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)

B9L8Z9

- SYI_NAUPA

UniProt

B9L8Z9 - SYI_NAUPA

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (24 Mar 2009)
      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 sitei564 – 5641Aminoacyl-adenylateUniRule annotation
    Binding sitei608 – 6081ATPUniRule annotation
    Metal bindingi887 – 8871ZincUniRule annotation
    Metal bindingi890 – 8901ZincUniRule annotation
    Metal bindingi902 – 9021ZincUniRule annotation
    Metal bindingi905 – 9051ZincUniRule 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

    BioCyciNPRO598659:GH7N-694-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:NAMH_0696
    OrganismiNautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH)
    Taxonomic identifieri598659 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaNautilialesNautiliaceaeNautilia
    ProteomesiUP000000448: 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_1000189183Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi598659.NAMH_0696.

    Structurei

    3D structure databases

    ProteinModelPortaliB9L8Z9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi57 – 6711"HIGH" regionAdd
    BLAST
    Motifi605 – 6095"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.
    OMAiERLMLHQ.
    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.

    B9L8Z9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDYKDTLLLP KTTFPMRGNL PQNEPKKYKK WFSEHVYERM KQNRVGNDKF    50
    NLHDGPPYAN GHIHIGHALN KILKDMIVKY YYFQGFDVRY TPGWDCHGLP 100
    IEQQVEKKIG REKKESLPKS KVRELCRQHA AKFIEIQKEE FQNLGVIGDW 150
    DNPYKTMDFE FEANIYKALA EIAKKGLLVE RSKPVFWCMH DKTALAEAEV 200
    EYEDKEDYSI YVAFPLSNEA KSKLGIDNAS IVIWTTTPWT LPANMGIALN 250
    PEEKYVLSED GKIVAKELYE NLKEAEVVSG EIVKEFDASE LENLKAINPL 300
    NGRESVIILG EHVTMDGGTG CVHTAPGHGE EDYRVWLKYG FSEILQPVDD 350
    EGKYSNLIVT EKLLPEEFKG MHIFEANPKI LDLLGDNLVK VSKFTHSYPH 400
    CWRCHNPVIF RATKQFFIAM DKEVNGDTLR HRALSEIEKV EFTPKTGKNR 450
    LSTMVANRPD WCISRQRDWG VPIAFFRNKD TGELIIDDEI IENVYEIFKV 500
    KGADAWYDLS IEELLPESKK EMASKLEKVN DILDVWFDSG STWFAVLKNG 550
    PYDAGEYPAN MYLEGSDQHR GWFQSSLLVS TSIEERAPYK SILTHGFTVD 600
    EKGEKMSKSK GNVVAPQEVS KKFGTEILRL WVATSDYSGD IKISDGILKQ 650
    VAEQYRKIRN TIRFLLANVN DLEEIKLTNP SMIDRWILAR SKEVFDEVVA 700
    LFGKYDFSKA FNILNNFIVT ELSAIYMDVC KDRLYCEPLN SEKRRNSQST 750
    MAVIVKELIS LLAPVLTYTM DEAVEHAPKV IKEDAKDVFD FVYTPLTAVE 800
    NPIDEEILEI RRRFFEIVDR LKKEKVIKDT LELAIETNYD KLLVDEMADF 850
    FVVSLISDNI EGETLDEFHI SDEQFVVKIK RSPLHKCPRC WRYLAEEEGA 900
    LCERCEKAIN G 911
    Length:911
    Mass (Da):104,913
    Last modified:March 24, 2009 - v1
    Checksum:i2061D723A2AA6983
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001279 Genomic DNA. Translation: ACM92881.1.
    RefSeqiWP_015901933.1. NC_012115.1.
    YP_002607107.1. NC_012115.1.

    Genome annotation databases

    EnsemblBacteriaiACM92881; ACM92881; NAMH_0696.
    GeneIDi7504838.
    KEGGinam:NAMH_0696.
    PATRICi22676107. VBINauPro131435_0667.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001279 Genomic DNA. Translation: ACM92881.1 .
    RefSeqi WP_015901933.1. NC_012115.1.
    YP_002607107.1. NC_012115.1.

    3D structure databases

    ProteinModelPortali B9L8Z9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 598659.NAMH_0696.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACM92881 ; ACM92881 ; NAMH_0696 .
    GeneIDi 7504838.
    KEGGi nam:NAMH_0696.
    PATRICi 22676107. VBINauPro131435_0667.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci NPRO598659:GH7N-694-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. "Adaptations to submarine hydrothermal environments exemplified by the genome of Nautilia profundicola."
      Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K., Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.
      PLoS Genet. 5:E1000362-E1000362(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-1463 / DSM 18972 / AmH.

    Entry informationi

    Entry nameiSYI_NAUPA
    AccessioniPrimary (citable) accession number: B9L8Z9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 43 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