Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A8F465

- SYI_THELT

UniProt

A8F465 - SYI_THELT

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Thermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / TMO)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (13 Nov 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 1 zinc ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei552 – 5521Aminoacyl-adenylateUniRule annotation
    Binding sitei596 – 5961ATPUniRule annotation
    Metal bindingi880 – 8801ZincUniRule annotation
    Metal bindingi883 – 8831ZincUniRule annotation
    Metal bindingi900 – 9001ZincUniRule annotation
    Metal bindingi903 – 9031ZincUniRule 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

    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

    BioCyciTLET416591:GI64-387-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:Tlet_0382
    OrganismiThermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / TMO)
    Taxonomic identifieri416591 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000002016: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 911911Isoleucine--tRNA ligasePRO_1000070892Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi416591.Tlet_0382.

    Structurei

    3D structure databases

    ProteinModelPortaliA8F465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi57 – 6711"HIGH" regionAdd
    BLAST
    Motifi593 – 5975"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.
    OMAiKPVHWCL.
    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.
    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.
    IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
    [Graphical view]
    PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 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.

    A8F465-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDYRSTLNLP GTEFSMRANL VEKEPRILEK WQKMNIYDYL LKHRENNPTF    50
    VLHDGPPYAN GDIHIGTAMN KILKDIVVRY KTLRGFKSPY VPGWDTHGLP 100
    IEHKVTTMLG EKARSMSQTE LRKACEEFAK QQIEMQKKQF QRLGVIGDWE 150
    NYYATLNPEY EYKIYEIFAK LVEDGYVYRA LKPVLWCNNC GTALAQAEIE 200
    YHDHDSPSIY VKFKMENSEN EYIIIWTTTP WTLPGNTGIA VHPDQQYVKI 250
    EVGSEIWILA EKLLKMAMQE IGIDEYRILE KFKGHFLEGK QAVHPIFDRK 300
    SRIITADFVD METGTGCVHI APGHGEEDYE FGHLVNGLAV ISPVDEKGYF 350
    TEEAGKYSGM HIEKANKQII EDLKNNGSLL KESTIKHSYP HCWRCKKPVI 400
    FRATEQWFIS VEKNNLRQRV LENIQNVAWI PAWGKNRISA MVEERPDWCI 450
    SRQRAWGTPI PAFRCSKCSE VVLDARLIRH FAEIVKKMGT NAWFELSEKQ 500
    LLPDGYVCPH CGSEDLVKMN DTLDVWIDSG SSFEAVLTTR PELTFPADMY 550
    LEGSDQHRGW FNSSLVLSVI THDKPPYKTV LTHGFIKDAE GKKMSKSLGN 600
    VVDPLEVCSK YGADVLRLWL ASSDYFNDIR ISKNIIFQQV EVYKKIRNTI 650
    RYLLGNLQDF SVTDSIGFQK MLPVDRWALG RLQQIIKSVT EAYESYEFSK 700
    AYNILVKYCS VELSAIYLDI VKDRLYVEGK HSLKRRSAQT VLYNILKSLL 750
    VMFSPILAFT CEEAYEFLNF GEKKYQTVMA ENWPEYKEEY IDTNLMNDFE 800
    ELLQLRDLVL KALEESRQNG LIGHSLDAKV AIKTGSKKTL DLLKKYSAYL 850
    EEFFIVSKVE ICNSDENLHI EVEHAEGEKC ERCWKYDPLT NSDSEFPNIC 900
    PRCMAVLKEK R 911
    Length:911
    Mass (Da):105,342
    Last modified:November 13, 2007 - v1
    Checksum:iB50424733D43F09B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000812 Genomic DNA. Translation: ABV32949.1.
    RefSeqiYP_001470013.1. NC_009828.1.

    Genome annotation databases

    EnsemblBacteriaiABV32949; ABV32949; Tlet_0382.
    GeneIDi5608531.
    KEGGitle:Tlet_0382.
    PATRICi23931275. VBITheLet125395_0407.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000812 Genomic DNA. Translation: ABV32949.1 .
    RefSeqi YP_001470013.1. NC_009828.1.

    3D structure databases

    ProteinModelPortali A8F465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 416591.Tlet_0382.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV32949 ; ABV32949 ; Tlet_0382 .
    GeneIDi 5608531.
    KEGGi tle:Tlet_0382.
    PATRICi 23931275. VBITheLet125395_0407.

    Phylogenomic databases

    eggNOGi COG0060.
    HOGENOMi HOG000246402.
    KOi K01870.
    OMAi KPVHWCL.
    OrthoDBi EOG644ZM1.

    Enzyme and pathway databases

    BioCyci TLET416591:GI64-387-MONOMER.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPi MF_02002. Ile_tRNA_synth_type1.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023585. Ile-tRNA-ligase_type1.
    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.
    IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
    [Graphical view ]
    PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
    Pfami PF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view ]
    PRINTSi PR00984. TRNASYNTHILE.
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsi TIGR00392. ileS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-301 / DSM 14385 / TMO.

    Entry informationi

    Entry nameiSYI_THELT
    AccessioniPrimary (citable) accession number: A8F465
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 50 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