LSM6_KLULA
ID LSM6_KLULA Reviewed; 80 AA.
AC Q6CPS7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN Name=LSM6; OrderedLocusNames=KLLA0E02530g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 ---------------------------------------------------------------------------
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; CR382125; CAG99149.1; -; Genomic_DNA.
DR RefSeq; XP_454062.1; XM_454062.1.
DR AlphaFoldDB; Q6CPS7; -.
DR SMR; Q6CPS7; -.
DR STRING; 28985.XP_454062.1; -.
DR EnsemblFungi; CAG99149; CAG99149; KLLA0_E02575g.
DR GeneID; 2894269; -.
DR KEGG; kla:KLLA0_E02575g; -.
DR eggNOG; KOG1783; Eukaryota.
DR HOGENOM; CLU_076902_7_1_1; -.
DR InParanoid; Q6CPS7; -.
DR OMA; MYISEQK; -.
DR Proteomes; UP000000598; Chromosome E.
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; Reference proteome;
KW Ribonucleoprotein; RNA-binding; rRNA processing; Spliceosome;
KW tRNA processing.
FT CHAIN 1..80
FT /note="U6 snRNA-associated Sm-like protein LSm6"
FT /id="PRO_0000333597"
SQ SEQUENCE 80 AA; 8953 MW; 4CA75E15E4B07BDD CRC64;
MESKATASGS FLENIIGKPV YVKLFSGILY QGKLESIDGF MNVTMSQVSE HYEAEENGTL
HKYPSEVFLR GSQVLYISEK