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Reviewed, UniProtKB/Swiss-Prot Q5LCU8 (SYI_BACFN)

Last modified November 3, 2009. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Isoleucyl-tRNA synthetase
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase
      Short name=IleRS
Gene names
Name: ileS
Ordered Locus Names: BF2367
OrganismBacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]
Taxonomic identifier272559 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length1141 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02003

Cofactor

Zinc By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11411141Isoleucyl-tRNA synthetase HAMAP MF_02003
PRO_0000098521

Regions

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

Sites

Binding site6921ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LCU8-1 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: C01F15AE981C9BB5

FASTA1,141130,111
        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 FIKQRVNVDL 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

Cross-references

Sequence databases

CR626927 Genomic DNA. Translation: CAH08065.1.
RefSeqYP_211991.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5LCU8.

Genome annotation databases

GeneID3289145.
GenomeReviewsGene locus BF2367 in contig CR626927_GR.
KEGGbfs:BF2367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5LCU8.
OMASNWYVRR.

Enzyme and pathway databases

BioCycBFRA272559:BF2367-MON.

Family and domain databases

HAMAPMF_02003.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-synt_Ia.
IPR015905. Ile-tRNA-synt_Ia_N.
IPR018353. Isoleucyl-tRNA_synthetase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_BACFN
AccessionPrimary (citable) accession number: Q5LCU8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 21, 2005
Last modified: November 3, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents