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P84178

- SY1_PHYPO

UniProt

P84178 - SY1_PHYPO

Protein

Putative isoleucine--tRNA ligase

Gene
N/A
Organism
Physarum polycephalum (Slime mold)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. isoleucine-tRNA ligase activity Source: UniProtKB-EC

    GO - Biological processi

    1. translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative isoleucine--tRNA ligase (EC:6.1.1.5)
    Alternative name(s):
    Isoleucyl-tRNA synthetase
    Short name:
    IleRS
    OrganismiPhysarum polycephalum (Slime mold)
    Taxonomic identifieri5791 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaMyxogastriaMyxogastromycetidaePhysariidaPhysaraceaePhysarum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›64›64Putative isoleucine--tRNA ligasePRO_0000098606Add
    BLAST

    Interactioni

    Subunit structurei

    Member of a complex that includes annexin.1 Publication

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the class-I aminoacyl-tRNA synthetase family.Sequence Analysis

    Sequencei

    Sequence statusi: Fragments.

    P84178-1 [UniParc]FASTAAdd to Basket

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    LSGVRVTDLH AGVNPGDPVE VFYAVKYTPL FNYFLKVMPY STVLTTSLIN   50
    ILYXDNVALA FXXI 64
    Length:64
    Mass (Da):7,116
    Last modified:April 26, 2005 - v1
    Checksum:iD4FEA4CFEB8C7ECE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 111 Publication
    Non-adjacent residuesi10 – 1121 Publication
    Non-adjacent residuesi25 – 2621 Publication
    Non-adjacent residuesi36 – 3721 Publication
    Non-adjacent residuesi47 – 4821 Publication
    Non-adjacent residuesi56 – 5721 Publication
    Non-terminal residuei64 – 6411 Publication

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Class-specific binding of two aminoacyl-tRNA synthetases to annexin, a Ca2+- and phospholipid-binding protein."
      Shirakawa T., Nakamura A., Kohama K., Hirakata M., Ogihara S.
      Cell Struct. Funct. 29:159-164(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, SUBUNIT.

    Entry informationi

    Entry nameiSY1_PHYPO
    AccessioniPrimary (citable) accession number: P84178
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 22 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Caution

    The order of the peptides shown is unknown.1 Publication

    Keywords - Technical termi

    Direct protein sequencing

    Documents

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

    External Data

    Dasty 3