ID A0A0P9EK94_RHOGW Unreviewed; 84 AA.
AC A0A0P9EK94;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm5 {ECO:0000256|RuleBase:RU365055};
GN Name=LSM5 {ECO:0000256|RuleBase:RU365055};
GN ORFNames=RHOBADRAFT_38011 {ECO:0000313|EMBL:KPV74122.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV74122.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV74122.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV74122.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
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; KQ474081; KPV74122.1; -; Genomic_DNA.
DR RefSeq; XP_018270171.1; XM_018413483.1.
DR AlphaFoldDB; A0A0P9EK94; -.
DR STRING; 578459.A0A0P9EK94; -.
DR GeneID; 28973932; -.
DR OMA; NNICTLI; -.
DR OrthoDB; 275126at2759; -.
DR Proteomes; UP000053890; 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:UP000053890};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365055};
KW RNA-binding {ECO:0000256|RuleBase:RU365055};
KW Spliceosome {ECO:0000256|RuleBase:RU365055}.
FT DOMAIN 5..80
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 84 AA; 9303 MW; 7705AF98AEDB5496 CRC64;
MSTILPLELV DRATGSQVWV IMKTEREFTG TLVGFDDYVN MVLEDVTEYE NTPQGRKTTK
LGQTLLNGNN IAMIVPGRGP EDDA
//