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Q8A9K9 (SYI_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:BT_0806
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length1162 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
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 – 11621162Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098522

Regions

Motif50 – 6011"HIGH" region HAMAP-Rule MF_02003
Motif710 – 7145"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site7131ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8A9K9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: B6CEFE096695451B

FASTA1,162132,494
        10         20         30         40         50         60 
MGKRFTEYSQ FDLSQVNKDV LKKWDENQVF AKSMTERDGC PSFVFFEGPP SANGMPGIHH 

        70         80         90        100        110        120 
VMARTIKDIF CRYKTMKGYQ VKRKAGWDTH GLPVELSVEK ALGITKEDIG KKISVADYNA 

       130        140        150        160        170        180 
ACRKDVMKYT KEWEDLTHQM GYWVDMKHPY ITYDNRYIET LWWLLKQLHK KGLLYKGYTI 

       190        200        210        220        230        240 
QPYSPAAGTG LSSHELNQPG CYRDVKDTTA VAQFKMKNPK PEMAEWGTPY FLAWTTTPWT 

       250        260        270        280        290        300 
LPSNTALCVG PKIDYVAVQT YNAYTGEPIT VVLAKALLNT HFNSKAADLK LEDYKAGDKL 

       310        320        330        340        350        360 
VPFKVVAEYK GADLIGMEYE QLIPWVKPVE VSEDGTWKVS GKGFRVIPGD YVTTEDGTGI 

       370        380        390        400        410        420 
VHIAPTFGAD DANVARAAGI PSLFMINKKG ETRPMVDLTG KFYMLDELDE NFVKECVDVD 

       430        440        450        460        470        480 
KYKEYQGAWV KNAYNPVFMV DGKYDEKAAQ AAESLDVALC MMMKANNQAF KIEKHIHNYP 

       490        500        510        520        530        540 
HCWRTDKPVL YYPLDSWFIR STACKERMME LNKTINWKPE STGTGRFGKW LENLNDWNLS 

       550        560        570        580        590        600 
RSRYWGTPLP IWRTEDGTSE ICIESVEELY NEIEKSVAAG FMKSNPYKDK GFVPGEYTEG 

       610        620        630        640        650        660 
NYDKIDLHRP YVDDIILVSE DGQPMKRESD LIDVWFDSGA MPYAQIHYPF ENKNILDNRE 

       670        680        690        700        710        720 
VYPADFIAEG VDQTRGWFFT LHAIATMVFD SVSYKAVISN GLVLDKNGNK MSKRLNNAVD 

       730        740        750        760        770        780 
PFTTIEKYGS DPLRWYMITN SSPWDNLKFD IDGIEEVRRK FFGTLYNTYS FFALYANVDG 

       790        800        810        820        830        840 
FEYKEADVPM AERPEIDRWI LSVLNTLIKE VDTCYNEYEP TKAGRLISDF VNDNLSNWYV 

       850        860        870        880        890        900 
RLNRKRFWGG EFTQDKLSAY QTLYTCLETV AKLMAPISPF YADRLYTDLT TATGRDNVVS 

       910        920        930        940        950        960 
IHLAEFPKYQ EEMIDKELEA RMQMAQDVTS MVLALRRKVN IKVRQPLQCI MIPVADEEQK 

       970        980        990       1000       1010       1020 
AHIEAVKALI MNEVNVKDIK FVDGAAGVLV KKVKCDFKKL GPKFGKQMKA VAAAVAEMSQ 

      1030       1040       1050       1060       1070       1080 
EAIAELEKNG KYALNLDGAE AVIEAADVEI FSEDIPGWLV ANEGKLTVAL EVTVTEELRR 

      1090       1100       1110       1120       1130       1140 
EGIARELVNR IQNIRKSSGF EITDKIKITI SKNTQTDDAV NEYNTYICNQ VLGTSLDLAD 

      1150       1160 
EVKDGTELNF DDFSLFVNVI KD 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015928 Genomic DNA. Translation: AAO75913.1.
RefSeqNP_809719.1. NC_004663.1.

3D structure databases

ProteinModelPortalQ8A9K9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226186.BT_0806.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO75913; AAO75913; BT_0806.
GeneID1073871.
KEGGbth:BT_0806.
PATRIC21056409. VBIBacThe70966_0824.

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKWIISEI.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-815-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 2 hits.
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_BACTN
AccessionPrimary (citable) accession number: Q8A9K9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 76 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