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    cysS cysteine--tRNA ligase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946969, updated on 3-Dec-2024

    Summary

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    Official Symbol
    cysS
    Official Full Name
    cysteine--tRNA ligase
    Primary source
    ECOCYC:EG10196
    Locus tag
    b0526
    See related
    ASAP:ABE-0001810
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK0519; syc
    Summary
    Cysteinyl-tRNA synthetase (CysRS) is a member of the family of aminoacyl-tRNA synthetases, which interpret the genetic code by covalently linking amino acids to their specific tRNA molecules. [More information is available at EcoCyc: EG10196].
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    Genomic context

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    Sequence:
    NC_000913.3 (554611..555996)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene UDP-2,3-diacylglucosamine diphosphatase Neighboring gene peptidyl-prolyl cis-trans isomerase B Neighboring gene PF04307 family inner membrane protein YbcI Neighboring gene putative RNA-binding protein YbcJ

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Cysteinyl-tRNA formation: the last puzzle of aminoacyl-tRNA synthesis. Li T, et al. FEBS Lett, 1999 Dec 3. PMID 10622715
    2. Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions. Fersht AR, et al. Biochemistry, 1979 Apr 3. PMID 371674
    3. Temperature-sensitive mutants in cysteinyl-tRNA ligase of E. coli K-12. Bohman K, et al. Mol Gen Genet, 1979 Oct 2. PMID 396450
    4. The anticodon and discriminator base are major determinants of cysteine tRNA identity in vivo. Pallanck L, et al. J Biol Chem, 1992 Apr 15. PMID 1373131
    5. Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase. Hou YM, et al. Proc Natl Acad Sci U S A, 1991 Feb 1. PMID 1992490, Free PMC Article

    See all (32) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on complete protein
      Title: Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure.
    2. cysteinyl-tRNA synthetase recognizes RNA in a shape specific manner
      Title: Shape-selective RNA recognition by cysteinyl-tRNA synthetase.
    3. Long-range covalent continuity between the active site domain at the N-terminus of cysteine tRNA synthetase and the cysteinyl-tRNA-binding anticodon domain at the enzyme C-terminus is required for efficient tRNA aminoacylaton.
      Title: Domain-domain communication for tRNA aminoacylation: the importance of covalent connectivity.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables ATP binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables aminoacyl-tRNA ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables aminoacyl-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables cysteine-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables cysteine-tRNA ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables cysteine-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cysteinyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within cysteinyl-tRNA aminoacylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in cysteinyl-tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA aminoacylation for protein translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    cysteine--tRNA ligase
    NP_415059.1

    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. NC_000913.3 Reference assembly

      Range
      554611..555996
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415059.1 cysteine--tRNA ligase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415059.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2W6Q295
      Conserved Domains (1) summary
      PRK00260
      Location:1 → 461
      cysS; cysteinyl-tRNA synthetase; Validated
    Nucleotide Protein
    Heading Accession and Version

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