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    Pfam ID: DUF1916 PDB: 1ufz_A
    Solved by: RSGI Priority Score: 3.6
    Member of this family is in PDB.
    Co-occurence with annotated domain(s) (no restrictions on number of architectures).
      # sequence matches: 73 # architectures: 6 # taxonomy ids:45
      Top FFAS hit in PDB: "1ufzA, Hypothetical protein BAB28515" No significant hits in Pfam.
      Top significant hit (PDB90): "1ufzA, translation ; solution structure of hbs1-like domain in hypothetical protein bab28515 "
      Publications(s) found: 69
      Publications(s) meeting filtering criteria: 9
    GeneSilico Metaserver: (Login and password: Jamboree)
    FFAS: PDB: 1ufz_A SCOP: a.5.9.1
    PRC: PDB: 1ufz_A SCOP: a.5.9.1
    SPARKS: PDB: 1ufz_A SCOP: a.5.9.1
    HHBLITS: PDB: 1ufz_A SCOP: a.5.9.1
    COMPASS: PDB: 1ufz_A SCOP: a.5.9.1
    COMA: PDB: 1ufz_A SCOP: a.5.9.1
    HHSEARCH: PDB: 1ufz_A SCOP: a.5.9.1

    Topsan Members

    Tag pages as 'PF08938' to appear in this list.

    No TOPSAN member(s) found.


    A recent manuscript by Becker and co-workers [Ref]  allows assignment of a probable function for members of the DUF1916 family (PF08938).  A structure representing this DUF1916 family has been deposited in the PDB (PDB ID 1ufz) , and the structure represents the N-terminal domain of an HBS1-like protein from Mus musculus. Hbs1 in eukaryotes is related to eukaryoytic release factor-3 (eRF3) and belongs to the eEF1A-like GTPases. Hbs1-like proteins contain an N-terminal DUF1916 domain, an Elongation Factor Tu GTP binding domain, an Elongation Factor Tu Domain 2, and an Elongation Factor Tu C-Terminal Domain. Hbs 1 is involved in No Go Decay (NGD), a process in eukaryotic cells during translation in which abberant mRNA is recognized and degraded.  In addition to Hbs1, another protein Dom34 is involved in NGD, and a Hbs1:Dom34 protein-protein complex recognizes the the stalled mRNA-ribosomal complex. Becker and co-workers in the report cited above used cryo-EM to visualize the NGD intermediates resulting from binding of Hbs1:Dom34 to stalled ribosomes. During that investigation, the sequence similarity of Hbs residues 20-84 to that corresponding to the NMR structure of a DUF1916 protein (PDB ID 1ufz described above) was used to construct a homology model that fit the observed EM electron density. In addition to the Hbs1 DUF1916 domain, all other domains of Hbs1 except the first 19 residues and the flexible linker (residues 85-159) between the DUF1916 domain and the EF Tu-GTP binding domain. In the complex structure, the DUF1916 domain of Hbs1 bridges rRNA h16 and rpS3 at the mRNA entry site.

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