LSM6_SCHPO
ID LSM6_SCHPO Reviewed; 75 AA.
AC Q9UUI1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm6;
GN Name=lsm6; ORFNames=SPAC2F3.17c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
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DR EMBL; CU329670; CAB54975.1; -; Genomic_DNA.
DR PIR; T38534; T38534.
DR RefSeq; NP_594380.1; NM_001019801.2.
DR PDB; 3SWN; X-ray; 2.50 A; B/E/Q/T=1-75.
DR PDB; 4EMK; X-ray; 2.30 A; B=1-75.
DR PDB; 6PPN; X-ray; 1.91 A; F/N=1-75.
DR PDB; 6PPP; X-ray; 2.33 A; F/N=1-75.
DR PDB; 6PPQ; X-ray; 1.81 A; F=1-75.
DR PDB; 6PPV; X-ray; 2.05 A; F=1-75.
DR PDBsum; 3SWN; -.
DR PDBsum; 4EMK; -.
DR PDBsum; 6PPN; -.
DR PDBsum; 6PPP; -.
DR PDBsum; 6PPQ; -.
DR PDBsum; 6PPV; -.
DR AlphaFoldDB; Q9UUI1; -.
DR SMR; Q9UUI1; -.
DR BioGRID; 278481; 2.
DR STRING; 4896.SPAC2F3.17c.1; -.
DR MaxQB; Q9UUI1; -.
DR PaxDb; Q9UUI1; -.
DR EnsemblFungi; SPAC2F3.17c.1; SPAC2F3.17c.1:pep; SPAC2F3.17c.
DR GeneID; 2541997; -.
DR KEGG; spo:SPAC2F3.17c; -.
DR PomBase; SPAC2F3.17c; lsm6.
DR VEuPathDB; FungiDB:SPAC2F3.17c; -.
DR eggNOG; KOG1783; Eukaryota.
DR HOGENOM; CLU_076902_7_4_1; -.
DR InParanoid; Q9UUI1; -.
DR OMA; KMRRSYG; -.
DR PhylomeDB; Q9UUI1; -.
DR Reactome; R-SPO-430039; mRNA decay by 5' to 3' exoribonuclease.
DR EvolutionaryTrace; Q9UUI1; -.
DR PRO; PR:Q9UUI1; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0120115; C:Lsm2-8 complex; TAS:PomBase.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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:0005697; C:telomerase holoenzyme complex; TAS:PomBase.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:PomBase.
DR GO; GO:0005688; C:U6 snRNP; ISO:PomBase.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISO:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISO:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; TAS:PomBase.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding; rRNA processing;
KW Spliceosome; tRNA processing.
FT CHAIN 1..75
FT /note="U6 snRNA-associated Sm-like protein LSm6"
FT /id="PRO_0000125577"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:6PPQ"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:6PPQ"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:6PPQ"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:6PPQ"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:6PPQ"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:6PPQ"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6PPQ"
SQ SEQUENCE 75 AA; 8336 MW; 20B1B1F2E380BCCF CRC64;
MDSSPNEFLN KVIGKKVLIR LSSGVDYKGI LSCLDGYMNL ALERTEEYVN GKKTNVYGDA
FIRGNNVLYV SALDD
