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    Rv3220c two component sensor kinase [ Mycobacterium tuberculosis H37Rv ]

    Gene ID: 888801, updated on 6-Oct-2023

    Summary

    Gene symbol
    Rv3220c
    Gene description
    two component sensor kinase
    Locus tag
    Rv3220c
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Mycobacterium tuberculosis H37Rv (strain: H37Rv, type-material: type strain of Mycobacterium tuberculosis)
    Lineage
    Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex
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    Genomic context

    Sequence:
    NC_000962.3 (3596029..3597534, complement)

    NC_000962.3Genomic Context describing neighboring genes Neighboring gene hypothetical protein Neighboring gene transcriptional regulator WhiB1 Neighboring gene acetyl-CoA carboxylase biotin carboxyl carrier protein subunit Neighboring gene anti-sigma factor RshA Neighboring gene hypothetical protein

    General protein information

    Preferred Names
    two component sensor kinase

    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_000962.3 Reference assembly

      Range
      3596029..3597534 complement
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      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_217736.1 two component sensor kinase [Mycobacterium tuberculosis H37Rv]

      See identical proteins and their annotated locations for NP_217736.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      R4LZF4
      Conserved Domains (3) summary
      COG3920
      Location:274498
      COG3920; Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms]
      pfam12282
      Location:9150
      H_kinase_N; Signal transduction histidine kinase
      cl21578
      Location:177291
      PAS; PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in ...