ID   LSM6_YEAS7              Reviewed;          86 AA.
AC   A6ZYX7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN   Name=LSM6; ORFNames=SCY_1265;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Component of LSm protein complexes, which are involved in RNA
CC       processing and may function in a chaperone-like manner, facilitating
CC       the efficient association of RNA processing factors with their
CC       substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is
CC       thought to be involved in mRNA degradation by activating the decapping
CC       step in the 5'-to-3' mRNA decay pathway. In association with PAT1,
CC       LSM1-LSM7 binds directly to RNAs near the 3'-end and prefers
CC       oligoadenylated RNAs over polyadenylated RNAs. Component of the nuclear
CC       LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs.
CC       LSM2-LSM8 associates with multiple snRNP complexes containing the U6
CC       snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6
CC       snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and
CC       plays a role in the biogenesis and stability of the U6 snRNP and U4/U6
CC       snRNP complexes. LSM2-LSM8 probably also is involved degradation of
CC       nuclear pre-mRNA by targeting them for decapping, and in processing of
CC       pre-tRNAs, pre-rRNAs and U3 snoRNA. Component of a nucleolar LSM2-LSM7
CC       complex, which associates with the precursor of the RNA component of
CC       RNase P (pre-P RNA) and with the small nucleolar RNA (snoRNA) snR5. It
CC       may play a role in the maturation of a subset of nucleolus-associated
CC       small RNAs (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex, which consists
CC       of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. LSM1-LSM7 associates
CC       with PAT1 and XRN1. Component of the heptameric LSM2-LSM8 complex,
CC       which consists of LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. The LSm
CC       subunits form a seven-membered ring structure with a doughnut shape (By
CC       similarity). Component of a LSM2-LSM7 complex, which consists of at
CC       least LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. It is not known whether
CC       another protein replaces the missing LSm to form a novel heptameric
CC       complex. Component of the spliceosome U4/U6-U5 tri-snRNP complex
CC       composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6,
CC       PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1,
CC       SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8,
CC       BRR2 and DIB1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC       {ECO:0000250}. Note=LSM1 and LSM8 act competitively with respect to the
CC       localization of LSM1-LSM7 to the cytoplasm and LSM2-LSM8 to the
CC       nucleus. LSm proteins shift to the cytoplasm under conditions of stress
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFW02000145; EDN60707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZYX7; -.
DR   SMR; A6ZYX7; -.
DR   PRIDE; A6ZYX7; -.
DR   EnsemblFungi; EDN60707; EDN60707; SCY_1265.
DR   HOGENOM; CLU_076902_7_1_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0120114; C:Sm-like protein family complex; IEA:UniProt.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR016487; Lsm6/sSmF.
DR   InterPro; IPR001163; LSM_dom_euk/arc.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   PANTHER; PTHR11021; PTHR11021; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Ribonucleoprotein;
KW   RNA-binding; rRNA processing; Spliceosome; tRNA processing.
FT   CHAIN           1..86
FT                   /note="U6 snRNA-associated Sm-like protein LSm6"
FT                   /id="PRO_0000333607"
SQ   SEQUENCE   86 AA;  9398 MW;  74FE40A4509CEF33 CRC64;
     MSGKASTEGS VTTEFLSDII GKTVNVKLAS GLLYSGRLES IDGFMNVALS SATEHYESNN
     NKLLNKFNSD VFLRGTQVMY ISEQKI