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Database: UniProt
Entry: A0A0D9P7G8_METAN
LinkDB: A0A0D9P7G8_METAN
Original site: A0A0D9P7G8_METAN 
ID   A0A0D9P7G8_METAN        Unreviewed;        80 AA.
AC   A0A0D9P7G8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm5 {ECO:0000256|RuleBase:RU365055};
GN   Name=LSM5 {ECO:0000256|RuleBase:RU365055};
GN   ORFNames=H634G_03919 {ECO:0000313|EMBL:KJK80770.1};
OS   Metarhizium anisopliae BRIP 53293.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK80770.1, ECO:0000313|Proteomes:UP000054544};
RN   [1] {ECO:0000313|Proteomes:UP000054544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX   PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA   Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA   Ash G.J.;
RT   "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT   comparative genomics of Metarhizium species.";
RL   BMC Genomics 15:660-660(2014).
CC   -!- FUNCTION: Plays a role in U6 snRNP assembly and function. Binds to the
CC       3' end of U6 snRNA. {ECO:0000256|RuleBase:RU365055}.
CC   -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC       {ECO:0000256|RuleBase:RU365055}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365055}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC       {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365055}.
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DR   EMBL; KE384728; KJK80770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9P7G8; -.
DR   STRING; 1291518.A0A0D9P7G8; -.
DR   Proteomes; UP000054544; Unassembled WGS sequence.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd01732; LSm5; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR033871; LSm5.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   PANTHER; PTHR20971; U6 SNRNA-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR20971:SF0; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM5; 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|RuleBase:RU365055};
KW   mRNA splicing {ECO:0000256|RuleBase:RU365055};
KW   Nucleus {ECO:0000256|RuleBase:RU365055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054544};
KW   Ribonucleoprotein {ECO:0000256|RuleBase:RU365055};
KW   RNA-binding {ECO:0000256|RuleBase:RU365055};
KW   Spliceosome {ECO:0000256|RuleBase:RU365055}.
FT   DOMAIN          6..78
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|PROSITE:PS52002"
SQ   SEQUENCE   80 AA;  8760 MW;  7B4FC759FCECACD3 CRC64;
     MASQLLPLEL IDKCVGSRIW VVMKGEKEFS GTLVGFDDYV NMVLEDVTEF DYSGTHTKLP
     KILLNGNNIC MLIPGGEGPA
//
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