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P46207

- SYI_AQUPY

UniProt

P46207 - SYI_AQUPY

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Aquifex pyrophilus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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) By similarity.By similarity

    Catalytic activityi

    ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei482 – 4821Aminoacyl-adenylateBy similarity
    Binding sitei526 – 5261ATPBy similarity

    GO - Molecular functioni

    1. aminoacyl-tRNA editing activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. isoleucine-tRNA ligase activity Source: UniProtKB-EC

    GO - Biological processi

    1. isoleucyl-tRNA aminoacylation Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoleucine--tRNA ligase (EC:6.1.1.5)
    Alternative name(s):
    Isoleucyl-tRNA synthetase
    Short name:
    IleRS
    Gene namesi
    Name:ileS
    OrganismiAquifex pyrophilus
    Taxonomic identifieri2714 [NCBI]
    Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›529›529Isoleucine--tRNA ligasePRO_0000098342Add
    BLAST

    Proteomic databases

    PRIDEiP46207.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP46207.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi523 – 5275"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)) By similarity.By similarity

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    InterProiIPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023585. Ile-tRNA-ligase_type1.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009008. Val/Leu/Ile-tRNA-synth_edit.
    [Graphical view]
    PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
    PfamiPF00133. tRNA-synt_1. 1 hit.
    [Graphical view]
    PRINTSiPR00984. TRNASYNTHILE.
    SUPFAMiSSF50677. SSF50677. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    P46207-1 [UniParc]FASTAAdd to Basket

    « Hide

    DTHGLPIERA VEKELSKKKI RKESLPKTEF RKLCREYANR YVNIQKEEFI    50
    RLGVLGDWEN PYLTMSPEYE ATEIRELGKF FEKGLAYRSK KPVYWCIYDK 100
    TAEGQAEVEY YEKEDPSIYV KFPLKKEIEG KKAYAVIWTT TPWTLPANLG 150
    IMVKEDADYS LVEVEGEVWI VAKELLENFF KNIGKTYTRV LKDVKGRDLV 200
    GLEYEHPFVD RDELKGYLSE ETLKNMWRIY PSEFVSLDTG TGLVHMAPGH 250
    GQEDYTVGKR YNLEPYAPLD DSGRFVEPAP EFIRGVRVFD ANKLIIALLK 300
    EKGYLVHEAR IRHSYPHCWR CKNPVIFRAT PQWFIGMDIE YEGKTLSGES 350
    LEEIEKVKWI PEYGKNRIKS MVENRPDWCI SRQRFWGVPI TVFYCENCGE 400
    VIKDKEVFER IASLVEKHPG GTDVWFEKSP EEILPEGYKC PKCGGTSFRK 450
    EEDILDVWFD SGCSHASVIR PLGFEKADLY LEGSDQHRGW FQASLLESVG 500
    SYGEAPYRSV LTHGFIVDEQ GRKMSKSLV 529
    Length:529
    Mass (Da):61,379
    Last modified:November 1, 1995 - v1
    Checksum:iFB6C40D69E26DDD8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei529 – 5291

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L37096 Genomic DNA. Translation: AAA87287.1.
    PIRiI39658.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L37096 Genomic DNA. Translation: AAA87287.1 .
    PIRi I39658.

    3D structure databases

    ProteinModelPortali P46207.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P46207.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    InterProi IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023585. Ile-tRNA-ligase_type1.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009008. Val/Leu/Ile-tRNA-synth_edit.
    [Graphical view ]
    PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
    Pfami PF00133. tRNA-synt_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00984. TRNASYNTHILE.
    SUPFAMi SSF50677. SSF50677. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications."
      Brown J.R., Doolittle W.F.
      Proc. Natl. Acad. Sci. U.S.A. 92:2441-2445(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiSYI_AQUPY
    AccessioniPrimary (citable) accession number: P46207
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 80 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3