ID   LSM6_SCLS1              Reviewed;          85 AA.
AC   A7F5M4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN   Name=lsm6; ORFNames=SS1G_12902;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
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=EDN98045.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476642; EDN98045.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001586324.1; XM_001586274.1.
DR   AlphaFoldDB; A7F5M4; -.
DR   SMR; A7F5M4; -.
DR   STRING; 665079.A7F5M4; -.
DR   GeneID; 5482289; -.
DR   KEGG; ssl:SS1G_12902; -.
DR   VEuPathDB; FungiDB:sscle_02g011990; -.
DR   InParanoid; A7F5M4; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
DR   GO; GO:0005688; C:U6 snRNP; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; rRNA processing; Spliceosome;
KW   tRNA processing.
FT   CHAIN           1..85
FT                   /note="U6 snRNA-associated Sm-like protein LSm6"
FT                   /id="PRO_0000333604"
SQ   SEQUENCE   85 AA;  9274 MW;  072720FD60316E80 CRC64;
     MENGALNQGE GKDPSSFLSD IIGSRVIVKL NNSLVFKGEL QSVDGYMNIA LEKCEEWVHG
     KKKTVHGDAF VRGNNVMYIS ADDSA