Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei569 – 5691Aminoacyl-adenylateUniRule annotation
Binding sitei613 – 6131ATPUniRule annotation
Metal bindingi894 – 8941ZincUniRule annotation
Metal bindingi897 – 8971ZincUniRule annotation
Metal bindingi909 – 9091ZincUniRule annotation
Metal bindingi912 – 9121ZincUniRule annotation

GO - Molecular functioni

  1. aminoacyl-tRNA editing activity Source: InterPro
  2. ATP binding Source: UniProtKB-HAMAP
  3. isoleucine-tRNA ligase activity Source: UniProtKB-HAMAP
  4. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. isoleucyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciCLAR306263:GH7X-1159-MONOMER.

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:Cla_1161
OrganismiCampylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
Taxonomic identifieri306263 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000007727: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 921921Isoleucine--tRNA ligasePRO_1000189141Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi306263.Cla_1161.

Structurei

3D structure databases

ProteinModelPortaliB9KD44.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi59 – 6911"HIGH" regionAdd
BLAST
Motifi610 – 6145"KMSKS" region

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 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0060.
HOGENOMiHOG000246402.
KOiK01870.
OMAiVLGDWDN.
OrthoDBiEOG644ZM1.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02002. Ile_tRNA_synth_type1.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSiPR00984. TRNASYNTHILE.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00392. ileS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B9KD44-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDYKDTLLLP NTTFAMRANL AELEPKRFDK WFENNYAYEK MKQKRQGVSE
60 70 80 90 100
SFTLHDGPPY ANGHLHIGHA LNKILKDIII KMHYFQGKKV RFTPGWDCHG
110 120 130 140 150
LPIEQQVEVK LKDKKQNLSK KQIRELCREH AREFVNIQRD EFKSLGVIAD
160 170 180 190 200
WDEPYLTMKN AFEADIYKAL CKIAKKGLLL ERSKPVFWSW AAKSALAEAE
210 220 230 240 250
VEYEEKEDYS IYVAFNLDEA SCKKLGVENA KAVIWTTTPW TLPANQAISL
260 270 280 290 300
NPNEKYIITK EGYIFAKALL ENMINKNFTQ GEIQKELLGS EFENLSAINP
310 320 330 340 350
LNQRKSTLIL GEHVLMDGGT GLVHTAPGHG EDDYYACLKY NIEVIMPVDD
360 370 380 390 400
GGYYDETLRA KGLLPEHLLA EFIGLHIFKA NERILELLGE ALLESSKFTH
410 420 430 440 450
SYPFCWRTHK PVIYRATKQW FILMDEKKLD GKSLRELALE QLNSVKFYPE
460 470 480 490 500
SGVKRLSSMI ENRPDWCISR QRDWGVPIAF FRDKKSQEVI FDDDVLDHLV
510 520 530 540 550
GIFEKNGADA WWDLEIKDLL PPNSKYNPNN LEKVYDILDV WFDSGSTWEA
560 570 580 590 600
VLNSARYDAG EYQASMYLEG SDQHRGWFQS SLLISTAINH KTPYKNILTH
610 620 630 640 650
GFTVDEKGQK MSKSKGNVVL PQNVAKNYGV EILRLWIMLS DYSTDLKISD
660 670 680 690 700
NILKQVSEQY RKIRNTIRFL LANTNDIEFV ETKNFTLLDK WILMRAKIAF
710 720 730 740 750
EICENAFEKY EFSKGFSVLL NFLSADLSGI YLDICKDRLY CNAKDDSKRV
760 770 780 790 800
SAQSAMVLIA RKLFALLAPS LTYTIDEALE HANVAIKENA KDVFDLLNKQ
810 820 830 840 850
GFEYEYKIED ELFIKSREKF FEIIDGLKKD KIIKSTLELS LQTSANELLS
860 870 880 890 900
EDLEEIADWF MVSVVESIDE QKALAEFKID NIGFKIVKSS LNKCPRCWKF
910 920
LAKEDGCLCP RCNGVEKAKN V
Length:921
Mass (Da):106,124
Last modified:March 24, 2009 - v1
Checksum:i16261B95FDBB0591
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000932 Genomic DNA. Translation: ACM64483.1.
RefSeqiYP_002575734.1. NC_012039.1.

Genome annotation databases

EnsemblBacteriaiACM64483; ACM64483; Cla_1161.
GeneIDi7410325.
KEGGicla:Cla_1161.
PATRICi20062809. VBICamLar15090_1149.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000932 Genomic DNA. Translation: ACM64483.1.
RefSeqiYP_002575734.1. NC_012039.1.

3D structure databases

ProteinModelPortaliB9KD44.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi306263.Cla_1161.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACM64483; ACM64483; Cla_1161.
GeneIDi7410325.
KEGGicla:Cla_1161.
PATRICi20062809. VBICamLar15090_1149.

Phylogenomic databases

eggNOGiCOG0060.
HOGENOMiHOG000246402.
KOiK01870.
OMAiVLGDWDN.
OrthoDBiEOG644ZM1.

Enzyme and pathway databases

BioCyciCLAR306263:GH7X-1159-MONOMER.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02002. Ile_tRNA_synth_type1.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSiPR00984. TRNASYNTHILE.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00392. ileS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete genome sequence and analysis of the human pathogen Campylobacter lari."
    Miller W.G., Wang G., Binnewies T.T., Parker C.T.
    Foodborne Pathog. Dis. 5:371-386(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RM2100 / D67 / ATCC BAA-1060.

Entry informationi

Entry nameiSYI_CAMLR
AccessioniPrimary (citable) accession number: B9KD44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: January 7, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.