ID   LSM3_YEAST              Reviewed;          89 AA.
AC   P57743; D6VZ73; Q05176; Q06759;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 1.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm3;
DE   AltName: Full=SmX4 protein;
GN   Name=LSM3; Synonyms=SMX4, USS2; OrderedLocusNames=YLR438C-A;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND FUNCTION.
RX   PubMed=7744014; DOI=10.1002/j.1460-2075.1995.tb07200.x;
RA   Seraphin B.;
RT   "Sm and Sm-like proteins belong to a large family: identification of
RT   proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs.";
RL   EMBO J. 14:2089-2099(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RC   STRAIN=07173;
RX   PubMed=7828914; DOI=10.1016/0378-1119(94)00633-4;
RA   Graack H.-R., Grohmann L., Kitakawa M., Goldschmidt-Reisin S.;
RT   "Gene MRP-L4, encoding mitochondrial ribosomal protein YmL4, is
RT   indispensable for proper non-respiratory cell functions in yeast.";
RL   Gene 152:107-112(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-89.
RX   PubMed=2824201; DOI=10.1111/j.1432-1033.1987.tb13597.x;
RA   Degols G.;
RT   "Functional analysis of the regulatory region adjacent to the cargB gene of
RT   Saccharomyces cerevisiae. Nucleotide sequence, gene fusion experiments and
RT   cis-dominant regulatory mutation analysis.";
RL   Eur. J. Biochem. 169:193-200(1987).
RN   [6]
RP   IDENTIFICATION IN THE LSM2-LSM8 COMPLEX, AND ASSOCIATION WITH PRE-P RNA.
RX   PubMed=10369684; DOI=10.1093/emboj/18.12.3451;
RA   Salgado-Garrido J., Bragado-Nilsson E., Kandels-Lewis S., Seraphin B.;
RT   "Sm and Sm-like proteins assemble in two related complexes of deep
RT   evolutionary origin.";
RL   EMBO J. 18:3451-3462(1999).
RN   [7]
RP   IDENTIFICATION, AND CHARACTERIZATION.
RX   PubMed=10428970; DOI=10.1093/emboj/18.15.4321;
RA   Mayes A.E., Verdone L., Legrain P., Beggs J.D.;
RT   "Characterization of Sm-like proteins in yeast and their association with
RT   U6 snRNA.";
RL   EMBO J. 18:4321-4331(1999).
RN   [8]
RP   SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA   Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA   Fabrizio P.;
RT   "Identification by mass spectrometry and functional analysis of novel
RT   proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL   EMBO J. 18:4535-4548(1999).
RN   [9]
RP   IDENTIFICATION IN THE LSM1-LSM7 COMPLEX, ASSOCIATION OF THE LSM1-LSM7
RP   COMPLEX WITH PAT1 AND XRN1, FUNCTION OF THE LSM1-LSM7 COMPLEX,
RP   IDENTIFICATION IN THE LSM2-LSM8 COMPLEX, ASSOCIATION OF THE LSM2-LSM8
RP   COMPLEX WITH U6 SNRNA, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10747033; DOI=10.1093/emboj/19.7.1661;
RA   Bouveret E., Rigaut G., Shevchenko A., Wilm M., Seraphin B.;
RT   "A Sm-like protein complex that participates in mRNA degradation.";
RL   EMBO J. 19:1661-1671(2000).
RN   [10]
RP   FUNCTION OF THE LSM1-LSM7 COMPLEX.
RX   PubMed=10761922; DOI=10.1038/35006676;
RA   Tharun S., He W., Mayes A.E., Lennertz P., Beggs J.D., Parker R.;
RT   "Yeast Sm-like proteins function in mRNA decapping and decay.";
RL   Nature 404:515-518(2000).
RN   [11]
RP   FUNCTION IN PROCESSING OF PRE-TRNAS.
RX   PubMed=12077351; DOI=10.1128/mcb.22.14.5248-5256.2002;
RA   Kufel J., Allmang C., Verdone L., Beggs J.D., Tollervey D.;
RT   "Lsm proteins are required for normal processing of pre-tRNAs and their
RT   efficient association with La-homologous protein Lhp1p.";
RL   Mol. Cell. Biol. 22:5248-5256(2002).
RN   [12]
RP   FUNCTION IN PROCESSING OF PRE-RRNAS.
RX   PubMed=12438310; DOI=10.1074/jbc.m208856200;
RA   Kufel J., Allmang C., Petfalski E., Beggs J.D., Tollervey D.;
RT   "Lsm Proteins are required for normal processing and stability of ribosomal
RT   RNAs.";
RL   J. Biol. Chem. 278:2147-2156(2003).
RN   [13]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [14]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [15]
RP   FUNCTION OF THE LSM2-LSM8 COMPLEX IN NUCLEAR MRNA DEGRADATION.
RX   PubMed=15485930; DOI=10.1128/mcb.24.21.9646-9657.2004;
RA   Kufel J., Bousquet-Antonelli C., Beggs J.D., Tollervey D.;
RT   "Nuclear pre-mRNA decapping and 5' degradation in yeast require the Lsm2-8p
RT   complex.";
RL   Mol. Cell. Biol. 24:9646-9657(2004).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), AND SUBUNIT.
RX   PubMed=18329667; DOI=10.1016/j.jmb.2008.01.007;
RA   Naidoo N., Harrop S.J., Sobti M., Haynes P.A., Szymczyna B.R.,
RA   Williamson J.R., Curmi P.M., Mabbutt B.C.;
RT   "Crystal structure of Lsm3 octamer from Saccharomyces cerevisiae:
RT   implications for Lsm ring organisation and recruitment.";
RL   J. Mol. Biol. 377:1357-1371(2008).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF LSM1-LSM7 COMPLEX, SUBUNIT, AND
RP   INTERACTION WITH PAT1.
RX   PubMed=24139796; DOI=10.1016/j.celrep.2013.10.004;
RA   Sharif H., Conti E.;
RT   "Architecture of the Lsm1-7-Pat1 complex: a conserved assembly in
RT   eukaryotic mRNA turnover.";
RL   Cell Rep. 5:283-291(2013).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF LSM1-LSM7 COMPLEX, SUBUNIT,
RP   FUNCTION, RNA-BINDING, AND MUTAGENESIS OF ARG-69.
RX   PubMed=24513854; DOI=10.1038/cr.2014.18;
RA   Zhou L., Zhou Y., Hang J., Wan R., Lu G., Yan C., Shi Y.;
RT   "Crystal structure and biochemical analysis of the heptameric Lsm1-7
RT   complex.";
RL   Cell Res. 24:497-500(2014).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS), SUBUNIT, INTERACTION WITH PAT1,
RP   FUNCTION, AND RNA-BINDING.
RX   PubMed=24247251; DOI=10.1038/cr.2013.152;
RA   Wu D., Muhlrad D., Bowler M.W., Jiang S., Liu Z., Parker R., Song H.;
RT   "Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for
RT   decapping activation.";
RL   Cell Res. 24:233-246(2014).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF LSM2-LSM8 COMPLEX, SUBUNIT,
RP   FUNCTION, RNA-BINDING, AND MUTAGENESIS OF HIS-36; ASN-38 AND ARG-69.
RX   PubMed=24240276; DOI=10.1038/nature12803;
RA   Zhou L., Hang J., Zhou Y., Wan R., Lu G., Yin P., Yan C., Shi Y.;
RT   "Crystal structures of the Lsm complex bound to the 3' end sequence of U6
RT   small nuclear RNA.";
RL   Nature 506:116-120(2014).
CC   -!- FUNCTION: Component of LSm protein complexes, which are involved in RNA
CC       processing and may function in a chaperone-like manner. Component of
CC       the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation
CC       by activating the decapping step. Component of the nuclear LSM2-LSM8
CC       complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8
CC       associates with multiple snRNP complexes containing the U6 snRNA (U4/U6
CC       snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6
CC       snRNA and plays a role in the biogenesis and stability of the U6 snRNP
CC       and U4/U6 snRNP complexes. It probably also is involved in degradation
CC       of nuclear pre-mRNA by targeting them for decapping. LSM3 binds
CC       specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably
CC       is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM3,
CC       probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8,
CC       associates with the precursor of the RNA component of RNase P (pre-P
CC       RNA) and may be involved in maturing pre-P RNA. LSM3 is required for
CC       processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
CC       {ECO:0000269|PubMed:10747033, ECO:0000269|PubMed:10761922,
CC       ECO:0000269|PubMed:12077351, ECO:0000269|PubMed:12438310,
CC       ECO:0000269|PubMed:15485930, ECO:0000269|PubMed:24240276,
CC       ECO:0000269|PubMed:24247251, ECO:0000269|PubMed:24513854,
CC       ECO:0000269|PubMed:7744014}.
CC   -!- SUBUNIT: Component of the heptameric LSM1-LSM7 complex that forms a
CC       seven-membered ring structure with a doughnut shape. The LSm subunits
CC       are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4.
CC       Except for LSM1, where a C-terminal helix crosses the ring structure to
CC       form additional interactions with LSM3 and LSM6, each subunit interacts
CC       only with its two neighboring subunits. The LSM1-LSM7 complex interacts
CC       with PAT1; within the complex PAT1 has direct interactions with LSM2
CC       and LSM3. Component of the heptameric LSM2-LSM8 complex that forms a
CC       seven-membered ring structure with a doughnut shape; an RNA strand can
CC       pass through the hole in the center of the ring structure. The LSm
CC       subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7
CC       and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. A complex comprising
CC       LSM2-LSM7 without LSM1 or LSM8 may exist. Likewise, LSM2 and LSM3 can
CC       assemble into a doughnut structure that binds PAT1 (in vitro). Besides,
CC       LSM3 can form a homooctameric ring (in vitro). Component of the U4/U6-
CC       U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least
CC       PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66,
CC       SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4,
CC       LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1. {ECO:0000269|PubMed:10369684,
CC       ECO:0000269|PubMed:10449419, ECO:0000269|PubMed:10747033,
CC       ECO:0000269|PubMed:18329667, ECO:0000269|PubMed:24139796,
CC       ECO:0000269|PubMed:24240276, ECO:0000269|PubMed:24247251,
CC       ECO:0000269|PubMed:24513854}.
CC   -!- INTERACTION:
CC       P57743; P47017: LSM1; NbExp=4; IntAct=EBI-10227, EBI-174;
CC       P57743; P38203: LSM2; NbExp=7; IntAct=EBI-10227, EBI-180;
CC       P57743; P40070: LSM4; NbExp=3; IntAct=EBI-10227, EBI-188;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 7060 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR   EMBL; Z30582; CAA83056.1; -; Genomic_DNA.
DR   EMBL; X06790; CAA29948.1; -; Genomic_DNA.
DR   EMBL; U21094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006945; DAA09739.1; -; Genomic_DNA.
DR   PIR; S78568; S78568.
DR   RefSeq; NP_013543.3; NM_001184308.3.
DR   PDB; 3BW1; X-ray; 2.50 A; A/B=1-89.
DR   PDB; 3JCM; EM; 3.80 A; d=1-89.
DR   PDB; 4C8Q; X-ray; 3.70 A; C=1-89.
DR   PDB; 4C92; X-ray; 2.30 A; C=1-89.
DR   PDB; 4M75; X-ray; 2.95 A; C/J=1-89.
DR   PDB; 4M77; X-ray; 3.11 A; C/J=1-89.
DR   PDB; 4M78; X-ray; 2.79 A; C/J=1-89.
DR   PDB; 4M7A; X-ray; 2.78 A; C/J=1-89.
DR   PDB; 4M7D; X-ray; 2.60 A; C/J=1-89.
DR   PDB; 4N0A; X-ray; 3.15 A; A/B/E/F=1-89.
DR   PDB; 5GAN; EM; 3.60 A; 3=1-89.
DR   PDB; 5NRL; EM; 7.20 A; 3=1-89.
DR   PDB; 5VSU; X-ray; 3.10 A; C=1-89.
DR   PDB; 5ZWM; EM; 3.40 A; r=1-89.
DR   PDB; 5ZWO; EM; 3.90 A; r=1-89.
DR   PDB; 6ASO; X-ray; 2.71 A; C=1-89.
DR   PDBsum; 3BW1; -.
DR   PDBsum; 3JCM; -.
DR   PDBsum; 4C8Q; -.
DR   PDBsum; 4C92; -.
DR   PDBsum; 4M75; -.
DR   PDBsum; 4M77; -.
DR   PDBsum; 4M78; -.
DR   PDBsum; 4M7A; -.
DR   PDBsum; 4M7D; -.
DR   PDBsum; 4N0A; -.
DR   PDBsum; 5GAN; -.
DR   PDBsum; 5NRL; -.
DR   PDBsum; 5VSU; -.
DR   PDBsum; 5ZWM; -.
DR   PDBsum; 5ZWO; -.
DR   PDBsum; 6ASO; -.
DR   AlphaFoldDB; P57743; -.
DR   EMDB; EMD-3683; -.
DR   EMDB; EMD-6972; -.
DR   EMDB; EMD-6974; -.
DR   EMDB; EMD-8012; -.
DR   SMR; P57743; -.
DR   BioGRID; 31697; 400.
DR   ComplexPortal; CPX-112; LSM1-7-PAT1 complex.
DR   ComplexPortal; CPX-24; U6 small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-32; U4/U6 small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-44; LSM2-8 complex.
DR   ComplexPortal; CPX-45; LSM1-7 complex.
DR   ComplexPortal; CPX-46; LSM2-7 complex.
DR   DIP; DIP-2587N; -.
DR   IntAct; P57743; 59.
DR   MINT; P57743; -.
DR   STRING; 4932.YLR438C-A; -.
DR   MaxQB; P57743; -.
DR   PaxDb; 4932-YLR438C-A; -.
DR   PeptideAtlas; P57743; -.
DR   EnsemblFungi; YLR438C-A_mRNA; YLR438C-A; YLR438C-A.
DR   GeneID; 851159; -.
DR   KEGG; sce:YLR438C-A; -.
DR   AGR; SGD:S000006434; -.
DR   SGD; S000006434; LSM3.
DR   VEuPathDB; FungiDB:YLR438C-A; -.
DR   eggNOG; KOG3460; Eukaryota.
DR   HOGENOM; CLU_076902_5_1_1; -.
DR   InParanoid; P57743; -.
DR   OMA; QAFDSHC; -.
DR   OrthoDB; 5485754at2759; -.
DR   BioCyc; YEAST:G3O-32519-MONOMER; -.
DR   Reactome; R-SCE-430039; mRNA decay by 5' to 3' exoribonuclease.
DR   BioGRID-ORCS; 851159; 6 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P57743; -.
DR   PRO; PR:P57743; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P57743; Protein.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:1990726; C:Lsm1-7-Pat1 complex; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR   GO; GO:0000932; C:P-body; IDA:ComplexPortal.
DR   GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IPI:SGD.
DR   GO; GO:0005681; C:spliceosomal complex; NAS:ComplexPortal.
DR   GO; GO:0071001; C:U4/U6 snRNP; NAS:ComplexPortal.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR   GO; GO:0005688; C:U6 snRNP; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP:ComplexPortal.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR   GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IMP:ComplexPortal.
DR   GO; GO:0008033; P:tRNA processing; IMP:ComplexPortal.
DR   CDD; cd01730; LSm3; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR034105; Lsm3.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR040002; Sm-like_LSM3.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   PANTHER; PTHR13110; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM3; 1.
DR   PANTHER; PTHR13110:SF0; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM3; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS52002; SM; 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..89
FT                   /note="U6 snRNA-associated Sm-like protein LSm3"
FT                   /id="PRO_0000125563"
FT   DOMAIN          3..82
FT                   /note="Sm"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
FT   MUTAGEN         36
FT                   /note="H->A: Strongly reduces affinity for poly-URNA ends."
FT                   /evidence="ECO:0000269|PubMed:24240276"
FT   MUTAGEN         38
FT                   /note="N->A: Strongly reduces affinity for poly-URNA ends."
FT                   /evidence="ECO:0000269|PubMed:24240276"
FT   MUTAGEN         69
FT                   /note="R->A: Strongly reduces affinity for poly-URNA ends."
FT                   /evidence="ECO:0000269|PubMed:24240276,
FT                   ECO:0000269|PubMed:24513854"
FT   HELIX           4..9
FT                   /evidence="ECO:0007829|PDB:4C92"
FT   TURN            10..13
FT                   /evidence="ECO:0007829|PDB:4C92"
FT   STRAND          14..20
FT                   /evidence="ECO:0007829|PDB:4C92"
FT   TURN            21..23
FT                   /evidence="ECO:0007829|PDB:4C92"
FT   STRAND          24..33
FT                   /evidence="ECO:0007829|PDB:4C92"
FT   STRAND          39..52
FT                   /evidence="ECO:0007829|PDB:4C92"
FT   STRAND          55..68
FT                   /evidence="ECO:0007829|PDB:4C92"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:4C92"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:4C92"
SQ   SEQUENCE   89 AA;  10030 MW;  787084EF6A5945B7 CRC64;
     METPLDLLKL NLDERVYIKL RGARTLVGTL QAFDSHCNIV LSDAVETIYQ LNNEELSESE
     RRCEMVFIRG DTVTLISTPS EDDDGAVEI
//