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Database: UniProt
Entry: M7TNT5_BOTF1
LinkDB: M7TNT5_BOTF1
Original site: M7TNT5_BOTF1 
ID   M7TNT5_BOTF1            Unreviewed;        98 AA.
AC   M7TNT5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   28-JUN-2023, entry version 26.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm3 {ECO:0000256|RuleBase:RU365046};
GN   Name=LSM3 {ECO:0000256|RuleBase:RU365046};
GN   ORFNames=BcDW1_6191 {ECO:0000313|EMBL:EMR85196.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85196.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
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; KB707917; EMR85196.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7TNT5; -.
DR   STRING; 1290391.M7TNT5; -.
DR   HOGENOM; CLU_076902_5_0_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
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:0005688; C:U6 snRNP; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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   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          13..98
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|PROSITE:PS52002"
SQ   SEQUENCE   98 AA;  10878 MW;  DE8B592B1B530769 CRC64;
     MADIDDGTSA PAEPLDLVRL CLDEVVYVKL RGDRELKGRL HAYDSHCNLV LGDVVETIYV
     VEESEDDDGE EIVKTVVKKS EMLFVRGDSV ILISPRSS
//
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