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I6I72_RS13185 trypsin-like serine protease [ Corynebacterium striatum ]

Gene ID: 72412956, updated on 10-Dec-2024

Summary

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Gene symbol
I6I72_RS13185
Gene description
trypsin-like serine protease
Locus tag
I6I72_RS13185
Gene type
protein coding
Organism
Corynebacterium striatum (strain: FDAARGOS_1115, culture-collection: DSM:7184)
Lineage
Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; Corynebacteriaceae; Corynebacterium
Old locus tag
I6I72_13185
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Genomic context

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NZ_CP068158.1Genomic Context describing neighboring genes Neighboring gene NYN domain-containing protein Neighboring gene hypothetical protein Neighboring gene DUF6891 domain-containing protein Neighboring gene hypothetical protein

Genomic regions, transcripts, and products

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Genomic Sequence:
NZ_CP068158.1

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis. Sprang S, et al. Science, 1987 Aug 21. PMID 3112942
  2. Families of serine peptidases. Rawlings ND, et al. Methods Enzymol, 1994. PMID 7845208, Free PMC Article

GeneRIFs: Gene References Into Functions

General gene information

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Homology

General protein information

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Preferred Names
trypsin-like serine protease
WP_034656866.1

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. NZ_CP068158.1 Reference assembly

    Range
    2822675..2822899 complement
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    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. WP_034656866.1 MULTISPECIES: trypsin-like serine protease [Corynebacterium]

    UniProtKB/TrEMBL
    A0AAN5KKQ7
    Conserved Domains (1) summary
    cl21584
    Location:36 → 56
    Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...
Nucleotide Protein
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Molecular Biology Databases