InterPro : IPR027141

Name  U6 snRNA-associated Sm-like protein LSm4/Small nuclear ribonucleoprotein Sm D1/D3 Short Name  LSm4/Sm_D1/D3
Type  Family Description  This entry includes U6 snRNA-associated Sm-like protein LSm4 and small nuclear ribonucleoproteins Sm D1 and D3.LSm4 is a component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. It binds specifically to the 3'-terminal U-tract of U6 snRNA [, ]. Sm D1 is involved in pre-mRNA splicing. It binds snRNA U1, U2, U4 and U5, which contain a highly conserved structural motif called the Sm binding site. It also binds telomerase RNA and is required for its accumulation [, ].Sm D3 appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. It binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner [].
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Proteins

InterPro protein domain ID --> Contigs

 

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5 Publications

First Author Title Year Journal Volume Pages
Pillai RS Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein. 2001 EMBO J 20 5470-9
Bouveret E A Sm-like protein complex that participates in mRNA degradation. 2000 EMBO J 19 1661-71
Kufel J Lsm proteins are required for normal processing of pre-tRNAs and their efficient association with La-homologous protein Lhp1p. 2002 Mol Cell Biol 22 5248-56
Rymond BC Convergent transcripts of the yeast PRP38-SMD1 locus encode two essential splicing factors, including the D1 core polypeptide of small nuclear ribonucleoprotein particles. 1993 Proc Natl Acad Sci U S A 90 848-52
Seto AG Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle. 1999 Nature 401 177-80



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)