(data stored in ACNUC7421 zone)

SWISSPROT: LSM6_ASHGO

ID   LSM6_ASHGO              Reviewed;          85 AA.
AC   Q75BR7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 93.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN   Name=LSM6; OrderedLocusNames=ACR204C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
DR   EMBL; AE016816; AAS51430.1; -; Genomic_DNA.
DR   RefSeq; NP_983606.1; NM_208959.1.
DR   SMR; Q75BR7; -.
DR   STRING; 33169.AAS51430; -.
DR   EnsemblFungi; AAS51430; AAS51430; AGOS_ACR204C.
DR   GeneID; 4619738; -.
DR   KEGG; ago:AGOS_ACR204C; -.
DR   HOGENOM; HOG000223542; -.
DR   InParanoid; Q75BR7; -.
DR   KO; K12625; -.
DR   OMA; TQVMYIS; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:1990726; C:Lsm1-7-Pat1 complex; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0005732; C:small nucleolar 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;
DR   PRODOM; Q75BR7.
DR   SWISS-2DPAGE; Q75BR7.
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_0000333587"
SQ   SEQUENCE   85 AA;  9382 MW;  78EA3233158C3AB6 CRC64;
     MSSAMQGPAV TSSSTFLSNI IGKPVNVKLH SGMLYQGTLE SIDGFMNVAL VDASEYYESE
     QNPVIHRYES DVFLRGTQVM YISEL
//

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