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Database: UniProt
Entry: D5GLD6_TUBMM
LinkDB: D5GLD6_TUBMM
Original site: D5GLD6_TUBMM 
ID   D5GLD6_TUBMM            Unreviewed;        95 AA.
AC   D5GLD6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-NOV-2023, entry version 53.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm3 {ECO:0000256|RuleBase:RU365046};
GN   Name=LSM3 {ECO:0000256|RuleBase:RU365046};
GN   ORFNames=GSTUM_00010142001 {ECO:0000313|EMBL:CAZ85329.1};
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ85329.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ85329.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ85329.1,
RC   ECO:0000313|Proteomes:UP000006911};
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA   Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA   Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA   Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA   Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA   Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA   Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA   Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA   Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA   Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT   of symbiosis.";
RL   Nature 464:1033-1038(2010).
CC   -!- FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
CC       {ECO:0000256|RuleBase:RU365046}.
CC   -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC       {ECO:0000256|RuleBase:RU365046}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365046}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC       {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365046}.
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DR   EMBL; FN430348; CAZ85329.1; -; Genomic_DNA.
DR   RefSeq; XP_002841138.1; XM_002841092.1.
DR   AlphaFoldDB; D5GLD6; -.
DR   STRING; 656061.D5GLD6; -.
DR   EnsemblFungi; CAZ85329; CAZ85329; GSTUM_00010142001.
DR   GeneID; 9186073; -.
DR   KEGG; tml:GSTUM_00010142001; -.
DR   eggNOG; KOG3460; Eukaryota.
DR   HOGENOM; CLU_076902_5_1_1; -.
DR   InParanoid; D5GLD6; -.
DR   OMA; QAFDSHC; -.
DR   OrthoDB; 5485754at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0140445; C:chromosome, telomeric repeat region; IEA:EnsemblFungi.
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:UniProtKB-UniRule.
DR   GO; GO:0005682; C:U5 snRNP; IEA:EnsemblFungi.
DR   GO; GO:0005688; C:U6 snRNP; IEA:UniProtKB-UniRule.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0008266; F:poly(U) RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0070034; F:telomerase RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0030620; F:U2 snRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:EnsemblFungi.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW   ECO:0000256|RuleBase:RU365046};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW   ECO:0000256|RuleBase:RU365046};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365046};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|RuleBase:RU365046};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365046};
KW   Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|RuleBase:RU365046}.
FT   DOMAIN          12..95
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|PROSITE:PS52002"
SQ   SEQUENCE   95 AA;  10679 MW;  BC40AA5B591A9268 CRC64;
     MSDADDTSPI QEPLDLVRLS LDEQVFVKLR GDRELRGRLH AYDSHCNLVL GDVEETIYTV
     GDDEEDDSVK TIKKQSEMLF VRGDSVVLIS PQAQS
//
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