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)

Q8PN19

- SYI_XANAC

UniProt

Q8PN19 - SYI_XANAC

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Xanthomonas axonopodis pv. citri (strain 306)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      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 sitei577 – 5771Aminoacyl-adenylateUniRule annotation
    Binding sitei621 – 6211ATPUniRule annotation
    Metal bindingi906 – 9061ZincUniRule annotation
    Metal bindingi909 – 9091ZincUniRule annotation
    Metal bindingi926 – 9261ZincUniRule annotation
    Metal bindingi929 – 9291ZincUniRule 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

    BioCyciXAXO190486:GH55-1254-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:XAC1254
    OrganismiXanthomonas axonopodis pv. citri (strain 306)
    Taxonomic identifieri190486 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    ProteomesiUP000000576: 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 – 943943Isoleucine--tRNA ligasePRO_0000098504Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi190486.XAC1254.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8PN19.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi59 – 6911"HIGH" regionAdd
    BLAST
    Motifi618 – 6225"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.

    Q8PN19-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTQDYKATLH LPATEFPMRG DLPKREPAML ERWEREGFYA QLRANAAGRP    50
    LFVLHDGPPY ANGQIHLGHA VNKILKDIIV KSKYLAGFDA PYIPGWDCHG 100
    LPIEIAIEKK YGKVGVKLDA AEFRQKCREY ATEQIDLQRR DFKRLGVIGD 150
    WDNPYKTLDF RFEANEIRAL AKVVDNGHLT RGVKPVHWCF DCGSALAEAE 200
    IEYADKVSPT VDIAYPARDP AAVAAAFGAS LPAGVGVAVP IWTTTPWTLP 250
    ASLAVSLGAE LDYVLVEGPA DRGQPRWLVI AEALAAKALA RYGVGEVVVH 300
    GHAKGAALEH MLLNHPFYAE REIPLLLGDH VSAEDGTGAV HTAPGHGQED 350
    YQVSKQYGLL ERYGAAQINP VDGRGVYLPS TPPLRDTVLA GLHIWKANDV 400
    IIEALRETGV LLAASKMEHS YPHCWRHKTP IAFRATPQWF ISMEQANLRA 450
    DALKAIENVH WYPSWGQARI AGMVDGRPDW TISRQRTWGV PIALFVHRET 500
    GEPHPRSTEL LRQVADRVEQ GGVDVWYTLD ASELLSSEAA DYEKITDILD 550
    VWFDSGVTHE AVLPDRGLPK PADLYLEGSD QHRGWFQSSL LSGVAMDKAA 600
    PYKQCLTHGF TVDEHGRKMS KSLGNGIEPQ DIMKTLGADI LRLWIASADY 650
    SNEMSLSQEI LKRNADAYRR LRNTARFLLG NLHGFDPLQH LVALDEMVLL 700
    DRWIVHRAHE LQEKIVAAYA RYDFAEIVQA LLNFCSVDLG SLYLDVTKDR 750
    LYTMAEDARG RRSAQSAMYH VAEAFVRWIA PVLSFTAEEL WGYLPGKHVD 800
    NVLFATWYDG LAPLPADAAL SGADFDKLLV LREQVAKVLE PMRANGAIGA 850
    ALEAEITVAA DAQTAARWQP LAEELRFLFI SGDVTVTAAS TDDIFVSAQP 900
    TTKAKCVRCW HHQASVGSDP RHPELCSRCV SNIEGPGERR RWF 943
    Length:943
    Mass (Da):104,739
    Last modified:October 1, 2002 - v1
    Checksum:i401115611B1AD660
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008923 Genomic DNA. Translation: AAM36126.1.
    RefSeqiNP_641590.1. NC_003919.1.
    WP_011050802.1. NC_003919.1.

    Genome annotation databases

    EnsemblBacteriaiAAM36126; AAM36126; XAC1254.
    GeneIDi1155325.
    KEGGixac:XAC1254.
    PATRICi24054481. VBIXanAxo33670_1322.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008923 Genomic DNA. Translation: AAM36126.1 .
    RefSeqi NP_641590.1. NC_003919.1.
    WP_011050802.1. NC_003919.1.

    3D structure databases

    ProteinModelPortali Q8PN19.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 190486.XAC1254.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM36126 ; AAM36126 ; XAC1254 .
    GeneIDi 1155325.
    KEGGi xac:XAC1254.
    PATRICi 24054481. VBIXanAxo33670_1322.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci XAXO190486:GH55-1254-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. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
      da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
      , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
      Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 306.

    Entry informationi

    Entry nameiSYI_XANAC
    AccessioniPrimary (citable) accession number: Q8PN19
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 82 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

    Documents

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

    External Data

    Dasty 3