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
//