNAVDP FSTIEQYGSD PLRWYMITNS 

       730        740        750        760        770        780 
SPWDNLKFDV DGIEEVRRKF FGTLYNTYSF FALYANVDGF EYKEADLPMN ERPEIDRWIL 

       790        800        810        820        830        840 
SVLNTLVKEV DTCYNEYEPT KAGRLISDFV NDNLSNWYVR LNRKRFWGGG FTQDKLSAYQ 

       850        860        870        880        890        900 
TLYTCLETVA KLMAPIAPFY ADRLYSDLIG VTGRDNVVSV HLAKFPEYNE KMVDKELEAQ 

       910        920        930        940        950        960 
MQMAQDVTSM VLALRRKVNI KVRQPLQCIM IPVVDEVQKA HIEAVKALIM SEVNVKEIKF 

       970        980        990       1000       1010       1020 
VDGAAGVLVK KVKCDFKKLG PKFGKQMKAV AAAVAEMSQE AIAELEKNGK YTFDLGGAEA 

      1030       1040       1050       1060       1070       1080 
VIESADVEIF SEDIPGWLVA NEGKLTVALE VTVTDELRRE GIARELVNRI QNIRKSSGFE 

      1090       1100       1110       1120       1130       1140 
ITDKIKLTLS KNPQTDDAVN EYNSYICNQV LGTSLTLADE VKDGTELNFD DFSLFVNVVK 


E 

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References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD49022.1.
RefSeqYP_099556.1. NC_006347.1.

3D structure databases

ProteinModelPortalQ64U07.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295405.BF2275.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD49022; BAD49022; BF2275.
GeneID3084057.
KEGGbfr:BF2275.
PATRIC21050193. VBIBacFra17906_2207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
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_02003. Ile_tRNA_synth_type2.
InterProIPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
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]
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_BACFR
AccessionPrimary (citable) accession number: Q64U07
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 70 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