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    RHA1 rhamnogalacturonan acetylesterase [ Aspergillus chevalieri ]

    Gene ID: 66978943, updated on 31-Oct-2024

    Summary

    Gene symbol
    RHA1
    Gene description
    rhamnogalacturonan acetylesterase
    Locus tag
    ACHE_20042S
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Aspergillus chevalieri (strain: M1)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus
    Orthologs
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    Genomic context

    See RHA1 in Genome Data Viewer
    Location:
    chromosome: 2
    Exon count:
    2
    Sequence:
    Chromosome: 2; NC_057363.1 (101097..101901)

    Chromosome 2 - NC_057363.1Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene bifunctional acetohydroxyacid reductoisomerase

    General protein information

    Preferred Names
    rhamnogalacturonan acetylesterase
    XP_043133106.1
    • CAZy:CE12;
      COG:V;
      EggNog:ENOG410PNVV;
      InterPro:IPR013830,IPR036514;
      PFAM:PF00657,PF13472;
      SECRETED:SignalP(1-16)

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_057363.1 Reference assembly

      Range
      101097..101901
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_043284301.1XP_043133106.1  rhamnogalacturonan acetylesterase [Aspergillus chevalieri]

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A7R7VH73
      Conserved Domains (1) summary
      cl01053
      Location:18229
      SGNH_hydrolase; or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical ...