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    SNM1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852089, updated on 11-Sep-2024

    Summary

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    Official Symbol
    SNM1
    Primary source
    SGD:S000002886
    Locus tag
    YDR478W
    See related
    AllianceGenome:SGD:S000002886; FungiDB:YDR478W; VEuPathDB:YDR478W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables rRNA primary transcript binding activity. Involved in mRNA processing; plasmid partitioning; and rRNA processing. Part of ribonuclease MRP complex. [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    Location:
    chromosome: IV
    Exon count:
    1
    Sequence:
    Chromosome: IV; NC_001136.10 (1414575..1415171)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene AMP-activated serine/threonine-protein kinase catalytic subunit SNF1 Neighboring gene Pex29p Neighboring gene Dig2p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001136.10

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Mutagenesis of SNM1, which encodes a protein component of the yeast RNase MRP, reveals a role for this ribonucleoprotein endoribonuclease in plasmid segregation. Cai T, et al. Mol Cell Biol, 1999 Nov. PMID 10523674, Free PMC Article
    2. Characterization of a unique protein component of yeast RNase MRP: an RNA-binding protein with a zinc-cluster domain. Schmitt ME, et al. Genes Dev, 1994 Nov 1. PMID 7958920
    3. A specialized processing body that is temporally and asymmetrically regulated during the cell cycle in Saccharomyces cerevisiae. Gill T, et al. J Cell Biol, 2006 Apr 10. PMID 16585272, Free PMC Article
    4. The Saccharomyces cerevisiae RNase mitochondrial RNA processing is critical for cell cycle progression at the end of mitosis. Cai T, et al. Genetics, 2002 Jul. PMID 12136008, Free PMC Article
    5. Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP. Perederina A, et al. Nat Commun, 2020 Jul 10. PMID 32651392, Free PMC Article

    See all (34) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables RNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nuclease activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables rRNA primary transcript binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in RNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in mRNA processing IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in plasmid partitioning IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in rRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in rRNA processing IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in rRNA processing IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tRNA processing IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    part_of endoribonuclease complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of nucleolar ribonuclease P complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of ribonuclease MRP complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    part_of ribonucleoprotein complex IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    Snm1p
    NP_010766.3
    • Ribonuclease MRP complex subunit; ribonuclease (RNase) MRP cleaves pre-rRNA and has a role in cell cycle-regulated degradation of daughter cell-specific mRNAs; binds to the NME1 RNA subunit of RNase MRP

    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_001136.10 Reference assembly

      Range
      1414575..1415171
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180786.3 → NP_010766.3  TPA: Snm1p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010766.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VTA1, P40993, Q6B1P4
      UniProtKB/TrEMBL
      B3LFI8, B5VH06, C7GKR7, C8Z636, G2WBK7, N1P7L6
      Conserved Domains (1) summary
      pfam04032
      Location:18 → 109
      Rpr2; RNAse P Rpr2/Rpp21/SNM1 subunit domain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P40993.1

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