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)

B4F2T5

- SYI_PROMH

UniProt

B4F2T5 - SYI_PROMH

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Proteus mirabilis (strain HI4320)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (23 Sep 2008)
      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 bindingi899 – 8991ZincUniRule annotation
    Metal bindingi902 – 9021ZincUniRule annotation
    Metal bindingi919 – 9191ZincUniRule annotation
    Metal bindingi922 – 9221ZincUniRule 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

    BioCyciPMIR529507:GJIW-15-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:PMI0015
    OrganismiProteus mirabilis (strain HI4320)
    Taxonomic identifieri529507 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus
    ProteomesiUP000008319: 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 – 936936Isoleucine--tRNA ligasePRO_1000189187Add
    BLAST

    Proteomic databases

    PRIDEiB4F2T5.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi529507.PMI0015.

    Structurei

    3D structure databases

    ProteinModelPortaliB4F2T5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi58 – 6811"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.
    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.

    B4F2T5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDYKNTLNL PETGFPMRGD LAKREPEMLS RWYKEGLYQA IRQAKSGKKT    50
    FILHDGPPYA NGNIHIGHSV NKILKDIIIK SKGLSGFDSP YIPGWDCHGL 100
    PIELKVEQIV GKPGEKVSAA QFREECRKYA YEQIEAQKKD FIRLGVLGDW 150
    DKPYLTMDYK TEANTIRALA RIIANGHLLK GAKPVHWCTA CGSSLAEAEV 200
    EYYDKTSPSI DVRFRAVDSN AVAAKFGVVT DKPISLVIWT TTPWTLPANR 250
    AIALNGEFNY ALVSFDDECV ILAADLVEHV MKRIGVTDWA VLGECKGSDL 300
    ELLRFNHPFM GFDVPAILGD HVTLDAGTGA VHTAPGHGPD DFVIGQKYGL 350
    EVANPVGPNG CYLPNTYPTL DGVFVFKAND VIVELLKEKG ALLHHEAMQH 400
    SYPCCWRHKT PVIFRATPQW FIGMDKNGLR QQSLKEIKGV KWIPDWGQAR 450
    IESMVENRPD WCISRQRTWG TPMSLFVHKE TQEPHPRTLE LMEEVAKRVE 500
    VSGIQAWWDL DIRELLGDEA DDYMKTPDTL DVWFDSGSTH STVVDARPEF 550
    HGNSADLYLE GSDQHRGWFM SSLMISTAIK GKAPYREVLT HGFTVDGQGR 600
    KMSKSIGNTV SPQDVMNKLG ADILRLWVAS TDYTGEIAVS DEILKRSADT 650
    YRRIRNTARF FLANLNGFDP AKHQVKPEEM VILDRWAVGR AKAAQEDILK 700
    HYENYDFHNV IQRLMQFCSV EMGSFYLDII KDRQYTAKSD SVARRSCQTA 750
    LYHIIEALVR WMAPIMSFTA DEIWAQLPGE RAKFVFTQEW YTDLFGLEAS 800
    ETLNDEYWAE LLAVRSEVNK VLEQARTDKQ LRGSLEAAVT LYADKALAEK 850
    LNALGNELRF VLLTSQATVA DIHDAPENAL ASDMAGLKIV LSKAQGEKCP 900
    RCWHYATDIG QVAEHADLCG RCVTNVAGNG EERKFA 936
    Length:936
    Mass (Da):105,191
    Last modified:September 23, 2008 - v1
    Checksum:iC93002D82AF46097
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM942759 Genomic DNA. Translation: CAR40255.1.
    RefSeqiYP_002149802.1. NC_010554.1.

    Genome annotation databases

    EnsemblBacteriaiCAR40255; CAR40255; PMI0015.
    GeneIDi6802405.
    KEGGipmr:PMI0015.
    PATRICi20514707. VBIProMir120933_0015.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM942759 Genomic DNA. Translation: CAR40255.1 .
    RefSeqi YP_002149802.1. NC_010554.1.

    3D structure databases

    ProteinModelPortali B4F2T5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 529507.PMI0015.

    Proteomic databases

    PRIDEi B4F2T5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAR40255 ; CAR40255 ; PMI0015 .
    GeneIDi 6802405.
    KEGGi pmr:PMI0015.
    PATRICi 20514707. VBIProMir120933_0015.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PMIR529507:GJIW-15-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: HI4320.

    Entry informationi

    Entry nameiSYI_PROMH
    AccessioniPrimary (citable) accession number: B4F2T5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 48 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