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)

Q7NS57

- SYI_CHRVO

UniProt

Q7NS57 - SYI_CHRVO

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      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 sitei560 – 5601Aminoacyl-adenylateUniRule annotation
    Binding sitei604 – 6041ATPUniRule annotation
    Metal bindingi888 – 8881ZincUniRule annotation
    Metal bindingi891 – 8911ZincUniRule annotation
    Metal bindingi908 – 9081ZincUniRule annotation
    Metal bindingi911 – 9111ZincUniRule 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

    BioCyciCVIO243365:GHUD-3664-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:CV_3569
    OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
    Taxonomic identifieri243365 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
    ProteomesiUP000001424: 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 – 925925Isoleucine--tRNA ligasePRO_0000098375Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243365.CV_3569.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7NS57.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi59 – 6911"HIGH" regionAdd
    BLAST
    Motifi601 – 6055"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.

    Q7NS57-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIDYRKTVN LLDTPFAMRG DLAKREPAWV KRWQEEKRYE KLRKLAAGRP    50
    KFILHDGPPY ANNDIHLGHA VNKVLKDIIV RSKTLAGFDA PYVPGWDCHG 100
    LPIELMVEKL HGKDIPAAKF RELCREYAKE QVARQKKGFI RLGVLGDWDN 150
    PYLTMDFKTE ADIVRTLGKI HENGYLTKGE KPVHWCIECG SSLAEAEVEY 200
    EDKVSPAIDV GFKVVDTDKA SAAFGADAAG AMAVIWTTTP WTLPANQAVA 250
    AGANLDYQLV DTPKGKLILG KDLVESAMKR YGVETYRVLG EAKGQALELL 300
    QLQHPFYGRQ VPVILGDHVT TDAGTGLVHT APAHGLEDFQ AGLQYKLPIA 350
    NPVADDGRYK STTELFAGML VWDANPRVIE TLESHGSLVH KSKLEHSYPH 400
    CWRHKTPIIF RATPQWFISM DRKANGGETL REVSQRAVDA TEFFPSWGRA 450
    RLDAMIKNSP DWCVSRQRNW GVPMTFFIHK ESGELHPRSA QLLEEVALRI 500
    EQQGIEAWFS LDAKELLGEE AEQYRKLTDT LDVWFDSGAT HFAVLKQRPE 550
    LAWPADLYLE GSDQHRGWFQ SSLKTGCATI GRAPYKQLLT HGFTVDDKGY 600
    KMSKSKGNGI APEEICGTLG ADILRLWVAS ADYSGDMSLS QEILKRTTES 650
    YRRLRNTIRF LLSNLSDFDP LEHVVPLANM VEMDQYALLR AREVQEKVVG 700
    ELYSRYAFHH VVQEVVGYCS EDLGAFYLDV IKDRLYTTKA DSHARRSAQT 750
    ALYHITRSLL LMVAPILCFT ADEAWNVLVD SEEESTLYHI WHEFPAQTVE 800
    REAALSSKWQ AIRELRAAVN KEIEALRSAD KLGSSLQAEV EIDAPAELAR 850
    HLASLGEELK FVLIVSKADV REAGEVAIRV SPSAHGKCDR CWHYRADVGS 900
    HAGHGAVCGR CVDNLDGQGE PRRYA 925
    Length:925
    Mass (Da):103,787
    Last modified:December 15, 2003 - v1
    Checksum:iE26FBAADD12CB49A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016825 Genomic DNA. Translation: AAQ61231.1.
    RefSeqiNP_903239.1. NC_005085.1.

    Genome annotation databases

    EnsemblBacteriaiAAQ61231; AAQ61231; CV_3569.
    GeneIDi2549895.
    KEGGicvi:CV_3569.
    PATRICi21441957. VBIChrVio67196_3494.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016825 Genomic DNA. Translation: AAQ61231.1 .
    RefSeqi NP_903239.1. NC_005085.1.

    3D structure databases

    ProteinModelPortali Q7NS57.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243365.CV_3569.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAQ61231 ; AAQ61231 ; CV_3569 .
    GeneIDi 2549895.
    KEGGi cvi:CV_3569.
    PATRICi 21441957. VBIChrVio67196_3494.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CVIO243365:GHUD-3664-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. "The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
      Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A.
      , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
      Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

    Entry informationi

    Entry nameiSYI_CHRVO
    AccessioniPrimary (citable) accession number: Q7NS57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 79 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