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Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Borrelia duttonii (strain Ly)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).UniRule annotation

Cofactori

Zn2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei597ATPUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase
Biological processProtein biosynthesis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Isoleucine--tRNA ligaseUniRule annotation (EC:6.1.1.5UniRule annotation)
Alternative name(s):
Isoleucyl-tRNA synthetaseUniRule annotation
Short name:
IleRSUniRule annotation
Gene namesi
Name:ileSUniRule annotation
Ordered Locus Names:BDU_846
OrganismiBorrelia duttonii (strain Ly)
Taxonomic identifieri412419 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorrelia
Proteomesi
  • UP000000611 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002162491 – 1044Isoleucine--tRNA ligaseAdd BLAST1044

Proteomic databases

PRIDEiB5RN32

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi412419.BDU_846

Structurei

3D structure databases

ProteinModelPortaliB5RN32
SMRiB5RN32
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi48 – 58"HIGH" regionAdd BLAST11
Motifi594 – 598"KMSKS" region5

Domaini

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)).UniRule annotation

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C07 Bacteria
COG0060 LUCA
HOGENOMiHOG000246403
KOiK01870
OMAiHLGTAWN
OrthoDBiPOG091H028I

Family and domain databases

CDDicd07961 Anticodon_Ia_Ile_ABEc, 1 hit
Gene3Di3.40.50.620, 2 hits
3.90.740.10, 1 hit
HAMAPiMF_02003 Ile_tRNA_synth_type2, 1 hit
InterProiView protein in InterPro
IPR002300 aa-tRNA-synth_Ia
IPR033709 Anticodon_Ile_ABEc
IPR002301 Ile-tRNA-ligase
IPR023586 Ile-tRNA-ligase_type2
IPR013155 M/V/L/I-tRNA-synth_anticd-bd
IPR014729 Rossmann-like_a/b/a_fold
IPR009080 tRNAsynth_Ia_anticodon-bd
IPR009008 Val/Leu/Ile-tRNA-synth_edit
PfamiView protein in Pfam
PF08264 Anticodon_1, 1 hit
PF00133 tRNA-synt_1, 1 hit
PRINTSiPR00984 TRNASYNTHILE
SUPFAMiSSF47323 SSF47323, 1 hit
SSF50677 SSF50677, 1 hit
TIGRFAMsiTIGR00392 ileS, 1 hit

Sequencei

Sequence statusi: Complete.

B5RN32-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKKVENKVH FPQLEEKILQ FWNDNKIFEK SMKQREGCEE FTFYDGPPFA
60 70 80 90 100
TGLPHFGHFV PNTIKDIIPR YQTMKGKHVK RYFGWDTHGL PVEYEVEKSL
110 120 130 140 150
KLSGRYEIEQ YGIDKFNEEC RNIVLRYTKE WKKIITRLGR WVDFENNYKT
160 170 180 190 200
MDLTFMESVW WVFKTLYNKG LIYESYYVLP YSPKLATPLS NFEVNLGEYK
210 220 230 240 250
EIHDPSLTIK FKIKDKNEYL LAWTTTPWTL PTNLGIAVGK DIDYSKVLDQ
260 270 280 290 300
EKNEIYIIGT KRLNHYYQDE NKYVIIEQFK GEHLKGIEYE PLFDYFVNQR
310 320 330 340 350
NKGAFKIHTA EYVTTDDGTG IVHIAPFGEE DYQILKKNTQ TDMITPIDAE
360 370 380 390 400
CKFTSEVKDF EGLFVKDADN KIIEKLKSMN LLFKRENYLH RYPFCYRTNS
410 420 430 440 450
PLIYRPISSW FVNIEKIKEK LIRSNEQINW IPEHLKKGRF GKWLENARDW
460 470 480 490 500
AISRNRFWGN PIPIWKCSKT GNKICIGSRE ELEKLSGQKI IDLHKDKIDK
510 520 530 540 550
ITWPSKYGGT YVRTSEVLDC WFESGSMPYA SKHYPFKDKD KFQNIFPADF
560 570 580 590 600
IAEGLDQTRG WFYTLTILGT ALFEKTAFKN VIVNGLVLSS DGKKMSKSLK
610 620 630 640 650
NYTDPIQIIN TFGADALRLY LIMSPVIKAD DLKYSDDGVK DVLKNIIIPI
660 670 680 690 700
WNAYSFFITY AIIDKFTPNN HVNLYKTNIL DKWIISEIES LKQILNEEID
710 720 730 740 750
KYNLTKSIDV LLTFIDKLNN WYIRRSRRRF WKSENDNDKT DAYETLYYTL
760 770 780 790 800
KNLMLMLAPF IPFLTEEIYQ NLKTKNEKES IHLNDYPQSI KELINIELEE
810 820 830 840 850
KMNFTRKVIT IARALRASHN IKIRKPIKTI YIITKNHKEQ NTLREMTEII
860 870 880 890 900
LEEINAKEIK IKSNEEELVT YKAKANFKEL GSKLGTNMKS VALAITKLSN
910 920 930 940 950
EDILEIINGN KHTITINNNT YDITLKDIIL ERHERKNLKV INEDSITIGL
960 970 980 990 1000
DTLITEELYL EGLSRELIRK VQNLRKESNF NVTDRIILYT NNDEILTKII
1010 1020 1030 1040
NNFENYIKTE TLAITIEINN KKALKTLELD EEISVNIGIE KCLN
Length:1,044
Mass (Da):122,965
Last modified:November 4, 2008 - v1
Checksum:i96679F4DE629A8E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000976 Genomic DNA Translation: ACH93768.1
RefSeqiWP_012538573.1, NC_011229.1

Genome annotation databases

EnsemblBacteriaiACH93768; ACH93768; BDU_846
KEGGibdu:BDU_846

Similar proteinsi

Entry informationi

Entry nameiSYI_BORDL
AccessioniPrimary (citable) accession number: B5RN32
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: November 4, 2008
Last modified: March 28, 2018
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
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Main funding by: National Institutes of Health