ID A0A125PI18_9BASI Unreviewed; 86 AA.
AC A0A125PI18;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm8 {ECO:0000256|RuleBase:RU365048};
DE Flags: Fragment;
GN Name=LSM8 {ECO:0000256|RuleBase:RU365048};
GN ORFNames=RHOSPDRAFT_20091 {ECO:0000313|EMBL:KWU43084.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU43084.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU43084.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU43084.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-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; KQ954495; KWU43084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A125PI18; -.
DR STRING; 1305733.A0A125PI18; -.
DR OrthoDB; 2032558at2759; -.
DR Proteomes; UP000062823; 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:UP000062823};
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..66
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KWU43084.1"
SQ SEQUENCE 86 AA; 9392 MW; 02ECB4299D7BD7AA CRC64;
EKVLVVTQDG RVIVGKLMGF DQTTNIILAD SIERIFSPDE PVIEEPLGVE IVRGDNITLI
GGLDEEADKE IDLSTIRAHP LADVTH
//
