ID   LSM6_PHANO              Reviewed;          89 AA.
AC   Q0UWI9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN   Name=LSM6; ORFNames=SNOG_03875;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(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. 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=EAT89080.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445329; EAT89080.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001794420.1; XM_001794368.1.
DR   AlphaFoldDB; Q0UWI9; -.
DR   SMR; Q0UWI9; -.
DR   STRING; 13684.SNOT_03875; -.
DR   GeneID; 5971283; -.
DR   KEGG; pno:SNOG_03875; -.
DR   eggNOG; KOG1783; Eukaryota.
DR   InParanoid; Q0UWI9; -.
DR   OrthoDB; 1627235at2759; -.
DR   Proteomes; UP000001055; 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..89
FT                   /note="U6 snRNA-associated Sm-like protein LSm6"
FT                   /id="PRO_0000333603"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   89 AA;  9420 MW;  6E1696B9885C4156 CRC64;
     MSTNGESPAP EGAGDSRDPS GFLSEIIGAP VTVKLNSGIV YKGDLQSVDG YMNIALERCK
     EVAEGRVIRN WGDAFVRGNN VTYISADNA