ID A0A0S4J0G1_BODSA Unreviewed; 95 AA.
AC A0A0S4J0G1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm8 {ECO:0000256|RuleBase:RU365048};
GN Name=LSM8 {ECO:0000256|RuleBase:RU365048};
GN ORFNames=BSAL_79590 {ECO:0000313|EMBL:CUG44759.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG44759.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5
CC tri-snRNP complex that is involved in spliceosome assembly, and as
CC component of the precatalytic spliceosome (spliceosome B complex). The
CC heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract
CC of U6 snRNA. {ECO:0000256|RuleBase:RU365048}.
CC -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC {ECO:0000256|RuleBase:RU365048}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365048}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365048}.
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DR EMBL; CYKH01000814; CUG44759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4J0G1; -.
DR VEuPathDB; TriTrypDB:BSAL_79590; -.
DR OMA; KDWRGRD; -.
DR OrthoDB; 123671at2759; -.
DR Proteomes; UP000051952; 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; cd01727; LSm8; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR034103; Lsm8.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR044642; PTHR15588.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR15588; LSM1; 1.
DR PANTHER; PTHR15588:SF9; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM8; 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:RU365048};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU365048};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365048};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365048};
KW RNA-binding {ECO:0000256|RuleBase:RU365048};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|RuleBase:RU365048}.
FT DOMAIN 1..75
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 95 AA; 10370 MW; E364C24641E1BB8E CRC64;
MSMAAEYLKK RVSVITADGR HYLGTLESCD QVLNVVLSSC VERIHSVEVG AEDMPLGVFL
IRGSRIVCIG AVDTFEEATI DVRNLRGPPL PRVVV
//