ID   LSM6_BOTFB              Reviewed;          85 AA.
AC   A6S5C9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN   Name=lsm6; ORFNames=BC1G_08321;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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. Component of the nuclear LSM2-
CC       LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8
CC       associates with multiple snRNP complexes containing the U6 snRNA (U4/U6
CC       di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds
CC       directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the
CC       biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes.
CC       LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by
CC       targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs
CC       and U3 snoRNA (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. Component of the
CC       heptameric LSM2-LSM8 complex, which consists of lsm2, lsm3, lsm4, lsm5,
CC       lsm6, lsm7 and lsm8. The LSm subunits form a seven-membered ring
CC       structure with a doughnut shape (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN28054.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH476886; EDN28054.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001553597.1; XM_001553547.1.
DR   AlphaFoldDB; A6S5C9; -.
DR   SMR; A6S5C9; -.
DR   VEuPathDB; FungiDB:Bcin01g09480; -.
DR   OrthoDB; 1627235at2759; -.
DR   GO; GO:1990726; C:Lsm1-7-Pat1 complex; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0000932; C:P-body; IEA:EnsemblFungi.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IEA:EnsemblFungi.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IEA:EnsemblFungi.
DR   GO; GO:0005688; C:U6 snRNP; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:EnsemblFungi.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IEA:EnsemblFungi.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:EnsemblFungi.
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..85
FT                   /note="U6 snRNA-associated Sm-like protein LSm6"
FT                   /id="PRO_0000333590"
SQ   SEQUENCE   85 AA;  9289 MW;  FCD0EA41A899C622 CRC64;
     MENGALQQGE GKDPSSFLSE IIGSKVIVKL NNSLVFKGEL QSVDGYMNIA LEKCEEWVHG
     KKKTVHGDAF VRGNNVMYIS ADESA